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  • Cell & Developmental Biology  (13,116)
  • 1995-1999  (2,509)
  • 1990-1994  (6,449)
  • 1980-1984  (2,672)
  • 1975-1979  (1,486)
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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 1 (1980) 
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 1 (1980), S. 1-15 
    ISSN: 0886-1544
    Keywords: centrosomes ; kinetochores ; microtubule initiation ; nuclease enzymes ; electron microscopy ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A lysed cell system was used to study the organelle structure and nucleation of exogenous tubulin at kinetochores and centrosomes in mitotic PtK2 cells. We have used this lysed cell system in conjunction with nuclease digestion experiments to determine which specific nucleic acids (DNA or RNA) are involved in either the structure and/or microtubule-initiating capacity of kinetochores and centrosomes. The results indicate that DNase I specifically decondenses the kinetochore plate structure, with the eventual loss in the ability of the chromosomes to nucleate microtubule assembly. DNase I had no effect on either the structure or nucleating capacity of centrosomes. Both RNase T1 and RNase A specifically attacked the amorphous pericentriolar material of the centrosomes, with a concomitant loss in the ability of this material to nucleate microtubule formation. Neither RNase appeared to affect the structure or nucleating capacity of the kinetochore. Therefore, the two types of nucleases appear to exert preferential effects on the different types of microtubule initiation sites in mitotic mammalian cells. The results suggest that DNA is a major component of the kinetochore, while RNA is a major component of the amorphous pericentriolar material. These findings support the concept that microtubule initiation sites in mitotic cells contain nucleic acids which are essential for the structural and functional integrity of the sites.
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 1 (1980), S. 31-40 
    ISSN: 0886-1544
    Keywords: actin ; fascin ; actin cross-linking proteins ; fertilization ; microvilli ; sea urchin eggs ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Following fertilization, the sea urchin egg cortex undergoes a structural change involving the assembly and organization of actin filaments into microvilli. Antifascin localizes this actin cross-linking protein in the microvilli of the fertilized egg cortex but no organized staining is present in the unfertilized cortex. Determination of the actin content of eggs using the DNAase I inhibition assay indicates that actin is about 1.4% of the total protein. Approximately 90% of this actin is soluble in low calcium isotonic extracts of unfertilized eggs while only 60-65% can be recovered in identical extracts of fertilized eggs. Similar measurements for fascin using a radioimmunoassay indicate this molecule represents about 0.3% of the total egg protein, essentially all of which is recovered in low calcium isotonic extracts of unfertilized eggs. After fertilization only 65-70% of this actin cross-linking protein is in the soluble phase. These results demonstrate a markedly different solubility for actin and fascin after fertilization, when the indirect immunofluorescence staining localizes fascin in the microvilli, and are consistent with the idea that fascin organizes newly polymerized actin filaments into the microvillar cores. A consideration of the amounts of actin and fascin incorporated into the cortex after fertilization and the number of microvilli on the egg surface indicates that the measured values are sufficient to account for the observed microvillar elongation.
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 1 (1980), S. 17-29 
    ISSN: 0886-1544
    Keywords: Ca-ion ; Labyrinthula ; contraction ; glycerination ; Ca-reservoir ; cell movement ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Colonies of Labyrinthula, a colonial marine protist, expand by protrusive movements of the specialized slimeways. The movements recorded in time-lapse films are of two types - filopodial and lamellipodial - and occur at rates equivalent to those of cell translocation.Evidence is presented that Ca2+ regulates the contraction of the actomyosin system of filaments present in the slimeways of Labyrinthula. In glycerinated models or in colonies exposed to ionophore A23187 contraction is evidenced by the occurrence of periodic contractions of the slimeways, giving them the appearance of strings of beads. Glycerinated slimeways contract on the addition of Ca2+ and ATP while slimeways provided with ionophore A23187 contract on addition of Ca2+ alone. The concentration required is 1.1 × 10-7 M Ca2+ while concentrations of 6.2 × 10-8 or lower were ineffective. Rates of contraction were measured in time-lapse films which provide evidence that contractions and beading occur everywhere in the slimeway system. When beading occurs, the 6-nm filaments transform from an array of parallel single filaments into an interwoven meshwork.We have identified by pyroantimonate-OsO4 fixation, as possible Ca2+ reservoirs, deposits of Ca2+ in bothrosomes - structures through which cell secretions pass into the slimeways. The electron-dense deposits are located at the base of the bothrosome and disappear after incubation with EGTA. We propose that the translocation of cells as well as the movements of slimeways may be regulated by the cells through the local measured liberation of Ca2+ from the bothrosome where it is sequestered.
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 1 (1980), S. 41-61 
    ISSN: 0886-1544
    Keywords: mitosis ; mitotic spindle ; kinetochore ; microtubule ; micronucleus ; Tetrahymena ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Mitotic micronuclei were isolated from Tetrahymena thermophila and data on spindle ultrastructure were obtained from serial, transverse sections. Comparison of data from nuclei at meta- and early anaphase with data from nuclei at late anaphase showed that during anaphase, sister kinetochores move from the equator to the spindle poles, but kinetochore translocation occurs without any apparent change in either the number or length of kinetochore microtubules. This unprecedented result is ascribed significance with regard to the mechanism of kinetochore transport since there are only a limited number of ways that result could be achieved. The organization of the peripheral sheath changes during anaphase as evidenced by gaps in the sheath at late anaphase. Numerous kinetochore and non-kinetochore microtubules are located in polar regions of the spindle at late anaphase, whereas those regions contained only peripherally arranged microtubules at earlier stages. Tracking of individual kinetochore microtubules in late anaphase nuclei showed that some of them appeared to become incorporated into the peripheral sheath near the pole. At early and late anaphase, crossbridges connect adjacent microtubules throughout the spindle poleward to the kinetochores, as well as in the interzone.
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  • 6
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 1 (1980), S. 63-71 
    ISSN: 0886-1544
    Keywords: Physarum polycephalum ; myosin light chains ; polyacrylamide gel electrophoresis ; calcium ; cytoplasmic streaming ; actomyosin ATPase regulation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Myosin from the slime mold Physarum polycephalum contains three sizes of polypeptides: a heavy chain and two light chains, LC-1 and LC-2. Using a simple qualitative test for calcium binding by comparing electrophoretic migration of the polypeptides in sodium dodecy1 sulfate (SDS) acrylamide gels in the presence and absence of calcium, we have found that Physarum myosin light chain LC-2 migrates with an apparent molecular weight of 16,900 daltons in the presence of the metal ion chelator ethylene glycol bis (B-aminoethyl ether) N,N′-tetraacetic acid (EGTA). However, if calcium chloride is added to the sample prior to electrophoresis, the apparent molecular weight decreases to 16,100. Lanthanide and cadmium ions, but not magnesium, can substitute for calcium. Because the ionic radii of Ca2+, La3+, and Cd2+ are almost identical, we conclude that Physarum myosin LC-2 possesses a very size-specific binding site for calcium. Physarum myosin LC-1 and the heavy chain give no evidence for binding calcium by this test. Since cytoplasmic streaming in the plasmodium of Physarum requires calcium, our evidence indicates that the calcium-binding property of Physarum myosin LC-2 may be important in regulating the production of force by actomyosin in the ectoplasm. Unexpectedly, the myosin light chain in Physarum capable of binding calcium, LC-2, is the essential light chain, while LC-1 is a member of the regulatory class of myosin light chains [V. T. Nachmias, personal communication]. Until now, essential myosin light chains have not been shown to have high affinity divalent cation binding sites. This means a new version of the myosin-based model for actomyosin regulation by calcium may be required to explain cytoplasmic movement in Physarum, and perhaps in other motile systems involving cytoplasmic myosins as well.
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  • 7
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 2 (1982), S. 273-285 
    ISSN: 0886-1544
    Keywords: actin gelation ; F-actin nucleation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A new actin binding protein has been purified to homogeneity from amoebae of Dictyostelium discoideum. This protein is a single polypeptide with a molecular weight of 120,000 upon sodium dodecyl sulfate gel electrophoresis. It is soluble and trypsin-sensitive, contains no carbohydrate, increases the viscosity and sedimentation rate of F actin, and inhibits the actin-stimulated Mg ATPase of rabbit muscle heavy meromyosin. The interaction of 120,000-dalton protein with F actin is not inhibited by millimolar ATP, pyrophosphate, or micromolar calcium. The 120,000-dalton actin binding protein increases the initial rate of actin polymerization and decreases the critical concentration of actin at steady state.These properties demonstrate that 120,000-dalton protein from Dictyostelium discoidum is not a myosinlike protein. Rather, this protein is probably involved in regulating the assembly of the actin cytoskeletion.
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  • 8
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 2 (1982), S. 287-308 
    ISSN: 0886-1544
    Keywords: actin-binding protein ; Dictyostelium ; cytoskeleton ; amoeboid movement ; calcium ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A protein from Dictyostelium discoideum with an apparent subunit molecular weight of 95,000 daltons (95K protein) was previously identified as an actin-binding protein ‘Hellewell and Taylor, 1979’. In this paper, we present a method for purifying the protein, and characterize some important aspects of its structure and function. Purification of the 95K protein is achieved by fractionation with ammonium sulfate followed by chromatography on DEAE-cellulose, gel filtration on 6% agarose, and final purification on hydroxyapatite. The 95K protein is a dimer, composed of apparently identical subunits. It is a rod-shaped molecule, 38 nm in length, with a Stokes radius of 74 Å. In these structural properties, the 95K protein is similar to muscle and nonmuscle α-actinins. The 95K protein and filamin are equally competent, when compared on a weight basis, to enhance the apparent viscosity of actin as determined by falling ball viscometry. The apparent viscosity of mixtures of the 95K protein and actin is dramatically reduced at pH greater than 7.0 or free ‘Ca2+’ greater than 10-7 M. We also examine the mechanism by which calcium regulates the interaction of the 95K protein and actin. A change in free ‘Ca2+’ induces no detectable change in the quaternary structure of the 95K protein. Our experiments indicate that the 95K protein does not dramatically alter the length distribution of actin filaments in the presence of micromolar free ‘Ca2+’. A large fraction of the 95K protein cosediments with actin in the presence of low free ‘Ca2+’ (ca. 3 × 10-8M), but not in the presence of high free ‘Ca2+’ (ca. 4 × 10-6M). We conclude that increased free ‘Ca2+’ inhibits gelation of actin by the 95K protein by reducing the affinity of the 95K protein for actin. We propose that 95K protein is an important component of the cytoskeletal/contractile system in D. discoideum amoebae.
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  • 9
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 2 (1982), S. 317-332 
    ISSN: 0886-1544
    Keywords: cytoskeleton ; platelets ; actin-binding protein ; actin ; myosin ; thrombin activation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: When human blood platelets were immersed in an ice-cold solution containing 1% Triton ×-1200, 40 mM KCl, 10 mM EGTA, 10 mM imidazole-HCl, and 2 mM NaN3 pH 7.0, a flocculent precipitate appeared immediately in the tube. This precipitate was collected at 3,000g and SDS-polyacrylamide gel analysis showed it to consist mainly of actin, α-actinin, actin-binding protein (ABP), and varying amounts of myosin.Any modifications of this solution used to isolate the platelets' Triton-insoluble cytoskeleton caused profound changes in the nature of the cytoskeleton isolated. Increasing the KCl concentration resulted in a lower yield of cytoskeletal actin and ABP. Inclusion of EDTA in the solution resulted in an increased amount of myosin associated with the cytoskeleton, whereas including MgATP decreased the myosin yield.Experiments with the purified proteins showed that ABP and myosin can each protect the actin from depolymerizing when dialyzed into the Triton solubilization solution. In addition, it was found that when platelets were stimulated with thrombin for 2 min prior to the addition of the Triton solution, 3-4 times more myosin was associated with the cytoskeletal precipitate.The results suggest, therefore, that any variations in solution conditions used for isolating the cytoskeleton from resting platelets, which results in alterations in the amount of ABP, may have profound effects on the state of actin polymerization. Likewise, in thrombin-activated platelets, it is suggested that the increased association of myosin with the cytoskeleton results in a greater stabilization of the F-actin associated with the cytoskeleton. These factors must be considered when interpreting the results regarding the nature of actin transformations in the resting and activated platelet.
