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  • Life and Medical Sciences  (43)
  • 2000-2004
  • 1990-1994  (19)
  • 1985-1989  (17)
  • 1965-1969  (7)
  • 1
    Electronic Resource
    Electronic Resource
    A histological and ultrastructural study of germinal differentiation of interstitial cells arising from gland cells in Hydra viridis (1966)
    New York, NY : Wiley-Blackwell
    Journal of Morphology 120 (1966), S. 1-8 
    Details
    ISSN: 0362-2525
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Gland cells of the gastrodermis of Hydra when isolated from the epidermis are capable of dedifferentiating into interstitial cells. Under proper environmental conditions these interstitial cells are capable of undergoing meiotic divisions and forming normal gametes. This dedifferentiation and redifferentiation sequence has been studied at the level of the light and electron microscope. It is concluded that in Hydra there is no specific germinal cell line determined during embryogeny, and that a somatic cell under proper environmental conditions can be induced to undergo meiosis.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jmor.1051200102
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  • 2
    Electronic Resource
    Electronic Resource
    The fine structure of the Limulus optic nerve (1968)
    New York, NY : Wiley-Blackwell
    Journal of Morphology 125 (1968), S. 61-70 
    Details
    ISSN: 0362-2525
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Two complete composite photographs of the optic nerve of Limulus, made by electron microscopy, reveal the presence of neurosecretory granules in the large axons of the rudimentary eye neurons. The number of intermediate sized, (3-7 μ), of eccentric cells corresponds with the number of ommatidia as expected, but only their sheath of Schwann cells show an intimate interfolding. Based on the number of fine axons within the nerve each ommatidium has an average of 12-13 retinular cells. The diameter of their fibers is between 0.2 and 3 μ although the majority are between 1 and 1.5 μ. They are aggregated into bundles of six to seven fibers by the sheath cells although some bundles contain only two, others as many as 181 fibers. There is no indication in these studies that retinular cell axons within a bundle are associated with the same, adjacent, or other pattern of ommatidia. The photographs suggest that physiological activity in retinular cell axons might be detected most easily in the smallest bundles because they contain the fewest, but the larger retinular cell axons.
    Additional Material: 1 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jmor.1051250104
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  • 3
    Electronic Resource
    Electronic Resource
    Excretion and ultrastructure of the antennal gland of the fiddler crab Uca mordaxThis work was supported by grant AMO 9975-01 of the National Institutes of Health, Bethesda, Maryland. (1968)
    New York, NY : Wiley-Blackwell
    Journal of Morphology 125 (1968), S. 473-495 
    Details
    ISSN: 0362-2525
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Function and ultrastructure of the excretory organs (antennal glands) of the shore crab Uca mordax were investigated. The crabs were maintained at three different salinities: 50%, 100% and 200% seawater. In spite of previous reports to the contrary, the investigation showed that the powerful osmoregulatory ability found in Uca mordax is not due to participation of the antennal glands. Freezing point depression of urine under all conditions was found to be slightly less than that of the hemolymph, indicating a slightly hypoosmotic urine. It was further found that the antennal gland is extremely effective in resorbing sodium from the filtrate. The higher the salinity to which the crabs were acclimated the lower the sodium concentration in the urine. No water was resorbed from the filtrate as shown by the fact that the inulin U/P ratio remained unity regardless of the salinity to which the crabs were adapted. Electronmicroscopy of the antennal glands revealed that the coelomosac cells are similar to the podocytes described in the crayfish by Kümmel ('64), and the coelomosac appears to be a typical filtration organ. The cells of the labyrinth showed brush border and very elaborate basal infoldings with numerous mitochondria. The deep cytoplasmic infoldings which represent interdigitations with neighboring cells may be correlated with the effective sodium reabsorption in the labyrinth, but apparently not with water movement.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jmor.1051250406
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  • 4
    Electronic Resource
    Electronic Resource
    Mean weights of chick embryos correlated with the stages of Hamburger and Hamilton (1968)
    New York, NY : Wiley-Blackwell
    Journal of Morphology 124 (1968), S. 79-82 
    Details
    ISSN: 0362-2525
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A total of 1125 normal chick embryos, representing 25 each of the 45 stages of Hamburger and Hamilton, were removed, fixed in Bouin's solution, stored in 70% ethanol and weighed with a semi-micro analytical balance. Entire blastoderms of stages 1-8 were weighed, whereas only embryos-proper were weighed in stages 9-45. As a consequence, results constituted two groups, each of which showed a geometric rate of growth marked only by minor deviations which were related to specific events of normal growth and development.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jmor.1051240105
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  • 5
    Electronic Resource
    Electronic Resource
    Distribution of phosphorylated spindle-associated proteins in the diatom Stephanopyxis turris (1989)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 12 (1989), S. 33-41 
    Details
    ISSN: 0886-1544
