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  • Articles  (353)
  • Chemistry  (339)
  • fibronectin  (9)
  • calcium  (7)
  • Wiley-Blackwell  (353)
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  • Institute of Physics
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  • 1985-1989  (353)
  • 1980-1984
  • 1970-1974
  • 1987  (182)
  • 1985  (171)
  • Medicine  (353)
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  • Energy, Environment Protection, Nuclear Power Engineering
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  • Articles  (353)
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  • 1985-1989  (353)
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  • 1
    Electronic Resource
    Electronic Resource
    Bending patterns of Chlamydomonas flagella: II. Calcium effects on reactivated Chlamydomonas flagella (1985)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 5 (1985), S. 53-60 
    Details
    ISSN: 0886-1544
    Keywords: calcium ; Chlamydomonas ; flagella ; motility ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Ca2+ has profound effects on the movement of cilia and eukaryotic flagella, including those of Chlamydomonas. Two clear changes seen in Chlamydomonas flagella with changes in Ca2+ are beat frequency and symmetry. Photographic and computer assisted analysis of flagellar bending patterns on a uniflagellate mutant of Chlamydomonas have been used to examine details of the effects of Ca2+ on the movement of ATP-reactivated, demembranated flagella. In addition to the forward mode bending pattern seen at low Ca2+ concentrations (10-9 M), which has a frequency of about 50 Hz and the reverse mode bending pattern seen at high Ca2+ concentrations (10-4 M) with a frequency around 70 Hz, we carefully examined bending patterns in the intermediate Ca2+ concentration range of 1-6.5 × 10-6 M. In this intermediate range, the bending patterns have significantly reduced asymmetry and slightly increased frequency, compared to the motility observed at low Ca2+ concentrations. These observations indicate that changes in these two parameters of motion do not occur in parallel and suggest that the effects of Ca2+ may be a multicomponent process. Physiologically, these changes in the beat pattern at intermediate Ca2+ may signal either (1) the beginning stages of transition to the symmetrical, high-frequency beating seen at high Ca2+, or (2) a more normal forward mode motility for the trans flagellum as suggested by Kamiya and Witman [1984]. No large amplitude bending patterns associated with transitions between forward and reverse mode beating in intact cells were seen at the intermediate Ca2+ concentrations.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970050105
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  • 2
    Electronic Resource
    Electronic Resource
    cAMP-mediated inhibitory effect of calmodulin antagonists on ciliary reversal of ParameciumA part of this work was presented as a poster session at the 3rd International Congress on Cell Biology, Tokyo, 1984. (1987)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 7 (1987), S. 154-159 
    Details
    ISSN: 0886-1544
    Keywords: calcium ; protein phosphorylation ; TFP ; Triton-extracted model ; ciliary orientation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: To explore possible roles of calmodulin in Ca2+-induced ciliary reversal, we tested the effects of calmodulin antagonists on Triton-extracted models of Paramecium. In the extracted models prepared by the method of Naitoh and Kaneko [Science 176:523-524, 1972], the Ca2+ -induced ciliary reversal was not inhibited by calmodulin antagonists, trifluoperazine (TFP), or 5-chloro-l-naphthalenesulphone amide (W-7). However, in the presence of adenosine 3′,5′-cyclic mono-phosphate (cAMP), whose concentration is below the one that alters the ciliary direction, TFP inhibited ciliary reversal and the models swam forward at 10-5 M Ca2+. When the washing medium in the preparation of the extracted models was replaced with one containing MgCl2, the extracted model showed sensitivity to calmodulin antagonists without addition of cAMP; at 10-5 M Ca2+, 40 μM TFP or 100 μM W-7 inhibited the ciliary reversal and the models swam forward. Such effect of antagonists was abolished by an inhibitor of cAMP-dependent protein kinase. On the other hand, addition of cAMP enhanced the inhibitory effect of antagonists. These results suggest that calmodulin antagonists act to increase the extent of cAMP-dependent protein phosphorylation that inhibits the Ca2+ -induced ciliary reversal.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970070207
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  • 3
    Electronic Resource
    Electronic Resource
    Regulation of activation state and flagellar wave form in epididymal rat sperm: Evidence for the involvement of both CA2+ and cAMP (1987)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 8 (1987), S. 324-332 
    Details
    ISSN: 0886-1544