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  • 10
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 2 (1982) 
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
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  • 11
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 2 (1982), S. 369-383 
    ISSN: 0886-1544
    Keywords: motility ; flagella ; cilia ; microtubules ; Gregarines ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The male gametes of the parasitic protozoan, Lecudina tuzetae, have a motile flagellum with a “6 + O” ultrastructure ‘Schrével and Besse, 1975’. These gametes were isolated from the cysts in which they develop and were observed and photographed under a variety of conditions. The flagella beat continuously, without stopping and starting, with a beat period of about 2 sec. They can beat in solutions whose viscosities are greater than 0.5 Nsm-2 (l Nsm-2 = 103 cP). The waveform can be approximated by a series of helical arcs and interconnecting straight regions that travel from the base to the tip. The helical regions have a radius of curvature of 3.2 μm and subtend a final angle of 1.7 radians. The straight portions are 2.0 μm in length. There are two sets of opposing bends, but they do not originate in the same plane. The resulting waveform is an approximately helical coil, with a pitch of 9.8 μm, a pitch angle of 0.6 radian and a peak-to-peak amplitude of 2.3 μm. The sense of the coil is left handed. The axoneme twists during beating. The main differences between the movement of this flagellum and that of typical 9 + 2 flagella are a low beat frequency and three-dimensional bends that produce relatively little forward movement of the cell. Twisting is discussed as a means of discriminating between some types of models of flagellar motility.
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  • 12
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 2 (1982), S. 393-403 
    ISSN: 0886-1544
    Keywords: motility ; Ca2+ ; ionophores ; spirulina subsalsa ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Motility of the marine filamentous cyanobacterium Spirulina subsalsa is both Ca2+ and Na+ dependent, and replacement of Na+ by mannitol arrests it. The data presented suggest that Ca2+ interacts with sites on the surface of the cell membrane. The inhibitory effect of dicyclohexylcarbodiimide (DCCD) hints at the possibility that the role of Ca2+ may be associated with a membrane bound Ca-ATPase. Motility is pH dependent, being nil at pH 〈 6.5 and 〉 10.0, with an optimum at 8.5. Norepinephrine abolishes most of the inhibitory effect of low pH on motility. Ca2+ has an “all-or-none” effect on motility that is triggered at 5 mM. Acetylcholine lowers the threshold of Ca2+ necessary for triggering motility.
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  • 13
    Electronic Resource
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    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 2 (1982), S. 445-455 
    ISSN: 0886-1544
    Keywords: clot structure ; platelet contractility ; protein networks ; rheological techniques ; viscoelasticity ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: When citrated plasma is recalcified, it forms a viscoelastic gel-a clot. The relationship between platelet contractility and clot rigidity was studied by using a rheological technique which simultaneously measured both the dynamic rigidity modulus and the contractile force during gel formation with platelet rich plasma (PRP). Protein network formation in a clot was accompanied by a contractile force throughout the clotting process. PRP demonstrated a maximum elastic modulus of 6,000 dynes/cm2 and a maximum contractile force/area of 1,500 dynes/cm2. The values of these parameters for a platelet-free clot (PFP) were 700 dynes/cm2 and less than 100 dynes/cm2 respectively. Sonicated control PRP and PRP from a Glanzmann thrombasthenia patient both clotted in a manner similar to PFP. Metabolic inhibitors, 2-deoxy-D-glucose and KCN (5 mM each), retarded the clotting curves of PRP. Cytochalasin B and E suppressed both structural rigidity and force generation in a concentration-dependent manner similar to their inhibitory effect on actin polymerization in platelets. Colchicine (2.5 mM) or vinblastine (0.11 mM) did not affect these clotting curves. Thrombi-activated, fixed platelets did not generate any force, nor did they significantly increase clot rigidity. Streptokinase induced a concurrent decrease of both rigidity and force in PRP clots. The elastic modulus of a PFP clot could be increased to 2,500 dynes/cm2 by externally straining the network with an axial force/area of 1,500 dynes/cm2. Our results indicate that clot structure formation in PRP is strongly coupled to the contractile force generated by the platelet microfilament system and that this force modulates clot rigidity.
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  • 14
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 2 (1982), S. 457-470 
    ISSN: 0886-1544
    Keywords: fragmin ; critical actin concentration ; nucleation ; filament growth ; pointed end ; barbed end ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: As reported previously, fragmin isolated form Physarum plasmodia restricts the polymerization of actin to produce short F-actin filaments in the presence of Ca2+ ions. Here it is shown that when actin is polymerized at low concentrations of salts, fragmin increases the critical concentration of actin for polymerization. This effect of fragmin on the critical concentration is independent of the molar ratio of fragmin to actin. The addition of actin monomers onto heavy meromyosin-decorated F-actin fragments treated with fragmin occurs unidirectionally at the pointed end of each fragment. These results suggest that fragmin binds to the barbed ends of F-actin filaments and inhibits association and dissociation of actin monomers at this end. Fragmin accelerates the initial stage of polymerization of actin. When a constant amount of G-actin is polymerized in the presence of small amounts of fragmin, the inverse of the half-polymerization time increases in proportion to the square root of the amount of fragmin added. This means that fragmin acts as a potent promoter of the nucleation step in actin polymerization. Both functions of fragmin-promotion of nucleation and capping at the barbed end of F-actin-require micromolar concentrations of Ca2+.
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  • 15
    Electronic Resource
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    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 2 (1982), S. 471-482 
    ISSN: 0886-1544
    Keywords: calmodulin ; myosin ; antibody ; immunofluorescence ; amoeba ; Dictyostelium ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A rabbit antiserum was raised against calmodulin from the eukaryotic microorganism Dictyostelium discoideum. In double immunodiffusion experiments, the antiserum formed an immunoprecipitation line with Dictyostelium calmodulin but not bovine brain calmodulin; competition radioimmunoassays showed no cross reactivity between the antiserum and calmodulins from bovine brain and spinach. The calmodulin content of vegetative Dictyostelium amoebae, determined by competition radioimmunoassay, was 0.5 μg/mg protein; similar levels were found in developing cells. The antiserum was used to visualize the distribution of calmodulin in Dictyostelium amoebae by indirect immunofluorescence. Cells were examined under various conditions: in suspension, attached to a substrate, and while phagocytosing yeast cells. In all cases, anticalmodulin staining was concentrated in the cell cortex. Parallel experiments using a monoclonal antibody against Dictyostelium myosin showed that this protein is also enriched in the cortical region of the cell.
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  • 16
    Electronic Resource
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    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 2 (1982), S. 355-367 
    ISSN: 0886-1544
    Keywords: proacrosome migration ; nuclear pore redistribution ; nuclear membrane fluidity ; electron microscopy ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Electron microscopic examination of thin sections and freeze fractures of Locusta spermatids revealed that the proacrosome docks to the nuclear membrane and glides around the nucleus during sperm development. Whereas nuclear pore complexes occur in groups distributed at random over the entire nucleus of the early spermatid, they are found only in a narrow ring closely surrounding the centriolar adjunct in later spermatids. The pores appear to be swept caudally in the nuclear envelope, perhaps by a process like capping; they are not merely excluded by structures adhering to the nucleus. The observations suggest that both proacrosome migration and the deployment of pores are facilitated by the inherent fluidity of the nuclear membranes.
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  • 17
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    Cell Motility and the Cytoskeleton 2 (1982), S. 343-354 
    ISSN: 0886-1544
    Keywords: NBD-phallacidin ; actin ; ocular tissues ; wound repair ; stress fibers ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The fluorescent derivative of the actin-binding toxin phallacidin, 7-nitrobenz-2-oxa-1,3 diazole phallacidin, has been used to cytologically demonstrate the presence of actin in lens epithelium, corneal endothelium, and retinal pigment epithelium. In these noninjured tissues, no stress fibers are observed and fluorescence is confined mainly to an area at or near the cell membrane, although some diffuse cytoplasmic staining can also be seen. However, following injury to either the lens epithelium or corneal endothelium of rats and frogs, stress fibers are detected, but only in those cells that migrate into the wound area. Cells on the periphery of each tissue do not partake in would repair and thus maintain their normal appearance. After the tissue has regenerated, stress fibers disappear, and those cells involved in the injury response return to their normal morphology.When rabbit corneal endothelium is placed in tissue culture, stress fibers are observed as the cells migrate away from the initial explant. Upon reaching confluency, these cells spread out and each is surrounded by thick actin-containing bands. Furthermore, they exhibit some stress cables within their cytoplasm. This is in contrast to their appearance in vivo where stress fibers are absent and fluorescence is limited to a region near the cell membrane.
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  • 18
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    Cell Motility and the Cytoskeleton 2 (1982), S. 385-391 
    ISSN: 0886-1544
    Keywords: ciliated cell ; basal body apparatus ; microtubules ; microfilaments ; respiratory epithelium ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: This is a descriptive study showing the three-dimensional interrelationship of cytoskeletal elements at the apex of ciliated cells of rat respiratory epithelium. Tissue specimens were serially thin sectioned in various planes and examined by transmission electron microscopy. Thicker sections were also cut at various angles and analyzed stereoscopically. Other specimens were cleared of soluble molecules by glycerination or Triton-X 100 treatment and sectioned as described above. It was found that C microtubules from the triplets of each basal body diverge from the A and B microtubules, run a short distance, and converge at the basal foot. These microtubules or other microtubules arising anew then dispersed deeper into the cytoplasm. The C fibers also interdigitated with other microtubules running perpendicular to them and parallel to the ciliated surface. Ten-nanometer intermediate filaments were organized in parallel sheets between adjacent basal bodies. Sixnanometer actin filaments were distributed throughout the apical cytoplasm. Neighboring basal bodies were linked to one another by microtubules and microfilaments. Basal bodies from each cell appear to be structured for stability, flexibility, and arranged to operate as a single unit.
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  • 19
    Electronic Resource
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    Cell Motility and the Cytoskeleton 2 (1982), S. 429-443 
    ISSN: 0886-1544
    Keywords: 21S dynein ; tubulin ; binding stoichiometry ; ATP sensitivity ; binding cooperativity ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The binding properties of Tetrahymena 21S dynein to doublet A and B subfiber microtubules were analyzed by both a turbidimetric assay (Δ A350 nm) and electron microscopy. KCl-extracted, sucrose-gradient, purified 21S dynein binds to each of the two kinds of axonemal microtubules in both ATP-insensitive and ATP-sensitive modes, even though only a single type of binding occurs to each of the subfibers in situ. Total dynein bound to axonemal microtubules is a composite of binding that is sensitive to dissociation by ATP and binding that is insensitive to ATP. Each exhibits a different binding profile. Total binding exhibits a sigmoid profile (h = 1.93) and saturates at 1.49 mg D/mg T. ATP-sensitive binding likewise exhibits a sigmoid profile (h = 2.66) but saturates at 1.06 mg D/mg T. Binding occurs with a similar affinity for both A and B subfibers. The Hill coefficient (h) for ATP-sensitive binding implies positive cooperativity between binding events. ATP-insensitive binding was studied independently in 20 μM ATP, 10 μM vanadate, which blocks ATP-sensitive binding. ATP-insensitive binding exhibits a hyperbolic profile (h = 1.0) and likewise occurs along each of the two kinds of axonemal tubules. Binding saturates at 0.87 mg D/mg T. The binding data suggest that the tubulin dimer has conserved both ATP-sensitive and ATP-insensitive binding sites for 21S dynein, even though the sites may not be expressed in vivo.
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  • 20
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    Cell Motility and the Cytoskeleton 2 (1982) 
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
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  • 21
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    Cell Motility and the Cytoskeleton 2 (1982), S. i 
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
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    Cell Motility and the Cytoskeleton 2 (1982), S. 573-582 
    ISSN: 0886-1544
    Keywords: Euglena flagella ; laser microsurgery ; stigma ; Mg2+ ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: When the area of the stigma of Euglena was irradiated with an infrared laser beam at a dose too low to cause permanent loss of motility, a reduction in flagellar motility was observed only when the external medium contained less than 1 mM Mg2+. At these low Mg2+ concentrations, the laser caused a decrease in flagellar frequency and a tendency for the flagellar waveform to shift towards that taken during reversed swimming. This suggests that the effect of the laser irrdiation was to deplete the cells of Mg2+. After the laser pulse the reversal response remained sensitive to the wavelength of the illuminating light. In white light (420-700 nm) 60% of the Euglena showed a reversed waveform; in orange light (530-700 nm) this increased to 90%. This shows that the photoreceptor was not destroyed by the laser irradiation.These experiments were performed on cells that had been impaled on a microelectrode. If direct electric current was passed into the laser-irradiated cells, the current necessary to cause flagellar arrest was 2 to 4 times less than that for cells not laser irradiated.It is concluded that an internal Mg2+ store is present in the Euglena, localized in the area of the paraflagellar swelling; and that the laser irradiation eliminates this Mg2+ store, but at the power used it does not destroy the ability of the stigmaparaflagella to control the flagellar activity.
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  • 23
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    Cell Motility and the Cytoskeleton 2 (1982), S. 599-614 
    ISSN: 0886-1544
    Keywords: monoclonal antibodies to tubulin ; radioimmune assay ; immunoautoradiography ; Western blots ; immunofluorescence ; tubulin heterogeneity ; eukaryotic flagellar motility ; immunomotility ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Two monoclonal antibodies reactive for α-tubulin but not for β-tubulin have been prepared, characterized in terms of their relative binding to tubulins from differnt sources by a solid-phase binding assay, immunoautoradiography, and indirect immunofluorescence, and utilized to study flagellar motility. Our results demonstrate that α-tubulins from different species, and even from different tissues of the same species, are nonidentical. Especially interesting was the observation that one of the antibodies, Ab2, immunofluorescently stained microtubules of chick embryo fibroblast cells, but was completely unreactive for microtubules of rat kangaroo (PtK2) fibroblasts; a different antibody, Ab1, stained both cell types. Results of these and additional experiments clearly show that Ab1 and Ab2 recognize discrete and different epitopes on α-tubulin.Monoclonal antitubulins Ab1 and Ab2 each inhibited the bend amplitude of reactivated sea urchin spermatozoa without affecting beat frequencies or the ability of the outer doublet microtubules to slide past each other in elastase-digested models. These results, together with those obtained previously using rabbit polyclonal antitubulin antibodies [Asai and Brokaw, 1980], demonstrate that inhibition of bend amplitude is a common property of antitubulin antibodies and is not due to the binding of antibodies to one specific site on the axoneme. Our results suggest that tubulin subunit conformational changes may occur on the outer doublet lattice and may be integrally involved in the mechanism and control of flagellar bending.
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    Cell Motility and the Cytoskeleton 2 (1982), S. 19-24 
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
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  • 25
    ISSN: 0886-1544
    Keywords: videomicroscopy ; differential interference microscopy ; streaming ; reticulopodial motility ; Allogromia ; microtubules ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A new method called Allen Video-enhanced Contrast, Differential Interference Contrast (AVEC-DIC) microscopy is shown to be sufficiently sensitive to detect several new features of microtubule-related motility in the reticulopodial network of the foraminifer, Allogromia. The method takes advantage of the variable gain and offset features of a binary video camera to operate the DIC microscope under conditions highly favorable for video imaging, but in which the optical image is virtually invisible to the eye yet retains its full information when viewed by a suitable video camera. The improvements are made possible by setting a dé Senarmont compensator to λ/9-λ/4 at maximal working aperture of internally corrected planapochromatic objectives. Under these conditions, the offset feature of the video camera can reject so much stray light from the instrument and specimen that contrast compares favorably with that observed in high-extinction images, and polarizing rectifiers offer scarcely any advantage. Freed from the constraints of the light-limited conditions of DIC microscopy, video images can be recorded 60 times per second, or over 1,000 times the rate of photomicrographs at comparable magnifications under high-extinction conditions.Application of this method to the reticulopodial network of Allogromia has shown that cytoplasmic organelles are translocated only in contact with single microtubules or bundles of microtubules, and that these organelles fail to move when separated from microtubules. Microtubules themselves undergo both axial translatory (“sliding”) and lateral “zipping and unzipping” movements that have been suggested to occur during mitosis and other biological processes.
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  • 26
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    Cell Motility and the Cytoskeleton 1 (1981), S. 329-347 
    ISSN: 0886-1544
    Keywords: actin ; microfilaments ; heavy meromyosin ; mammary gland ; secretion ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Cytochalasin B, a microfilament-altering drug, inhibits lactose synthesis in lactating guinea pig mammary gland [Biochim. Biophys. Acta 392:20, 1975] but not primarily by inhibiting glucose transport [Eur. J. Cell Biol. 20:150, 1979]. In order to study the possible role of microfilaments in lactose synthesis and secretion, we isolated both the alveolar (milk-secreting) and myoepithelial (contractile) cells from lactating mammary gland. Light microscopy shows that the alveolar cell fraction (viability approximately 71%) is homogenous and that the cells retain strong polarity of secretory structures in the apical region. Two proteins were extracted from the alveolar cell fraction. One (mol wt 42,000) comigrates with skeletal muscle actin on SDS-PAGE gels. The other, a high-molecular-weight (180,000) protein (HMWP) may be analogous to actin-binding protein or clathrin. An extract from the myoepithelial cell fraction also contains a protein that comigrates with actin but no HMWP. Whole tissue extract contains the 42K protein, and a 185K HMWP. Examination of the alveolar cell extract by electron microscopic (EM) negative staining revealed meshworks of multistranded, interconnecting filaments, with attached globular structures (100-200 A) (possibly the HMWP) and single filaments (40-60 A diameter) branching off. To localize these filamentous structures in situ, whole tissue was glycerinated and incubated with rabbit skeletal muscle heavy meromyosin (HMM). Masses of filaments in myoepithelial cells served as convenient standards for HMM decoration. Decorated filaments have cross-arms or projections, unlike the narrow, smooth filaments of control tissue. Decorated filaments in alveolar cells are located beneath the plasma membrane, in close association with secretory vacuoles, and near the Golgi apparatus; filaments near the latter two are often oriented perpendicular to the plasma membrane. Microvesicles are embedded in meshworks under the plasmalemma and near the Golgi apparatus. Intermediate-sized (85-115 A diameter), non-decorated filaments diverge from the meshworks of decorated filaments. Microvesicles are associated with intermediate-sized filaments as well. The association of actin-like filaments with secretory vacuoles and microvesicles and their location in areas of the cell concerned with biosynthetic activities suggest a possible function in the intracellular transport of secretory products.
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    Cell Motility and the Cytoskeleton 3 (1983), S. 131-150 
    ISSN: 0886-1544
    Keywords: flagella ; Chlamydomonas ; motility ; flagellar reversal ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Using a uniflagellate mutant of Chlamydomonas and flash photomicrography at 300 Hz, we have obtained detailed information on the forward and reverse beating modes of Chlamydomonas flagella and on the relationship between rotation of the uniflagellate cell and the bending cycle of the forward mode. Flagella ranging in length from 5 to 15.5 μm were photographed. There is a decrease in wavelength and an increase in curvature in the principal bends when the length of the flagellum is less than the normal length of 12-13 μm, but these changes are not sufficient to maintain similarity of the bending pattern. In the reverse mode, the flagellum propagates symmetrical, planar, undulatory waves with a shear amplitude which is the same as in the forward mode: there is a 19% increase in beat frequency and a similar decrease in wave length. The reorientation of the flagellar beat direction towards the axis of the cell in the reverse mode is caused both by the decrease in asymmetry of beat and by activation of sliding in the principal bends at an earlier time in the beat cycle, relative to the time of activation of sliding in reverse bends. There are additional rare modes of beating which may be related to intermediate stages in the transition between forward and reverse beating modes.
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    Cell Motility and the Cytoskeleton 3 (1983), S. 123-130 
    ISSN: 0886-1544
    Keywords: taxol ; microtubules ; flagellar outer doublets ; tubulin ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Taxol induces the in vitro assembly of calcium stable microtubules from flagellar tubulin solubilized from sea urchin (Strongylocentrotus purpuratus) sperm tail outer doublets by sonication. Assembly occurs in the presence or absence of exogenous GTP. The drug (10 μM) reduces the critical concentration of protein required for assembly to ≤0.04 mg/ml. 3H-Taxol binds specifically to both isolated flagellar outer doublets and to reassembled microtubules with calculated maximal binding ratios of 0.25 and 1.32 moles taxol/mole polymerized flagellar tubulin dimer, respectively. We suggest that the discrepancy in maximal binding ratios may result from the presence of an endogenous molecule(s) along the surface of outer doublet microtubules that restricts taxol binding to that structure.
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    Cell Motility and the Cytoskeleton 3 (1983), S. 185-197 
    ISSN: 0886-1544
    Keywords: dynein ; microtubules ; cell motility ; fibroblasts ; in vitro ; phagokinetic tracks ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Patients with Kartagener syndrome (KS) show defects in ciliary and flagellar movement that are usually associated with the partial or total absence of dynein side arms from axonemal microtubules. Dynein is essential for such movements, but its involvement in other cellular (particularly microtubule-related) processes is unknown. It has recently been reported that neutrophils from KS patients show impaired motility including responses to chemotactic stimuli, suggesting that dynein-like proteins may be generally involved in motile processes. In support of this, we have now found that spontaneous motility of cultured skin fibroblasts from KS patients is also markedly impaired. Three cell lines derived from skin explants of KS patients with deficient dynein side arms in nasal cilia and eight cell lines derived from normal volunteers were studied. Fibroblasts were seeded into dishes containing colloidal gold-coated cover glasses [Albrecht-Buehler, 1977], incubated for 24 h at 37°C, and the area of cell “phagokinetic” tracks determined.Each cell line studied in this manner reproducibly displayed an amount of spontaneous motility characteristic for that cell line. The mean track area (± SE) for all control cells studied was 14.6 ± 0.5 × 103μm2 whereas for KS fibroblasts was 8.7 ± 0.4 × 103μm2 (P 〈 0.001). Immunofluorescence microscopy using antitubulin and antihuman 210 K MAP antibodies revealed no differences in the staining patterns between control and KS fibroblasts. Pinocytic rates were identical, and the complement of tubulin and major microtubule associated proteins as seen on one-dimensional SDS polyacrylamide gel autoradio-graphs appeared similar for control and KS cells. Thus, the observed motility defect is probably not the result of alterations in the occurrence or distribution of microtubules or in the occurrence or binding of the major microtubule-associated proteins. This defect in cellular motility may be related to the absence of dynein or may reflect another independent cellular defect.
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    Cell Motility and the Cytoskeleton 3 (1983), S. 321-332 
    ISSN: 0886-1544
    Keywords: microtubule sliding ; interdoublet links ; radial spokes ; bend formation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Ciliary axonemes from Tetrahymena extracted by KCl to remove the dynein arms reveal an orderly array of interdoublet links connecting adjacent A-B or A-A subfibers. The links repeat every 96 nm at a stable site on the A subfiber positioned near the bases of radial spokes 2 and 3. Both links and radial spokes are in lateral register across the nine successive doublets of unbent axonemes. In contrast, bent axonemes or those reactivated by ATP to undergo partial sliding disintegration exhibit systematic displacement of the interdoublet links. The links show no evidence of having elastic or other extendable properties and, therefore, must have undergone intermittent attachment with nonstructural binding sites on the adjacent subfiber. These observations suggest a more dynamic role for the interdoublet links in ciliary motion than previously has been envisioned.
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    Cell Motility and the Cytoskeleton 3 (1983), S. 213-226 
    ISSN: 0886-1544
    Keywords: microtubules ; fertilization ; cell division ; sea urchin ; cytoskeleton ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The microtubule-containing structures that appear in eggs during fertilization and cell division in the sea urchins Lytechinus variegatus and Arbacia punctulata were detected by antitubulin immunofluorescence microscopy of detergent extracted cytoskeletal preparations. The extraction buffer, which is composed of 0.55 mM MgCl2, 10 mM EGTA, 25 mM MES, 25% glycerol, 1% Nonidet P-40, and 25 μM PMSF, pH 6.7, allows for dramatically improved fluorescent images compared to those obtained using conventional staining procedures, with residual background staining being reduced to near zero.The immunofluorescent images obtained using this technique provide information on several motile events that occur during the first cell cycle. This technique demonstrates that all of the cytoplasmic microtubules are associated with the incorporated sperm's centrioles during female pronuclear migration. This changes during the centration of the male and female pronuclei at which time a monastral array of microtubules forms in the egg's cytoplasm. A large proportion of the monastral microtubules do not appear to be associated with the centrioles. At prophase and early metaphase, the centrioles are the dominant microtubule organizing centers (MTOCs) consistent with mitotic theories that the kinetochore catches, but does not initiate, microtubules. Observations of intercentriolar distances show that there are three stages of pole separation during the first cell cycle. The initial separation occurs during pronuclear centration, the second during the streak stage, and the final one during the late stages of mitosis. At telophase, polar microtubules appear to extend into the cortex supporting the cell surface at all regions except the presumptive cleavage site.
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    Cell Motility and the Cytoskeleton 3 (1983), S. 281-282 
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
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    Cell Motility and the Cytoskeleton 3 (1983), S. 307-320 
    ISSN: 0886-1544
    Keywords: contact inhibition ; contact guidance ; growth cones ; cell-cell interactions ; neuronal contact behavior ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The outcome of contact interactions involving neurons and nonneurons varies depending on the cell types involved. When neuronal growth cones from either ciliary (motor) or dorsal root (sensory) ganglia directly contact the lamellipodium of an embryonic heart fibroblast, both neurite elongation and fibroblast locomotion are inhibited. This occurs in spite of the fact that cell-surface activity in both cells continues unabated. Such contact inhibition is not observed when homologous ganglionic nonneurons are involved in the interaction. In fact, these cells become intimately associated with growth cones and/or neuritic shafts as a result of the contact. The detailed nature of the respose to contact exhibited by nerves and nonnerves varies not only with cell type but also with the portion of the cell involved in the contact. Growth cone filopodia tend to actively palpate the fibroblast surface, whereas spread regions, termed “veils,” form areas of apposition with fibroblast lamellipodia. This latter situation resembles the “typical” contact inhibition of locomotion that occurs following embryonic heart fibroblast-fibroblast interactions. Growth cones also frequently exhibit contact guidance when interacting with nonruffling lateral surfaces of heart fibroblasts.