    Keywords: sperm motility ; procaine ; calcium ; cAMP ; flagellum ; epididymis ; TMB-8 ; hyperactivation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Rat sperm from the cauda epididymis exhibit increased motility, longevity, and a distinct circular pattern of flagellar curvature in response to 5 mM procaine-HCI or 0.1 mM 8-(N, N-diethylamino)-octyl-3,4,5-trimethoxybenzoate (TMB-8), reagents that are thought to play a role in the immobilization of free cellular calcium. Triton X-100-extracted sperm models will exhibit the same pattern of motility and curvature as procaine- or TMB-8-activated cells, but only when calcium is removed by a strong chelating agent, and in the pesence of cAMP (3 μM). Demembranated sperm models produced from epididymal rat sperm are quiescent unless cAMP is added. In these sperm models, the presence or absence of free calcium mediates a transition in flagellar curvature. The increased activity of the procaine-treated intact cells was not accompained by a change in cellular ATP content, nor was ATP availability the limiting factor in the quiescent sperm. Therefore, the increased motility produced by procaine is probably mediated by a fall in free intracellular Ca2+ accompained by a rise in cAMP. Our finding that calcium controls the curvature of sperm flagella may explain altered patterns of flagellar beating, such as the hyperactivated motility that sperm exhibit in the female reproductive tract.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970080405
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  • 4
    Electronic Resource
    Electronic Resource
    Ionic control of locomotion and shape of epithelial cells: I. Role of calcium influx (1985)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 5 (1985), S. 123-136 
    Details
    ISSN: 0886-1544
    Keywords: locomotion and shape control ; epithelial cells ; calcium ; reflection-interference contrast-microscopy ; cinematography ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The role of calcium in the induction of locomotion, control of direction of locomotion, and modulation of shape of epithelial cells derived from Xenopus laevis tadpole epidermis is investigated. Local influx of calcium is achieved by electrophoretic release of small amounts of calcium from a micropipette (tip diameter 0.1-0.5 μUm) closely apposed to the cell body or lamella. The cells are made permeable for calcium by calcium ionophore A23187, and they are kept in Ca++-free, Mg++-rich EGTA Ringer. Another method used to induce Ca++ influx is local application of A23187 while cells move in normal culture medium.Influx of Ca++ into the lamella induces a localised increase in thickness and enlargement of the lamella. Stationary cells become active and show movement in the direction of the Ca++ gradient. Fried-egg-shaped cells tend to acquire a semicircular shape and start moving. Moving cells change the direction of their locomotion, following the direction of Ca++ release. Influx of Ca++ in the cell body region induces its contraction concomitant with an increase in lamellar area.These observations suggest the presence of two different Ca++-sensitive components: an actomyosin meshwork in the cell body and an actin gel in the lamella. Influx of Ca++ induces contraction of actomyosin and solation of actin gel. Interaction of these two systems would explain modulation of shape and generation of locomotion in epithelial cells.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970050205
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  • 5
    Electronic Resource
    Electronic Resource
    Effect of microinjectecd calcium-calmodulin on mitosis in PtK2 cells (1987)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 7 (1987), S. 1-9 
    Details
    ISSN: 0886-1544
    Keywords: mitosis ; calcium ; calmodulin ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Calcium and calmodulin are believed in play a significant role in the regulation of mitosis, because they are both localized in the mitotic spindle and because they can potentiate microtubule depolymerization in the test tube and in the living cell. It has been hypothesized, specifically, that calcium-saturated calmodulin drives the shortening of the kinetochore microtubules that must occur during prometaphase, when the chromosomes congress to the metaphase plate, and during anaphase A, when the half-spindles shorten. We have examined the role of calmodulin in mitosis by observing the consequences of calmodulin microinjection on the progress of mitosis and morphology of the mitotic spindle in PtK2 cells. We have found that the injection of excess calcium-saturated calmodulin during early prometaphase significantly prolongs the time required for the cell to go into anaphase, and that neither calcium-depleted calmodulin nor buffer alone produce a similar perturbation. Calcium ion alone produces a similar but much smaller retardation of mitosis. Immunofluorescence and fluorescent analogue cytochemical studies of spindle morphology reveal that the immediate (〈5-min) effect of calcium-saturated calmodulin on prometaphase spindles is a significant shortening of the kinetochore fibers and “interpolar” microtubules but not the astral microtubules. After this perturbation, however, the spindle quickly recovers its normal form. An equivalent transient shortening of the spindle fibers is seen following the injection of calcium chloride solutions but not after the injection of calciumdepleted calmodulin or buffer alone. Taken together, these observations suggest that calcium-saturated calmodulin plays a significant role in the regulation of mitosis, and that this regulatory pathway involves more than spindle fiber shortening.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970070102