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    Cell Motility and the Cytoskeleton 3 (1983), S. ix 
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
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  • 35
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    Cell Motility and the Cytoskeleton 1 (1981), S. 455-468 
    ISSN: 0886-1544
    Keywords: intercellular bridge ; intercellular communication ; cytokinesis ; squid ; ultrastructure ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Incomplete cytokinesis followed by the disappearance of the midbody and spindle remnant results in intercellular bridges between the cells of the blastoderm of the squid embryo. An electron microscope study of the morphology of the stages of development of the intercellular bridge is presented. Cytokinesis ceased as the furrow base reached a diameter slightly larger than the midbody. As furrowing stopped, a dense material accumulated to form a cylindrical sheath 50 nm thick, lining the inner surface of the furrow base. Proteolytic enzymes showed this material to have a significant protein component. As the midbody broke down, vesicles lined the inner surface of the bridge sheath. In this configuration, there was cyto-plasmic continuity between the cells, and organelles appeared to pass through the bridge.The intercellular bridge could become temporarily closed. Vesicles entered the channel and fused with the vesicles lining the inner surface of the sheath. The vesicles enlarged until the channel became occluded with a series of transverse cisternae, the edges of which were embedded in the material of the sheath. When the bridge reopened, the transverse cisterna appeared to dissociate from the sheath, move out of the channel, and break down. Occasionally bridges were seen in which the bridge wall appeared distorted into lobes. It is suggested that such bridges might be in the porcess of breaking down, resulting in the final separation of the cells.
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    Cell Motility and the Cytoskeleton 1 (1981), S. 469-483 
    ISSN: 0886-1544
    Keywords: microtubules ; nucleation ; mitosis ; nocodazole ; immunocytochemistry ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The reassembly of microtubules is described in mitotic cells after release from nocodazole-induced block. The formation of microtubules was followed by light microscopic immunocytochemical staining using the PAP method, combined with to-luidine blue staining of the chromatin. The light microscopic observations on whole cells were compared with ultrastructural observations on thin sections. This step is essential to ascertain complete destruction of microtubules during the nocodazole treatment and to correlate immunocytochemical staining with the presence of microtubules.Removal of nocodazole (10 or 1 μg/ml) after a sufficiently long incubation to induce a complete disappearance of microtubules resulted in the appearance of tubulin staining specifically associated with the centromeres and with one or two isolated points in the cytoplasm. Electron microscopy confirmed that the staining was due to the massive accumulation of small microtubules at the kinetochores and centrosomes. Kinetochore nucleation was seen only in association with condensed metaphase-stage chromosomes and not with the less-condensed prophase chromosomes.In a second type of experiment cells were allowed to enter mitosis in the presence of an incompletely active concentration of nocodazole (0.1 μg/ml). The construction of the mitotic spindle was arrested; however, short microtubules were assembled at the kinetochores and centrosomes.These experiments demonstrate that in living mitotic PTK2 cells the kinetochores, as well as the centrosomes, exert a nucleating action on tubulin assembly.The further elongation of microtubules after removal of nocodazole was seen to occur preferentially along axes between the centrosomes and the kinetochores. This resulted in the construction of normal metaphases that evolved through anaphase and telophase. We have attempted to formulate a hypothesis that may explain the oriented assembly that seems to be essential in the construction of the spindle.
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    Cell Motility and the Cytoskeleton 1 (1981), S. 485-497 
    ISSN: 0886-1544
    Keywords: actin ; tubulin ; nucleotides ; polymerization ; microfilaments ; microtubules ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Both actin and tubulin, the major proteins of the cytoskeleton, bind nucleotide triphosphate (NTP) and exhibit the phenomenon of “polymerization-coupled” NTP hydrolysis. In this report I review the nature of polymerization-coupled NTP hydrolysis, and its possible role in the cellular function of actin and tubulin. Polymerization-coupled hydrolysis may be viewed as simply reflecting differences in the NTPase activity of free subunit as compared to polymer. Making assumptions concerning the values of various rate constants, it is possible to write expressions for the effects of NTP hydrolysis on the kinetics of polymerization. The role of NTP hydrolysis may be viewed in at least three different ways: (1) Hydrolysis alters the kinetics of assembly and disassembly. This leads to a consideration of the role of subunit flow in microtubule and microfilament function. (2) Hydrolysis is an essentially irreversible step that separates the assembly and disassembly reactions. This suggests a role of NTP in the regulation of polymer content during cellular cycles of assembly and disassembly. (3) NTP may allow transient stabilization of intersubunit bonds. This suggests a role of NTP in nucleation and possible regulation of nonequilibrium states of assembly.
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    Cell Motility and the Cytoskeleton 1 (1981), S. 499-515 
    ISSN: 0886-1544
    Keywords: dynein ; tubulin ; axonemes ; microtubules ; microtubule-associated proteins ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Microtubule-associated proteins (MAPs), isolated from brain tubulin, bound to and saturated outer fibers of Chlamydomonas flagella. MAPs present on these microtubules prevented the subsequent recombination of dynein. MAPs also bound to intact axonemes and thus did not specifically bind to the dynein binding sites on the A subfiber. A molar ratio of 1 mole MAP2 per 27 moles tubulin dimers at saturation of the outer fibers with MAP2 suggested that MAPs could effectively interfere with dynein recombination only if the MAPs were near the dynein binding sites to sterically prevent binding. However, electron microscopic observations indicated that MAPs were not localized but, instead, were dispersed around the outer fibers. In addition, MAP2 present at saturating amounts on in vitro assembled brain microtubules had no significant effect on dynein binding. Dynein-decorated microtubules contained clusters of arms suggesting that there may be cooperative interaction between the arms during dynein binding. Because the A subfiber of axonemes contains sites to which dynein preferentially attaches, MAPs may prevent recombination by interfering with cooperative binding to these specific sites. Dynein presumably binds with equal affinity to any protofilament on in vitro assembled microtubules, and, therefore, the MAPs may not be capable of effectively interfering with cooperative binding of dynein to these microtubules.
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    Cell Motility and the Cytoskeleton 2 (1982) 
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    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
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    Cell Motility and the Cytoskeleton 2 (1982), S. 1-8 
    ISSN: 0886-1544
    Keywords: microfilaments ; F-actin ; brain actin-depolymerizing factor ; tropomyosin stabilization of microfilaments ; DNase I inhibition assay ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Brain or muscle F-actin is rapidly depolymerized to monomeric actin in vitro by actin-depolymerizing factor, a protein isolated from chick embryo brain. Binding of muscle tropomyosin to muscle F-actin protects the F-actin from depolymerization by this factor. A 8.4/1.0 molar ratio of actin subunits to tropomyosin, achieved by incubation of the F-actin with excess tropomyosin, protects 58% of the F-actin from depolymerization by excess actin-depolymerizing factor for at least 3 hr at 25°C. Thus, actin-depolymerizing factor seems to be specifically directed toward actin filaments lacking tropomyosin.
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    Cell Motility and the Cytoskeleton 2 (1982), S. 9-24 
    ISSN: 0886-1544
    Keywords: amoebae ; actinopoda ; heliozoa ; Actinophrys ; phagocytosis ; pseudopodia ; membrane ; extrusomes ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Two phases of prey capture by the heliozoon Actinophrys sol are documented by electron microscopy. The phases are those of prey adhesion to the predator and enclosure of the prey by the predator. Adherence is brought about by numerous small pieces of adhesive membrane produced by the predator at the site of prey contact. Some of the heliozoan extrusomes expel their contents at this time, but the significance of this event is unclear. Enclosure of the prey is effected by a funnelshaped pseudopodium. This is drawn over the prey by the action of the leading margin. The ultrastructural appearance of the cytoplasm of the leading margin differs from the rest of the cell, being homogeneous and finely filamentous. Both force and traction for the progression of the pseudopod are generated primarily at the tip. During the development of the funnel-pseudopod, extrusomes expand and fuse with each other and with the plasma membrane. Their investing membrane is thereby made available as food vacuole membrane.
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    ISSN: 0886-1544
    Keywords: cell migration ; epithelial cell culture ; 2-deoxyglucose ; glycolysis ; microtrabecular lattice ; ATP ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Using a line of epithelial cells (SCCA5) derived from a spontaneous rat carcinoma, the glucose analogue 2-deoxyglucose (2DG) has been shown by time-lapse cinemicrography to produce a cessation of motility by 1 hour that can be reversed by replacement of the 2DG, and does not occur in equivalent media with or without glucose or in 2DG-containing media with added pyruvate and citrate. The effect on the cells at the edge of an epithelial island is to prevent the formation of new lamellipodia and produce a progressive retraction and condensation of lamellipodia already present. This effect of 2DG on motility corresponds with a significant reduction in the level of ATP that is partially restored after 30 minutes in the recovery incubation. Only a slight reduction in protein synthesis occurs in the presence of 2DG. The external morphology and the cytoplasmic ground substance of the cells were studied by scanning electron microscopy and high voltage electron microscopy respectively. It was found that after incubation in 2DG for 1 hour the outline of the free edges of the cells was distorted resulting in redistribution of microvilli, condensation of cytoplasm into strands, and irregular projections from the edges of residual lamellipodia. The structure of the cytoplasmic ground substance in lamellipodia from cells incubated in 2DG for 3 hours was distinctly different from that in cells incubated for 3 hours in 2DG then recovered for 25 minutes, or in cells incubated in glucose-containing medium for 3 hours. In the 2DG-treated cells the lattice-like structure evident in critical-point-dried cells was condensed into short thick strands that terminated in bulbous ends, whereas in cells recovered for 25 minutes the lattice material was elongated and tapering and the interlattice space relatively expanded. The results obtained support the concept of modulation occuring in the structure of the microtrabecular lattice component of the cytoplasmic ground substance coincident with alterations in cell function and metabolic state.
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    Cell Motility and the Cytoskeleton 2 (1982), S. 497-508 
    ISSN: 0886-1544
    Keywords: cilia ; electric motor control ; ciliates ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We have studied the motor responses to membrane hyperpolarization of the marginal cirri in Stylonychia using voltage-clamp, high-speed cinematography, and computer-processing techniques. The cirri started beating when voltage step amplitudes rose beyond 5 mV. The power stroke was oriented toward the posterior cell and (hyperpolarizing motor activation). The frequency rose slightly during a voltage step, and decreased with similar rates for 100 ms following the step end. Amplitude and duration of the step tended to increase the motor response of the cirri. The late response declined exponentially. The time constant of the decay rose with the step amplitude. Among three response parameters tested (frequency, duration, number of cycles), the number of evoked ciliary cycles was best correlated with the amplitude of the hyperpolarization. Comparisons with the responses to depolarizing voltage steps reveal similarities in the relaxation of ciliary activity which appears to be uncoupled, in part, from the electric membrane events during the voltage stimulus.
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    Cell Motility and the Cytoskeleton 2 (1982), S. 583-597 
    ISSN: 0886-1544
    Keywords: endocytic vesicles ; microtubules ; 10-nm filaments ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Ligand binding to cell surface receptors induces rapid internalization of ligandreceptor complexes by receptor mediated endocytosis. We have examined the intracellular movement of endocytic vesicles, induced by the lectin concanavalin A (Con A), in cultured rat ovarian granulosa cells using fluorescence and electron microscopy. Within 20 minutes of ligand treatment at 37°C, numerous Con A-containing endocytic vesicles form, which migrate to the cell center by 60 minutes. Double label fluorescence microscopy, using fluorescien-Con-A and rhodamine immunofluorescent staining of tubulin or vimentin, indicates that during vesicle migration microtubules and 10-nm filaments are altered in their organization. By 30 minutes, vesicles are associated with microtubule bundles, which subsequently collapse around the nucleus. Similarly, 10-nm filaments accumulate around the nucleus in conjunction with the perinuclear aggregation of endocytic vesicles. Electron microscopy of Con A-horseradish peroxidase-labeled cells demonstrates that endocytic vesicles fuse to form large receptosome-like structures during intracellular migration and these structures are associated with cytoplasmic microtubules and 10-nm filaments. Taxol, a drug that stabilizes microtubules, prevents endocytic vesicle translocation to the Golgi region. Nocodazole, which causes microtubule disassembly, results in the collapse of 10-nm filaments and the central aggregation of endocytic vesicles. The data indicate that the cytoskeleton participates in the directed intracellular movement of endocytic vesicles; the possible subcellular basis for this movement is discussed.
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    Cell Motility and the Cytoskeleton 2 (1982), S. 13-18 
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    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
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    Cell Motility and the Cytoskeleton 4 (1984) 
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    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
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    Cell Motility and the Cytoskeleton 3 (1983), S. 699-719 
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    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
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    Cell Motility and the Cytoskeleton 2 (1982), S. 59-65 
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    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
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    Cell Motility and the Cytoskeleton 4 (1984), S. 371-385 
    ISSN: 0886-1544
    Keywords: microtubules ; dynein ; tubulin ; cilia and flagella ; microtubule associated proteins ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Dynein, obtained from axonemes of Chlamydomonas, binds by both its A and B ends to microtubules assembled from twice cycled (2 ×) and purified (6S) brain tubulin as well as to microtubules in native spindles, thereby inducing microtubule crossbridging. The two ends of the dynein arm exhibit distinct binding characteristics for the different microtubule preparations. Greater than 99% of the dynein arms are bound exclusively by their B ends to microtubules assembled from 6S tubulin in the presence of dynein and decorated to saturation. In contrast, greater than 80% of the dynein arms are bound by both their A and B ends to and, therefore, crossbridge 6S microtubules that are only partially dynein decorated. Binding of the A end of the dynein arm to saturated 6S microtubules can be enhanced by destabilizing the binding of the B end upon addition of ATP and vanadate. These observations suggest that Chlamydomonas dynein arms can bind by their A ends to microtubules assembled from 6S tubulin only when the B ends of the arms either are not bound or are bound but do not occupy all available dynein binding sites. Dynein exhibits a slight preference for binding by its A end to microtubules assembled from 2 × tubulin and containing microtubule associated proteins (MAPs). Approximately 90% of the dynein arms crossbridge adjacent 2 × microtubles that are only partially decorated. But as saturation of these microtubules with dynein is approached, the majority of the arms are bound solely by their A ends, while a smaller percentage are bound by their B ends or by both their A and B ends. These studies indicate that the type of microtubule as well as the degree of saturation of the microtubule with dynein can determine whether microtubule crossbridging occurs.
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    Cell Motility and the Cytoskeleton 4 (1984), S. 431-441 
    ISSN: 0886-1544
    Keywords: dynein ; chromatophores ; permeabilization ; melanosomes ; motility ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Teleost chromatophores are filled with individual pigment granules that rapidly aggregate to the cell center or become dispersed throughout the cytoplasm in response to environmental stimuli. Microtubules appear to be required for pigment aggregation (movement toward the cell center), and recent findings have suggested that a dynein-like ATPase may participate in force production. Based on previous studies, however, it has been argued that pigment aggregation does not require energy directly, a view that supports the involvement of an elastic component in granule movement. To examine this point further, we have reinvestigated the energy requirements for pigment aggregation using both intact cells and detergent-permeabilized cell models of Fundulus melanophores. Poisons of oxidative phosphorylation, namely, 2,4 dinitrophenol and NaCN, reversibly inhibit melanosome aggregation in response to adrenaline. Inhibition of movement results directly from depletion of intracellular ATP, since pigment translocation can be reactivated in permeabilized cells by the addition of exogenous ATP to the lysis buffer. Non-hydrolyzable analogues, including β,γ-imidoadenosine-5′-triphosphate (AMPPNP), β,γ-methylene adenosine-5′-triphosphate (AMPPCP), and ATPγS, will not substitute for ATP in reactivation of movement. Similarly, other nucleotides such as ADP, AMP, GTP, CTP, and ITP, have limited ability to support melanosome aggregation in metabolically poisoned cells subjected to detergent lysis. ATP itself has no effect on intact cells. These results indicate that melanosome aggregation is ATP-dependent and energy-driven, and are consistent with a role for a force-transducing ATPase in particle movement.
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    Cell Motility and the Cytoskeleton 4 (1984) 
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    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
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    Cell Motility and the Cytoskeleton 3 (1983) 
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    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
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    Cell Motility and the Cytoskeleton 3 (1983), S. 431-438 
    ISSN: 0886-1544
    Keywords: myotendinous junction ; laminin ; type IV collagen ; heparan sulfate proteoglycan ; alpha actinin ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The muscle-tendon junction of murine skeletal muscles has been analyzed by a variety of extraction techniques, by myosin subfragment-1 binding experiments, and by ultrastructural immunocytochemistry. The results indicate that the muscle-tendon junction is composed of four distinct domains: an intracellular domain, the internal lamina; a domain connecting the internal lamina with the lamina densa of the external lamina, the connecting domain; the lamina densa; and a domain which attaches the lamina densa to the collagen fibers, the matrix. Each of these domains is distinct with respect to position, three-dimensional organization, and molecular composition, and is therefore considered to have a unique role in the transmission of contractile force.
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    Cell Motility and the Cytoskeleton 3 (1983), S. 579-588 
    ISSN: 0886-1544
    Keywords: calcium-dependent protease ; contractile proteins ; platelets ; Life and Medical Sciences ; Cell & Developmental Biology
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    Cell Motility and the Cytoskeleton 3 (1983), S. 609-622 
    ISSN: 0886-1544
    Keywords: erythrocyte membrane ; surface elastic shear modulus ; membrane viscosity ; hereditary disorders of blood ; membrane yield ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Measurements of the mechanical properties of the erythrocyte membrane provide a direct assessment of the proper function of its structural components. To assess the effects of alterations in molecular structure on membrane mechanical properties, measurements have been performed on cells from six individuals whose membranes contain inherited, biochemically characterized structural defects. Because the contribution of the memmbrane skeleton to the mechanical behavior of the membrane is most evident in shear deformation, mechanical experiments were performed to measure the material constants which characterize the response of the membrane to shear force resultants. The surface elastic shear modulus characterizes the elastic response of the membrane; the yield shear resultant is the maximum shear force resultant which the membrane can support elastically; and the plastic viscosity coefficient characterizes the rate of membrane deformation when the elastic limit has been exceeded.Generally, it was found that when the molecular defect is found to occur in a region of the skeleton which is stress-supporting, the maximum elastic strength of the membrane is reduced. However, the magnitude of the reduction can be quite different for membranes having similar or even identical defects. In some cases the differences can be attributed to the removal of the most fragile cells of the population by the spleen, but other results indicate that the biochemical description of the defects may be incomplete. These results emphasize the need for further refinements both in the biochemical characterization of membrane skeleton structure and in the description and measurement of membrane mechanical properties.
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    Cell Motility and the Cytoskeleton 3 (1983), S. 671-682 
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    Keywords: actin ; cytoskeleton ; membrane connections ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Recently, molecules highly related to erythrocyte spectrin have been identified in nonerythroid cells. Here we summarize our current understanding of these molecules and suggest a model for their organization. Significant differences exist between this family of proteins isolated from mammalian cells and avian cells, and this may explain the variability in antibody preparations as well as differences in peptide maps of these subunits which have been reported. We have prepared antibodies specific for the variant subunits of the spectrinlike proteins fodrin, spectrin, and TW260/240 and analyzed the distribution of these variant subunits in different chicken cell types as well as their developmental distribution in the intestine. The results suggest that fodrin is the general member of this family of proteins and can even coexist with other spectrinlike proteins in the same cells.
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    Cell Motility and the Cytoskeleton 15 (1990) 
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    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
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    Cell Motility and the Cytoskeleton 16 (1990), S. 1-6 
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    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
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    Cell Motility and the Cytoskeleton 15 (1990), S. 23-33 
    ISSN: 0886-1544
    Keywords: centrosome ; cytaster ; MTOG ; pericentriolar material ; 51 kD protein ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Miniasters formed in mitotic sea urchin egg after treatment with 5% hexylene-glycol were investigated with the combined techniques of indirect immunofluo-rescence using anti-tubulin and anti-51 kD protein antibodies and electron microscopy.The formation of miniasters was dependent on the mitotic cycle. In the cytoplasm of eggs treated with hexyleneglycol at early prometaphase, a small number of microtubule fragments was observed, whereas in those treated at pro-metaphase, many miniasters and microtubule fragments were seen. When treated at metaphase, we found a great number of miniasters: 250-350 in one egg. In contrast, no miniasters were seen in eggs treated at anaphase, although many long microtubules that spread throughout the cytoplasm were observed. In the eggs treated at telophase, we scarcely noticed microtubule structures in the cytoplasm. In the center of miniasters, granules were found, showing the same size and electron density as those of the microtubule-organizing granules (MTOGs). Furthermore, the 51 kD protein, a component of the centrosome and mitotic spindle, was observed to be localized in the region of miniasters.
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    Cell Motility and the Cytoskeleton 15 (1990), S. 41-50 
    ISSN: 0886-1544
    Keywords: adhesion plaques ; cytoskeletal interactions ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
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    Notes: Vinculin and talin are adhesion plaque proteins which have been shown to interact with each other in vitro. In order to begin to investigate where the talin-binding domain is in vinculin, vinculin was digested with Staphylococcus aureus V8 protease to generate two major fragments of 85 and 30 kDa, and these fragments were purified. Nitrocellulose overlays with 125I-talin and the 125I-85 kDa vinculin fragment and sucrose density gradient centrifugation demonstrated that the talin-binding domain was localized to the 85 kDa vinculin fragment. Quantification of 125I-talin binding in the overlays showed that four times more talin bound to the 85 kDa fragment as compared to intact vinculin. Competitive immunoprecipitation experiments demonstrated that unlabeled 85 kDa fragment, was about three fold more effective at competing for 125I-85 kDa binding to talin than was unlabeled vinculin. These results suggest that the 30 kDa fragment inhibits the vinculin-talin interaction even though the talin-binding domain is localized in the 85 kDa fragment.
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    Cell Motility and the Cytoskeleton 15 (1990), S. 34-40 
    ISSN: 0886-1544
    Keywords: rat liver cells ; immunoprecipitation ; immunocytochemistry ; membrane-bound proteins ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Confluent and proliferatively quiescent T51B rat liver epithelial cells provide a cellular model for the study of epidermal growth factor (EGF) effects in non-neoplastic cells. Immunoreactive calpactin II, a well-known substrate for EGF-receptor kinase, was found predominantly in the cytosol, although a second im-munoreactive pool was found in a Triton X-100-extractable membrane fraction. Stimulation with EGF resulted in a rapid and transient (2-;5 min) formation of ruffles at the cell surface and at the cell-cell contacts. Both calpactin II and filamentous actin were found co-localized at the membrane ruffles. Immunopre-cipitations of membrane-bound calpactin II from 32P-labeled cells indicate a transient EGF-dependent phosphorylation of calpactin II correlating with membrane ruffling. These results suggest a temporal (2-5 min) function for calpactin II at the plasma membrane during the EGF-induced mitogenesis of T51B cells.
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    Cell Motility and the Cytoskeleton 15 (1990) 
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    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
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    Cell Motility and the Cytoskeleton 15 (1990), S. 67-70 
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    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
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    Cell Motility and the Cytoskeleton 15 (1990), S. 51-62 
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    Keywords: microtubule-associated proteins ; intracellular motility ; CTPase ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A high molecular weight microtubule binding protein has been isolated from homogenates of Dictyostelium. Because of its sedimentation velocity (20s), ATP-sensitive binding to microtubules. UV-vanadate-ATP mediated fragmentation, prominent CTPase activity, and its ability to produce limited microtubule movement in vitro, we consider this protein to be a form of cytoplasmic dynein. A polyclonal antibody monospecific to this protein was produced, and dynein's intracellular distribution in ameboid cells was examined by immunofluorescence. The antibody labels a punctate cytoplasmic pattern, localizes to a spherical region adjacent to the nucleus, and also appears to label the nuclei. The punctate staining pattern is consistent with cytoplasmic dynein's proposed function in organelle transport. The spherical juxtanuclear object stained is coincident with this cell's microtubule organizing center, an obvious termination point for minus-end directed microtubule motors. By immunofluorescence, there does not appear to be a substantial amount of dynein in the intranuclear mitotic spindles of Dictyostelium, These data provide evidence for localization of cytoplasmic dynein in cells, and suggest that Dictyostelium will be a useful system in which to study the molecular biology of microtubule-associated motor enzymes.
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    Cell Motility and the Cytoskeleton 15 (1990), S. 71-75 
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    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
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    Cell Motility and the Cytoskeleton 15 (1990), S. 88-98 
    ISSN: 0886-1544
    Keywords: tau ; MAP2 ; dynamic instability ; microtubule nucleation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: In this paper, we report on the effect of brain microtubule-associated proteins (MAPs) on the dynamic instability of microtubules as well as on the nucleation activity of purified centrosomes. Under our experimental conditions, tau and MAP2 have similar effects on microtubule nucleation and dynamic instability. Tau increases the apparent elongation rate of microtubules in proportion to its molar ratio to tubulin, and we present evidence indicating that this is due to a reduction of microtubule instability rather than to an increase of the on rate of tubulin subunits at the end of growing microtubules. Increasing the molar ratio of tau over tubulin leads also to an increase in the average number of microtubules nucleated percentrosome. This number remains constant with time. This suggests that the number of centrosome-nucleated microtubules at steady state can be determined by factors that are not necessarily irreversibly bound to centrosomes but, rather, affect the dynamic properties of microtubules.