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  • 6
    Electronic Resource
    Electronic Resource
    Comparisons of evolutionarily distinct fibronectins: Evidence for the origin of plasma and fibroblast cellular fibronectins from a single gene (1985)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 27 (1985), S. 97-107 
    Details
    ISSN: 0730-2312
    Keywords: fibronectin ; peptide mapping ; ELISA ; evolution ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Plasma and fibroblast cellular fibronectins from three different species were compared for structural similarities and differences. Partial tryptic digestion of either human or chicken plasma and cellular fibronectins yields homologous protease-resistant domains within a species but few homologies between species regardless of the source. Within a species, human or chicken plasma and fibroblast cellular fibronectins are immunologically indistinguishable as determined by the ELISA technique. There is limited immunological cross-reactivity between species. Two-dimensional tryptic peptide maps of fibroblast cellular and plasma fibronectins from the same species are also very similar: 85-95% of the spots on such maps comigrate. When peptide maps from different species are compared no more than 10% of the spots comigrate.Three models for the genetic origin of cellular and plasma fibronectins in vertebrates are considered. A model in which both fibroblast cellular and plasma fibronectins arise from the same gene is the simplest that is consistent with the data.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240270204
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  • 7
    Electronic Resource
    Electronic Resource
    Basement membrane component changes in skeletal muscle transplants undergoing regeneration or rejection (1985)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 27 (1985), S. 337-346 
    Details
    ISSN: 0730-2312
    Keywords: laminin ; fibronectin ; basement membrane ; regeneration ; immune rejection ; skeletal muscle ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The basement membrane of myofibers plays an important role during orderly regeneration of skeletal muscle after injury. In this report, changes in various basement membrane components were analyzed in skeletal muscle grafts undergoing regeneration (autografts) or immune rejection (allografts). The immunofluorescence technique using specific antibodies against laminin, types IV and V collagen, heparan sulfate proteoglycan, fibronectin, in combination with binding of concanavalin A (ConA) was used to monitor basement membranes. In normal muscle, these components were localized in the pericellular region of myofiber corresponding to its basement membrane, After transplantation, the majority of myofibers underwent degeneration as a result of is chemic injury, followed by regeneration from precursor myosatellite cells. Various components of basement membrane zone disappeared from the degenerating myofibers, leaving behind some unidentifiable component that still bound ConA. A new basement membrane appeared around the regenerated myotubes which persisted during maturation of the regenerating muscle, In rejected skeletal muscles, the immunoreactivity of various components persisted even after the disappearance of myotubes and myofiber cytoplasm. In addition, an accumulation of fibronectin was seen throughout the rejected muscle with the onset of immune rejection. These results demonstrate that the major basement membrane components disappear and reappear sequentially during myofiber degeneration and regeneration. Such a turnover is not seen in rejected skeletal muscles. Thus, the myofiber basement membrane is not a static structure as previously thought but one which changes chemically during degeneration and regeneration. This feature of basement membrane may be important in the orderly regeneration of skeletal muscle after injury.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240270404
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  • 8
    Electronic Resource
    Electronic Resource
    Amino acid sequence specificities of an adhesive recognition signal (1985)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 28 (1985), S. 99-104 
    Details
    ISSN: 0730-2312