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    Cell Motility and the Cytoskeleton 16 (1990) 
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    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
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    Cell Motility and the Cytoskeleton 16 (1990), S. 225-228 
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    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
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    Keywords: Aspergillus ; benomyl ; chimeric gene ; tubulin mutants ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We have constructed a chimeric β-tubulin gene that places the structural gene for the tubC β-tubulin of Axpergillus nidulans under the control of the benA β-tubulin promoter. Introduction of cither this chimeric gene or a second wild-type ben.A gene into a benomyl-resistant benA22 strain causes it to become benomyl sensitive, indicating that the introduced genes are functional. Analysis of the tubulin proteins synthesized in benA22 strains into which a second wild-type benA β-tubulin gene was transformed showed that the total amount of β-tubulin protein was the same as in the parental strain with a single benA gene. Thus the level of β-tubulin must be regulated. This was also true of transformants carrying an extra copy of the chimeric β-tubulin gene. The total amount of β-tubulin was the same as in the parental strain. Two-dimensional gel analysis showed that the endoge-nous benA22 and the introduced chimeric tubC gene contributed equally to the total β-tubulin pool. Th; fact that one-half of the benA β-tubulin could be replaced by tubC β-tubulin with no effect on the growth of the cells suggests that the benA and tubC β-tubulins are functionally interchangeable.
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    Cell Motility and the Cytoskeleton 18 (1991), S. 41-54 
    ISSN: 0886-1544
    Keywords: contractile ring ; mitotic spindle ; birefringence ; video-enhanced microscopy ; fluorescence microscopy ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: This study focuses on the dynamic reorganization of actin and myosin (“conventional” myosin, or myosin-II) during cytokinesis in D. discoideum. This is the first study identifying the birefringence of the spindle microtubules as well as three sets of microfilamentous structure in Dictyostelium. The change of organization in these fibrillar structures was followed in real-time with video microscopy, using a Universal Polarizing Microscope equipped with polarized-light (POL) and differential interference contrast (DIC) optics combined with digital image processing. High-frequency mitotic cells were obtained by semi-synchronous culture, and high-resolution observations were made by utilizing the agar-overlay method (Yumura et al.: Journal of Cell Biology 99:894-899, 1984). The molecular identity of the birefringent structures was determined by fluorescence microscopy. Through-focus observations were performed with an axial resolution of 0.3 μm depth of field.The actomyosin fibrils show a dramatic reorganization throughout mitosis. The fibrils at the leading lamellipodia disappear, and there is a striking assembly of the cortical actomyosin in pro-metaphase, which is accompanied by a decrease in cell volume. The cortical actomyosin gradually increases through anaphase. After late anaphase, very active polar lamellipodia, with an average life of less than 1 minute, are formed. We confirmed that the polar lamellipodia include actin, but not myosin-II. At the cleavage furrow, the microfilaments form two distinctive structures: circular contractile ring at the equator, and a cortical filament array parallel to the polar axis. Myosin is localized in the contractile ring, but not associated with the axial array of F-actin. Actomyosin in the contractile ring gradually transforms into cortical network at the posterior region of daughter cells. The constriction of the furrow is accompanied by a drastic efflux of water as evidenced by highly active contractile vacuole formation and turbulent motion of minute vesicles connected to the furrow. This study demonstrates the presence of a new microfilament structure, as well as the dynamic property of the contractile ring, and sheds new light on the contractile mechanisms underlying cytoki-nesis.
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    Cell Motility and the Cytoskeleton 18 (1991), S. 76-76 
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
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    Cell Motility and the Cytoskeleton 16 (1990) 
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
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    Cell Motility and the Cytoskeleton 16 (1990), S. 80-87 
    ISSN: 0886-1544
    Keywords: cytoskeleton ; chemotaxis ; polymerization ; motility ; nucleation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Definition of the kinetics of ligand-activated actin polymerization in the neutrophil is important for ultimately understanding the mechanisms utilized for regulation of actin polymerization in this non-muscle cell. To better define the kinetics of formyl peptide (fMLP) -induced actin polymerization in neutrophils we determined F-actin content at 5 second intervals after activation of human neutrophils with a range (10-11-10-9M) of fMLP concentrations. The state of actin polymerization was monitored by quantifying F-actin content with NBD phallacidin binding in both flow cytometric and extraction assays. Results demonstrate three successive kinetic periods of fMLP-induced actin polymerization in neutrophils, a lag period, a 5 second period when rate of polymerization is maximal, and a period of declining rate of actin polymerization as F-actin content approaches a maximum. The duration of the lag period, the maximum rate of polymerization, and the maximum extent of polymerization all depend upon the fMLP concentration. The lag period varies from 0 to 12 seconds and is followed in 5-10 seconds by a 5 second burst of actin polymerization when the rate is as great as 9% increase in F-actin content per second. After the 5 second burst of polymerization, the rate of polymerization rapidly declines. The study defines three distinct kinetic periods of fMLP-induced actin polymerization during which important rate-limiting biochemical events occur. The mechanistic and motile implications of kinetic periods are discussed.
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    Cell Motility and the Cytoskeleton 17 (1990) 
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
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    Notes: No Abstarct.
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    Cell Motility and the Cytoskeleton 17 (1990), S. 250-263 
    ISSN: 0886-1544
    Keywords: myosin ; microinjection ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We present microinjection data in support of an indirect approach by which cytoplasmic protein interactions important in the processes of bone resorption can be elucidated. Three polyclonal antibodies (M1, M3, M5) raised against myosin II from perfused rat liver differently affected the actin-activated Mg ATPase of myosin II. These antibodies microinjected into isolated rat osteoclasts affected osteoclast morphology and activity in bone resorption. M1, which completely inhibited myosin ATPase activity at a antibody:myosin ratio of 10:1, initially promoted the extension/retraction motility of lamellipodia but eventually reduced the spread area of osteoclasts along the substrate after 20 hr. M3, which inhibited ATPase activity by 70%, had similar effects; however, M5, which weakly inhibited ATPase activity, neither promoted extension/retraction nor reduced spread area of osteoclasts. Immunofluorescence showed that these antibodies removed myosin II from the majority of actin filaments in injected osteoclasts. Because antibodies that did not bind to a myosin II column had little effect on the extension/retraction of lamellipodia or the osteoclast spread area, these data suggest that myosin II participates in the stabilization of osteoclast lamellipodia along the substrate. M1 injection strongly inhibited injected osteoclasts from excavating resorption lacunae in bone slices, compared to control antibody. M3 and M5 were less effective but also inhibited bone resorption. These data show that myosin II is functionally important in bone resorption and that the osteoclast-differentiated activity of bone resorption is a more sensitive assay for myosin activity than lamellipodia motility or cell morphology.
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    Cell Motility and the Cytoskeleton 17 (1990), S. 267-275 
    ISSN: 0886-1544
    Keywords: microtubule-associated proteins ; cell cycle ; phosphorylation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Microtubule-interacting proteins have been studied in the lower eukaryote Physarum polycephalum. We show for the first time 1) the presence in Physarum amoebal crude extracts of at least six polypeptides that bind specifically to amoebal microtubules, 2) the binding between these proteins and mammalian microtubules, 3) the heat stability of two of these polypeptides (125 and 235 kDa), 4) the functional properties of a fraction containing a heat-soluble 125 kDa polypeptide, and 5) the phosphorylation of the 125 kDa polypeptide during two distinct periods of the cell cycle in Physarum synchronous plasmodia, first at late S/early G2 phase and second at late G2/prophase.
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    Cell Motility and the Cytoskeleton 17 (1990), S. 276-290 
    ISSN: 0886-1544
    Keywords: isoforms ; cytoskeleton ; angiosperms ; synthetic peptides ; IEF-SDS PAGE ; Western blot ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Actin protein isovariants have been identified in animals with distinct cytoplasmic or muscle specific patterns of expression. Analysis of vascular plant actin gene sequences suggests that an even greater diversity should exist within the plant actin protein families, but previous studies on plant proteins have not demonstrated the presence of multiple actin isovariants. Antibodies recognizing a conserved amino-terminal plant actin peptide, a family of plant actin peptides from a variable region, and two monoclonal antibodies to conserved epitopes within animal actins were used to identify isovariants of soybean actin resolved by two-dimensional isoelectric focusing (IEF) sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Approximately six to eight actin isovariants with pi values ranging from 5.1 to 5.8 have been identified from soybean hypocotyls. Stems, leaves, and roots with varying amounts of most isovariants present in all four organs. Acidic isovariants were present in much higher levels in leaves and stems. Antisera with λ-class actin specificity detected a subset of three isovariants in all organs examined. One monoclonal and one antipeptide antisera are shown to react well with a wide variety of plant actin isovariants. Similar patterns of actin isovariants were detected in the distant angiosperms, Arabidopsis petunia, and maize. It is likely that many of these diverse classes of isovariants have been preserved throughout vascular plant evolution and reflect the ancient diversity within plant actin gene families. The extreme difference among isovariants implies the presence of a complex actin-based cytoskeletal system in plants.
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    Cell Motility and the Cytoskeleton 17 (1990), S. 291-300 
    ISSN: 0886-1544
    Keywords: PtK1 keratin filaments ; electrophoresis ; autoradiography ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Treatment of PtK1 cells with 5 mM acrylamide for 4 hr induces reversible de-phosphorylation of keratin in concert with reversible aggregation of intermediate filaments (Eckert and Yeagle, Cell Motil. Cytoskeleton 11:24-30, 1988). We have examined this phenomenon by 1) in vitro phosphorylation of isolated PtK1 keratin filaments and 2) combined treatments of PtK1 cells with both acrylamide and agents which elevate intracellular cAMP levels. PtK1 keratins were incubated in gamma-32P-ATP in the presence or absence of cAMP-dependent kinase (A-kinase) and cAMP. Levels of phosphorylation were analyzed by electrophoresis and autoradiography. Phosphorylation of keratin polypeptides (56 kD, 53 kD, 45 kD, 40 kD) occurred without added kinase, suggesting the presence of an endogenous kinase which remains with intermediate filaments in residues of Triton X-100 extracted cells. Phosphorylation levels were increased by A-kinase but not by cAMP alone, indicating the presence of cAMP-dependent phosphorylation sites in addition to sites phosphorylated by the endogenous kinase. To study the possible role of cAMP-dependent phosphorylation in acrylamide-induced aggregation of keratin filaments, we treated cells with acrylamide in the presence of 8-bromo-cAMP (brcAMP), pertussis toxin (PT), isobutylmethylxanthine (IBMX), or forskolin, which increase intracellular cAMP levels. The distribution and phosphorylation levels of keratin filaments, as well as intracellular cAMP levels, were determined for each of these treatments. In addition to aggregation and dephosphorylation of keratin filaments reported previously, treatment of cells with acrylamide alone also results in reduced levels of intracellular cAMP. 8-bromo-cAMP, IBMX, and forskolin prevent acrylamide-induced aggregation of keratin filaments and result in both normal levels of keratin phosphorylation and normal intracellular cAMP levels. PT was apparently ineffective. These observations suggest that 1) PtK1 keratins are phosphorylated by cAMP-dependent kinase and an endogenous, cAMP-independent kinase and 2) alteration of levels of cAMP-dependent phosphorylation may be involved in aggregation of keratin filaments in response to acrylamide.
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    Cell Motility and the Cytoskeleton 17 (1990), S. 309-316 
    ISSN: 0886-1544
    Keywords: digitization ; flagellum ; image analysis ; microcomputer ; simplex ; spermatozoa ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Methods are described for computerized analysis of digitized images obtained by scanning photomicrographs of swimming sperm flagella. After storing a series of image frames in computer memory, the entire series is analyzed automatically. For each sperm image, the sperm head is located to obtain a starting point for analysis of the flagellum. This location is obtained by minimizing image intensity along a model of the sperm head outline. The flagellum is modelled by a series of straight segments of equal length: 0.5 or 1 μm. The angles between these segments are adjusted to give minimum image intensity along the line of the model as well as minimizing smoothing functions. Extensions to analyze a series of images in each frame, and to measure the positions of beads attached to the flagellar microtubules, are also described.
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    Cell Motility and the Cytoskeleton 17 (1990), S. 46-58 
    ISSN: 0886-1544
    Keywords: circumferential microfilament bundles ; intercellular adhesion ; cytoskeleton ; junctional complex ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The junctional complexes in chick retinal pigment epithelial (RPE) cells in situ contain unusually large zonulae adhaerentes (ZAs) composed of subunits termed zonula adhaerens complexes (ZACs). To determine whether the properties of the ZAs differ between RPE cells which contain ZACs, and MDCK cells which lack ZACs, we investi-gated the effects of treatment with trypsin and/or low Ca2+ by transmission electron microscopy and staining for F-actin. Treatment of RPE cells for 1 h with trypsin alone has no apparent effect on the morphology of the ZA in either MDCK or RPE cells. In contrast to the ZAs in MDCK cells, which split after 3 min in low Ca2+, the ZAs in chick RPE cells stay intact even after 2 h, although the intermembrane discs, i.e., the extracellular components of the ZACs, are no longer visible. After 30 min of treatment with trypsin and low Ca2+, the ZAs split in both cell types. The CMBs start to contract, translocate toward the cell interior, and eventually disappear. This process continues even when the RPE cells are returned to normal medium. New ZAs, composed of ZACs, form between RPE cells 3 h after return to normal medium. These findings suggest that the ZACs in the ZAs of RPE cells are not directly responsible for the increase in resistance to low Ca2+. They also show that the ZA-junctions in RPE cells are not only structurally different from those previously examined, but also behave differently in response to experimental manipulation.
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    Cell Motility and the Cytoskeleton 17 (1990) 
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    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
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    Cell Motility and the Cytoskeleton 17 (1990), S. 71-74 
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    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
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    Cell Motility and the Cytoskeleton 17 (1990), S. 59-67 
    ISSN: 0886-1544
    Keywords: Polytoma papillatum ; Megaselia scalaris ; protofilament ; mitosis ; meiosis ; spindle ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The association of incomplete microtubule assemblies with either another incom-plete structure or complete microtubules was studied in two organisms, the phytoflag-ellate Polytoma papillatum and the phorid fly Megaselia scalaris, using transmission electron microscopy. In the alga, hook-shaped appendages on cytoplasmic and spindle microtubules were detected. These resulted from the lateral association of a curved ribbon of protofilaments with the surface of a complete microtubular wall. In the fly, an S-shaped protofilament sheet was found embedded in the kinetochore plate of a prometaphase I spematocyte. Tracing of the S-shaped element towards the spindle pole revealed that it was formed by the lateral junction of two curved protofilament sheets. In all cases, the C-shaped protofilament sheets represented the endings of complete micro-tubules. Incomplete microtubules are generally considered as representing intermediates of microtubule assembly and disassembly. Since high molecular weight proteins are believed to be responsible for maintaining microtubule-microtubule spacing, it is hypo-thesized that the endings of growing and shrinking microtubules are sparsely studded with these proteins; their depletion allows lateral microtubule contacts. In addition, the microtubule-microtubule contacts may be rendered possible by the flexibility of the slender elongated microtubule-associated molecules. Relatively long C-shaped proto-filament appendages (0.6-1.4 μm) were detected in this study. Therefore, it is plausible to assume that the protofilament sheets are stabilized by contact with one another or with an intact tubule wall.
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    Cell Motility and the Cytoskeleton 17 (1990), S. 75-86 
    ISSN: 0886-1544
    Keywords: intermediate filaments ; microtubules ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
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    Notes: Sea urchin spermatozoa, eggs, and embryos were labeled with the universal antibody against the intermediate filament proteins (anti-IFA) described by Pruss et al. [Cell 27:419-428, 1981] and with anti-beta-tubulin. Localization of these antibodies was by indirect immunofluorescence microscopy. Cytoskeleton of unfertilized eggs, prepared according to a procedure adapted from Kane [Exp. Cell Res. 162:495-506, 1986] or as described by Dufresne et al. [Biochem. Cell Biol. 66:780-791, 1988], and reacted with the anti-IFA demonstrate a uniformly stained background except for the nuclear areas, which appear as dark rings. During the first cell cycle, the anti-IFA staining pattern coincides with that of spindle-associated tubulin but not with the cortical pattern of microtubules. Swimming embryos reacted with the anti-IFA show a labeling located on the cilia and within the cytoplasm of each individual cell of the larva. In spermatozoa, the labeling occurs all along the flagellae. Immunoblots of proteins from eggs and embryos reveal one major protein of 117 kDa and sometimes a component of 66 kDa, both of which cosediment with tubulin during the isolation procedure of microtubules described by Vallee and Bloom [Proc. Natl. Acad. Sci. USA 80:6259-6263, 1983]. These data show that proteins homologous to the intermediate filament proteins reported in vertebrate cells are present in both gametes of sea urchins. The specific localization ofthese proteins in the spindle, the flagella, and the cilia suggest that they may play a significant role in the organization and function of the microtubular lattice of the spermatozoa and of the embryo.
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    Cell Motility and the Cytoskeleton 18 (1991), S. 204-214 
    ISSN: 0886-1544
    Keywords: actin-binding ; muscle ; Z-line ; capping ; isoform ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Chicken adult muscle and liver cDNA libraries were screened with a cDNA, α1, previously isolated from a chicken embryo library by screening with antibodies against the α subunit of chicken CapZ. cDNAs with a new coding region, called α2, were found in addition to ones with the α1 coding region. α2 predicts a protein sequence that matches exactly the N-terminal sequence of 5 peptides prepared from CapZ α purified from chicken muscle, while the protein sequence predicted by α1 matches the peptides well, but not exactly. The predicted protein sequences of α1 and α2 are very similar to each other, and they are similar to those of the α subunit of capping protein from Dictyostelium [Hartmann et al., J. Biol. Chem. 163:5254-5254, 1989] and an actin-binding protein from Xenopus [Ankenbauer et al., Nature 342:822-824, 1989]. Other conserved features of the predicted primary and secondary structures are noted. Chicken α1 and α2 are transcribed in all of 7 adult chicken muscle and non-muscle tissues in comparable amounts by Northern analysis. α2 has four poly(A)+ RNA transcripts, one of which is rare in liver. α1 has two transcripts. α1 and α2 are encoded by different single-copy genes by Southern analysis of chicken genomic DNA.
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    Cell Motility and the Cytoskeleton 18 (1991), S. 15-25 
    ISSN: 0886-1544
    Keywords: cytoskeleton ; microfilaments ; immunocytochemistry ; photoreceptors ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Actin has many diverse functions in the outer retina. To help elucidate its organization in this area, we have investigated the extent of its association with the actin cross-linking protein alpha-actinin. Ultrathin sections of chicken retina were double-immunolabelled with monospecific antibodies against actin and alpha-actinin. The highest relative amount of alpha-actinin to actin label was measured in the adherens junctions between the individual retinal pigmented epithelial (RPE) cells and between the photoreceptor and Mueller cells; in the photoreceptor myoid; and in the RPE basal microvilli. The lowest amount was in the Mueller cell microvilli, the RPE apical processes, and in the photoreceptor ellipsoid. It is likely that the areas containing the highest ratio of alpha-actinin to actin labelling are where the actin filaments are most highly cross-linked into bundles and linked to the plasma membrane by alpha-actinin. Actin filaments terminate in these areas, and, except for the myoid region, they are involved in cell-cell or cell-substrate adherens junctions.
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    Cell Motility and the Cytoskeleton 18 (1991), S. 1-14 
    ISSN: 0886-1544
    Keywords: centrin ; centrosome ; pericentriolar lattice ; pericentriolar material ; mitosis ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: In this study, we follow changes in localization of the centrin-related 165,000-Mr protein of PtK2 cells during the cell cycle. This protein is a component of a pericentriolar lattice that consists of pericentriolar satellites, pericentriolar matrix, and basal feet (Baron A.T., and J.L. Salisbury, J. Cell Biol. 107:2669-2678, 1988). By immunofluorescence microscopy, the 165,000-Mr protein is seen as a constellation of pericentrosomal spots. We observe that cells in late G1 and S are characterized by a dense centrosomal focus of spots with additional spots dispersed throughout the cytoplasm. In G2, one bright centrosomal focus of clustered spots is observed. As the cells proceed through prophase this single focus divides, forming two foci that move toward opposite sides of the nucleus. During prometaphase, each polar focus of spots disperses. At metaphase, the spots are distributed throughout each half-cytoplast from the poles to the chromosomes. During anaphase chromosome movement, some spots are seen beside and behind the trailing chromosome arms while others are clustered at the poles. At telo-phase, pericentrosomal spots radiate from the poles to surround each mass of chromatin. In early G1, pericentrosomal spots surround each newly formed nucleus. We conclude that the 165,000-Mr protein is a dynamic component of both the centrosome (pericentriolar matrix) and the mitotic apparatus (spindle matrix).
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    Cell Motility and the Cytoskeleton 18 (1991) 
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    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
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    Cell Motility and the Cytoskeleton 18 (1991), S. 228-240 
    ISSN: 0886-1544
    Keywords: Quin-2/AM ; spermatozoa ; calcium depletion ; motility ; flagellum ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: In order to elucidate the effects of calcium on the movement of human spermatozoa, studies were conducted using motile cells selected by swim-up migration at 37°C in 5% CO2 in air in a synthetic BWW medium containing 1.7 × 10-3 M CaCl2 or BWW without added calcium (BWW-Ca). Preliminary experiments have confirmed that the addition of EGTA (5 × 10-3; 10-2 M) to BWW medium decreased the intracellular calcium concentration ((Ca++)i) of spermatozoa, as measured in cells loaded with a fluorescent Ca++ indicator, Quin-2. Concomitant measurements of (Ca++)i and sperm movement (analysed by videomicrography at 200 f/s at room temperature) were carried out on Quin-2 loaded cells incubated in BWW-Ca medium plus EGTA (10-5 M; 10-4 M; 10-3 M). Under these conditions a decrease in (Ca++)i was observed and associated with a decrease in mean amplitude of lateral head displacement (ALH). Analysis using an automatic analyser (Hamilton Thorn at 37°C) confirmed these results: the percentage of spermatozoa swimming with ALH ≤ 6 μm is decreased when the external free calcium in BWW-Ca is decreased by the addition of 10-5 M, 10-4 M, or 10-3 M EGTA. Flagellar analysis of the sperm population characterized by ALH ≤ 6 μm showed a large proximal curvature of the tail associated with a low propagation wave velocity and a low beat frequency as compared to the spermatozoa with ALH ≤ 6 μm with similar progressive velocities. These characteristics result in a high flagellar beat efficiency (in terms of head displacement per beat). The disappearance of this pattern of movement when intracellular calcium is lowered indicates that calcium plays a complex role in the relationship between curvature and wave propagation. The ability of spermatozoa to modulate their movement in response to an alteration in the intracellular calcium level confirms the role of calcium in controlling flagellar movement in intact cells.
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    Cell Motility and the Cytoskeleton 19 (1991), S. 91-98 
    ISSN: 0886-1544
    Keywords: motion analysis ; motility ; adaptation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Paramecium letraurelia is a ciliated protist that alters its swimming behavior in response to various stimuli. Like the sensory responses of many organisms, these responses in Paramecium show adaptation to continued stimulation. For quantitative studies of the initial response to stimulation. and of the time course of adaptation, we have developed a computerized motion analysis assay that can detect deviations from the normal swimming pattern in a population of cells. The motion of an average of ten cells was quantified during periods ranging from 15 to 60 seconds, with a time resolution of 1/15 seconds. During normal forward swimming, the maximum deviation from a straight-line path was less than 17°. Path deviations above this threshold value were defined as changes in swimming direction. The percentage of total path time that cells spent deviating from forward swimming was defined as percent directional changes (PDC). This parameter was used to construct dose-response curves for the behavioral effects of various externally added cations known to induce behavioral changes and also to show the time course of adaptation to a depolarizing K+ stimulus. This assay is a valuable tool for studies of chemoeffectors or mutations that alter the swimming behavior of Paramecium and may also be applicable to other motile organisms.