    Keywords: fibronectin ; cell adhesion ; synthetic peptides ; fibroblasts ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Synthetic peptides derived from the cell-binding domain of fibronectin have previously been found to inhibit fibronectin-mediated adhesion in vitro competitively and reversibly, as well as inhibiting cell migratory events in vivo. The amino acid sequence specificity required for this inhibitory activity has been examined further using variations of the originally identified active peptide sequences. The most active small peptide was found to be the pentapeptide Gly-Arg-Gly-Asp-Ser. Although the tetrapeptide Arg-Gly-Asp-Ser was found to retain substantial activity, it was approximately threefold less active. An “inverted” peptide sequence with these same four amino acids arranged in the mirror sym-metrical sequence Ser-Asp-Gly-Arg was found to be nearly as active as the forward sequence. However, the same inverted tetrapeptide sequence embedded in a synthetic decapeptide derived from a sequence of histocompatibility antigens has minimal activity, suggesting the importance of adjacent sequences in modifying the activity of such peptides. Neither substitution of amino acids of the same charge nor reversal of the positions of the two charged amino acids retains biological activity. Decreasing the spacing between the charged residues also causes a loss of activity. Our results suggest the hypothesis that this adhesive recognition signal consists of a specific arrangement of one acidic and one basic charged group and additional information provided by adjacent amino acids.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240280203
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  • 9
    Electronic Resource
    Electronic Resource
    The cell attachment determinant in fibronectin (1985)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 28 (1985), S. 115-126 
    Details
    ISSN: 0730-2312
    Keywords: cell adhesion ; fibronectin ; peptides ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Fibronectin possesses a domain that interacts with cell surfaces. The ability of fibronectin to promote cell attachment can be duplicated with a short amino acid sequence, glycyl-L-arginyl-glycyl-L-aspartyl-L-serine, taken from that domain. The tripeptide Arg-Gly-Asp appears to be irreplaceable for maintenance of the activity of this peptide, wheareas the serine residue can be replaced with some, but apparently not all, possible residues. This recognition sequence, or a closely related sequence, is present in a number of proteins other than fibronectin that interact with cells. These proteins include collagens, fibrinogen, thrombin, a bacterial surface protein, and two viral proteins, as well as discoidin-I, a protein implicated in the aggregation of Dictyostelium discoideum. A similar sequence is also repeated in some, but not all, fibronectin molecules, making it possible that some fibronectin molecules have more than a single cell attachment site. Synthetic peptides constructed from sequences taken from several of these other proteins have also been shown to promote cell attachment. The tripeptide sequence may, therefore, constitute an ancient cellular recognition mechanism common to many proteins.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240280205
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  • 10
    Electronic Resource
    Electronic Resource
    Immunochemical and biochemical characterization of a glioma-associated extracellular matrix glycoprotein (1985)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 28 (1985), S. 183-195 
    Details
    ISSN: 0730-2312
    Keywords: extracellular matrix ; glioma-associated glycoprotein ; fibronectin ; GMEM ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: A novel human glioma-associated extracellular matrix (ECM) glycoprotein has been identified by murine monoclonal antibody 81C6. The glycoprotein, designated GMEM, is expressed in the ECM of glioma and mesenchymal cell cultures, in the perivascular matrix of endothelial proliferations of human gliomas, and in the stroma of human glioma xenografts in athyrnic mice, where it has been used as a target antigen for monoclonal antibody tumor localization and radioimaging. We report here on the immunochemical and biochemical characterization of GMEM. Polyacrylamide gel analysis of immunoprecipitated [3H]-leucine- and [3H]-glucosamine-labeled ECM from the human glioma cell line U-251MG has shown that GMEM is a high-molecular-weight macromolecule (Mr ∼ 1,000,000) composed of Mr ∼ 230,000 disulfide-bonded glycoprotein subunits. Immunoprecipitation, immunoblot, and one-dimensional peptide map analysis have shown that GMEM is distinct from human fibroblast and plasma fibronectin. These results support previous immunohistology and absorption analysis findings, indicating that GMEM is distinct from fibronectin, laminin, and glycosaminoglycans secreted by U-251MG.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240280302
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