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    Cell Motility and the Cytoskeleton 19 (1991), S. 109-120 
    ISSN: 0886-1544
    Keywords: intermediate filaments ; vimentin ; myogenesis ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Desmin and vimentin are two type III intermediate filament (IF) proteins, which can be phosphorylated in vitro by cAMP-dependent kinase (kinase A) and protein kinase C, and the in vitro phosphorylation of these proteins appears to favor the disassembled state. The sites of phosphorylation for desmin and vimentin have been mapped to their amino-terminal headpiece domains; in chicken smooth muscle desmin the most kinase A-reactive residues are ser-29 and ser-35. In this study we have examined the phosphorylation of desmin by the catalytic subunit of kinase A by using anti-peptide antibodies directed against residues 26-36. The antibodies, which we call anti-D26, recognize both native and denatured desmin and can discriminate between intact desmin and those derivatives that do not possess residues 26-36. Pre-incubation of desmin with affinity purified anti-D26 blocks total kinase A catalyzed incorporation of 32P into desmin by 75-80%. When antibody-treated IFs are subjected to phosphorylation, no filament breakdown is observed after 3 hours. Thus anti-D26 antibodies block phosphorylation of IF in vitro. We have also explored the role of desmin phosphorylation in skeletal muscle cell differentiation using these antibodies. Quail embryo cells, induced to differentiate along the myogenic pathway by infection with avian SKV retroviruses expressing the ski oncogene, were microinjected with affinity purified anti-D26 at the mononucleated, myoblast stage. By 24 h post-injection, the vast majority of uninjected cells had fused into multinucleated myotubes, but all microinjected cells were arrested in the process of incorporating into myotubes and remained mononucleated. This observation suggests that kinase A phosphorylation-induced dynamic behavior of the desmin/vimentin IF cytoskeleton may be one of the many cytoskeletal restructuring events that must take place during myoblast fusion.
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    Cell Motility and the Cytoskeleton 17 (1990), S. 187-196 
    ISSN: 0886-1544
    Keywords: axonemal shape changes ; Ca/Ba/Sr ; macrocilia ; Beroë ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Macrocilia of the ctenophore Beroë undergo Ca/Ba/Sr-dependent activation of ciliary beating and microtubule sliding disintegration [Tamm, J. Comp. Physiol. A163:23-31. 1988a: Tamm, Cell Motil. Cytoskeleton 11:126-138, 1988b; Tamm, Cell Motil. Cytoskeleton 12:104-112, 1989: Tamm and Tamm, Proc. Natl. Acad. Sci. U.S.A. 86:6987-6991, 1989]. Here we report that detergent-extracted macrocilia show an ATP-independent conformational change in response to high concentrations of Ca. Ba. or Sr ions. When applied locally by iontophoresis, these ions induce a rapid planar curvature of the distal end of the macrociliary shaft, followed by a slower relaxation to the rest position. Tip curling occurs in a direction opposite to the physiological Ca/Ba/Sr response. When applied uniformly in the bath, a threshold concentration of 10-1 M Sr is required to induce curling of the tip, and the distal ends remain curved. Calmodulin antagonists do not inhibit the tip curling response.Previous workers found that Ca induces changes in the helical shape of isolated doublet microtubules [Miki-Noumura and Kamiya, Exp. Cell Res. 97:451-453, 1976: Miki-Noumura and Kamiya. J. Cell Biol. 81:355-360, 1979; Takasaki and Miki-Noumura. J. Mol. Biol. 158:317-324, 1982] and sperm axonemes [Okuno and Brokaw, Cell Motil. 1:349-362. 1981] and suggested that conformational changes in microtubules may play a role in Ca regulation of ciliary motility. We propose that the Ca/Ba/Sr-induced curling of the macrociliary tip is due to similar helical changes of doublet microtubules, some of which in macrocilia are prevented from sliding by permanent connections (compartmenting lamellae) between adjacent axonemes within the shaft. Although the tip curling response does not appear to be directly relevant to the physiological Ca response of macrocilia, it provides a novel system for investigating Ca-induced conformational changes of microtubules independent of dynein-powered active sliding.
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  • 93
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    Cell Motility and the Cytoskeleton 17 (1990), S. 197-213 
    ISSN: 0886-1544
    Keywords: cell organelles ; MTOC ; development ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: This paper suggests that the formation and structure of the microtubular skeleton of centrioles and basal bodies can be derived from the following simple geometric principle. A closed ring of nine microtubular initiation sites defines (1) a template for the packing of 18 additional microtubular initiation sites, and (2) the shape of nine rigid arms. Upon swivelling of each arm around a point located four initiation sites away on the initial ring, the array unfolds in a manner similar to the opening of an iris diaphragm.As a consequence, the curved shape of the microtubular triplet blades arises together with the clockwise rotational sense of the slanted blades of the centriole or basal body. The final diameter of the centriole (basal body) self-adjusts. Furthermore, the pitch of the triplet blades, the taper of centrioles and basal bodies, and the change of slant of the blades towards the distal end can be derived. In addition, the model points to a method of replication of pro-centrioles (pro-basal bodies). The hypothesis was tested by the fitting of electron microscopical cross sections of centrioles of 3T3 cells to the geometric shapes predicted by the model.
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  • 94
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    Cell Motility and the Cytoskeleton 17 (1990), S. 214-226 
    ISSN: 0886-1544
    Keywords: actin ; cytoskeleton ; dynamic instability ; protozoa ; video microscopy ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Microtubule dynamics has been studied extensively in vitro, but comparatively little information is available on the in vivo behavior of microtubules. Here we report on the assembly, disassembly, and sliding of microtubules in the giant freshwater amoeba, Reticulomyxa. We have found that treating the cell with 0.25% trypsin induces the rapid formation of exceedingly flat areas within the reticulopodial network, allowing for the direct observation of microtubule behavior by DIC optics and computer-enhanced video microscopy. In flattened areas, microtubule sliding occurs at rates of between 1 and 6.5 μm/sec. The average rate of microtubule assembly is 1.6 μm/sec, while microtubule disassembly takes place at about 4 μm/sec and can reach up to 19.5 μm/sec. We also observed many cases where a microtubule forms a hairpin loop and eventually breaks, resulting in bidirectional disassembly from the point of breakage. Our observations demonstrate sliding of cytoplasmic microtubules in vivo. The high rates of microtubule assembly/disassembly in this cell type are difficult to reconcile with conventional views of association and dissociation processes at microtubule ends and suggest unconventional mechanisms for the growth and shrinkage of microtubules.
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  • 95
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    Cell Motility and the Cytoskeleton 17 (1990), S. 227-235 
    ISSN: 0886-1544
    Keywords: mitosis ; kinetochores ; cell division cycle ; protein phosphorylation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Antibodies to both the C-terminal and the N-terminal regions of the 34 kd serinethreonine specific protein kinase, p34cdc2, were used to study the distribution of this protein in dividing cells and isolated chromosomes of the Indian muntjac. p34cdc2 was found to be present throughout the cytoplasm of dividing cells. In addition, a portion of cellular p34cdc2 was localized to the centrosome, kinetochore, and intercellular bridge and along kinetochore-to-pole microtubules during cell division. Tubulin-denuded metaphase kinetochores retained their association with p34cdc2. The detection of p34cdc2 within a variety of domains of the mitotic apparatus, in addition to the previous reported association with the centrosome [Bailly et al., EMBO J. 8:3985-3995, 1989; Raibowol et al., Cell 57:393-401, 1989] suggests that p34cdc2 may play a role in events associated with anaphases A and B as well as with the transition between interphase and mitosis.
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  • 96
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    Cell Motility and the Cytoskeleton 20 (1991), S. 109-120 
    ISSN: 0886-1544
    Keywords: nonmuscle tropomyosin ; Ca++/calmodulin-binding protein ; actin-binding protein ; epitope ; actomyosin ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Monoclonal antibodies, C2, C9, C18, and C21, against chicken gizzard caldesmon (called high molecular weight isoform) were shown to crossreact with a low molecular weight isoform of caldesmon in chicken embryo fibroblasts (CEF). These antibodies were used in a microinjection study to investigate the in vivo function of caldesmon in nonmuscle cell motility. Injected cells did not appear to change their morphology significantly; the cells displayed a flat appearance and were able to ruffle and locomote normally. However, in the C21 injected cells, saltatory movements of granules and organelles appeared to be greatly inhibited. This inhibition of granule movement was reversible, so that by 3 hr after injection, granules in injected cells had already recovered to normal speed. The inhibition of granule movement by C21 antibody was also very specific; the average speeds of granule movement in cells injected with C2, C9, or C18 antibody, or with C21 antibody preabsorbed with caldesmon, were not significantly different from that in uninjected cells. In a previous epitope study, we demonstrated that, of the antibodies used in this study, only C21 antibody was able to compete with the binding of caldesmon to Ca++/calmodulin and to F-actin, although both C21 and C2 antibodies recognized the same carboxyl-terminal 10K fragment of gizzard caldesmon [Lin et al., 1991: Cell Motil. Cytoskeleton 20:95-108]. The caldesmon distribution in C21 injected cells changed from stress-fiber localization to a more diffuse appearance, when the injection was performed at 10-30 mg/ml of C21 antibody. We have previously shown that a monoclonal anti-tropomyosin antibody exhibited motility-dependent recognition of an epitope, and that micro-injection of this antibody specifically inhibited intracellular granule movements of CEF cells [Hegmann et al., 1989: J. Cell Biol. 109:1141-1152]. Therefore, it is likely that tropomyosin and caldesmon may both function in intracellular granule movement by regulating the contractile system in response to [Ca++] change inside nonmuscle cells.
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  • 97
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    Cell Motility and the Cytoskeleton 20 (1991), S. 121-135 
    ISSN: 0886-1544
    Keywords: centrosome ; pericentriciar material ; spindle poles ; MTOCs ; autoimmunity ; autoantibodies ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Human autoimmune sera were screened for the presence of anticentrosome autoantibodies. Two high titer sera were identified that reacted with HeLa, CHO, and PtK2 centrosomes by immunofluorescence, although the fluorescent patterns that were obtained using the two antisera were separate and distinct. Serum obtained from patient IJ contained antibodies that reacted with epitopes present only in mitotic centrosomes; staining of interphase centrosomes was never detected uing IJ antiserum. Immunoblot analysis demonstrated that antibodies present in IJ antiserum reacted with a 190 kD spindle pole antigen. Immunofluorescent staining of cultured mammalian cells demonstrated that antibodies present in serum obtained from patient SPJ reacted with both interphase and mitotic centrosomes. Characterization of SPJ antiserum by immunoblotting demonstrated that antibodies present in the SPJ serum recognized proteins of Mrs of 39, 185, and 220 kD, although the possibility that the 185 kD polypeptide was a proteolytic breakdown product of the 220 kD protein has not been eliminated. Neither antiserum was able to inhibit microtubule nucleation from centrosomes in a lysed cell system in which pure 6S tubulin was added to permeabilized cells following pretreatment of the cells with either SPJ or IJ antiserum. These antisera should be useful probes for studying the biochemistry of the mammalian centrosome.
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  • 98
    ISSN: 0886-1544
    Keywords: cardiac muscle ; actin dynamics ; α-actinin ; vinculin ; microinjection ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: When fluorescently labeled contractile proteins are injected into embryonic muscle cells, they become incorporated into the cells' myofibrils. In order to determine if this exchange of proteins is unique to the embryonic stage of development, we isolated adult cardiac myocytes and microinjected them with fluorescently labeled actin, myosin light chains, α-actinin, and vinculin. Each of these proteins was incorporated into the adult cardiomyocytes and was colocalized with the cells'native proteins, despite the fact that the labeled proteins were prepared from noncardiac tissues. Within 10 min of injection, α-actinin was incorporated into Z-bands surrounding the site of injection. Similarly, 30 sec after injection, actin was incorporated into the entire I-bands at the site of injection. Following a 3-h incubation, increased actin fluorescence was noted at the intercalated disc. Vinculin exchange was seen in the intercalated discs, as well as in the Z-bands throug hout the cells. Myosin light chains required 4-6 h after injection to become incorporated into the A-bands of the adult muscle. Nonspecific proteins, such as fluorescent BSA, showed no association with the myofibrils or the former intercalated discs. When adult cells were maintained in culture for 10 days, they retain the ability to incorporate these contractile proteins into their myofibrils. T-tubules and the sarcoplasmic reticulum could be detected in periodic arrays in the freshly isolated cells using the membrane dye WW781 and DiOC3[3], respectively. In conclusion, the myofibrils in adult, as in embryonic, muscle cells are dynamic structures, permitting isoform transitions without dismantling of the myofibrils.
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  • 99
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    Cell Motility and the Cytoskeleton 21 (1992), S. 132-137 
    ISSN: 0886-1544
    Keywords: microtubules ; vesicles ; cytoplasmic movement ; monoclonal antibody ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A cytoskeletal apparatus is involved in the movement of vesicles, organelles, and gametes in the pollen tube. The function of microfilaments has been defined quite precisely, but the role of microtubules needs to be further clarified. On the basis of immunological and biochemical investigations, we have identified a polypep-tide showing common properties with kinesin, a microtubule-based motor mainly described in nonplant tissues, in the pollen tube of Nicotiana tabacum. Like mammalian kinesin, the kinesin-immunoreactive homolog from Nicotiana tabacum pollen tubes binds to mammalian microtubules in an AMP-PNP dependent manner. The kinesin-like component is likely to be involved in the movement of vesicular material in the growing pollen tube.
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    Cell Motility and the Cytoskeleton 21 (1992) 
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
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