    Keywords: phosphorylation ; MPM-2 ; mitotic spindle ; microtubule-associated protein ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Mitotic spindles isolated from the diatom Stephanopyxis turris become thiophosphorylated in the presence of ATPγS at specific locations within the mitotic apparatus, resulting in a stimulation of ATP-dependent spindle elongation in vitro. Here, using indirect immunofluorescence, we compare the staining pattern of an antibody against thiophosphorylated proteins to that of MPM-2, an antibody against mitosis-specific phosphoproteins, in isolated spindles. Both antibodies label spindle poles, kinetochores, and the midzone. Neither antibody exhibits reduced labeling in salt-extracted spindles, although prior salt extraction inhibits thiophosphorylation in ATPγS. Furthermore, both antibodies recognize a 205 kd band on immunoblots of spindle extracts. Microtubule-organizing centers and mitotic spindles label brightly with the MPM-2 antibody in intact cells. These results show that functional mitotic spindles isolated from S. turris are phosphorylated both in vivo and in vitro. We discuss the possible role of phosphorylated cytoskeletal proteins in the control of mitotic spindle function.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970120105
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  • 6
    Electronic Resource
    Electronic Resource
    Epitope mapping of monoclonal antibodies against caldesmon and their effects on the binding of caldesmon to Ca++/calmodulin and to actin or actin-tropomyosin filaments (1991)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 20 (1991), S. 95-108 
    Details
    ISSN: 0886-1544
    Keywords: actomyosin ; smooth muscle contraction ; nonmuscle cell motility ; microinjection ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The effects of monoclonal anti-caldesmon antibodies, C2, C9, C18, C21, and C23, on the binding of caldesmon to F-actin/F-actin-tropomyosin filaments and to Ca++/calmodulin were examined in an in vitro reconstitution system. In addition, the antibody epitopes were mapped by Western blot analysis of NTCB (2-nitro-5-thiocyanobenzoic acid) and CNBr (cyanogen bromide) fragments of caldesmon. Both C9 and C18 recognize an amino terminal fragment composed of amino acid residues 19 to 153. The C23 epitope lies within a fragment ranging from residues 230 to 386. Included in this region is a 13-residue repeat sequence. Interestingly this repetitive sequence shares sequence similarity with a sequence found in nuclear lamin A, a protein which is also recognized by C23 antibody. Therefore, it is likely that the C23 epitope corresponds to this 13-residue repeat sequence. A carboxyl-terminal 10K fragment contains the epitopes for antibodies C2 and C21. Among these antibodies, only C21 drastically inhibits the binding of caldesmon to F-actin/F-actin-tropomyosin filaments and tc Ca++/calmodulin. When the molar ratio of monoclonal antibody C21 to caldesmon reached 1.0, a maximal inhibition (90%) on the binding of caldesmon to F-actin filaments was observed. However, it required double amounts of C21 antibody to exhibit a maximal inhibition of 70% on the binding of caldesmon to F-actin-tropomyosin filaments. These results suggest that the presence of tropomyosin in F-actin enhances caldesmon's binding. Furthermore, C21 antibody also effectively inhibits the caldesmon binding to Ca++/calmodolin. The kinetics of C21 inhibition on caldesmon's binding to Ca++/calmodulin is very similar to the inhibition obtained by preincubation of caldesmon with free Ca++/calmodulin. This result suggests that there is only one Ca++/calmodulin binding domain on caldesmon and this domain appears to be very close to the C21 epitope. Apparently, the Ca++/calmodulin-binding domain and the actin-binding domain are very close to each other and may interfere with each other. In an accompanying paper, we have further demonstrated that microinjection of C21 antibody into living chicken embryo fibroblasts inhibit intracellular granule movement, suggesting an in vivo interference with the functional domains [Hegmann et al., 1991: Cell Motil. Cytoskeleton 20:109-120].
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970200203
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  • 7
    Electronic Resource
    Electronic Resource
    Protein phosphorylation and dynamics of cytoskeletal structures associated with basal bodies in Paramecium (1987)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 8 (1987), S. 44-54 
    Details
    ISSN: 0886-1544
    Keywords: monoclonal antibody ; phosphoproteins ; basal bodies ; morphogenesis ; Paramecium ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The presence of phosphorylated proteins associated with microtubule organizing centers in tissue culture cells during mitosis has been demonstrated by the use of monoclonal antibodies raised against mitotic HeLa cells [Vandre et al., Proc. Natl. Acad. Sci. U.S.A. 81:4439-4443, 1984]. We report here that in Paramecium two of the mitosis specific antibodies, MPM-1 and MPM-2, decorate throughtout the cell cycle all the microtubule organizing centers (MTOCs) located in the cortex and in the oral apparatus (gullet). Immuno-electron microscopy showed that these antibodies labeled the electron-dense material surrounding basal bodies from which several microtubule networks as well as kinetodesmal fibers originate. During mitosis, these antibodies also stained other cortical cytoskeletal structures, the kinetodesmal fibers (MPM-1 and MPM-2) and the epiplasm (MPM-1). Among the different polypeptides recognized by the antibodies on immunoblots, three major ones of 60, 63, and 116 kDa were found to be common to the cortex (where several thousand ciliary basal bodies are anchored) and the oral apparatus (which comprises several hundred basal bodies around which various arrays of cytoplasmic microtubules are organized). Alkaline phosphatase treatment abolished the immunoreactivity of the polypeptides and the labeling observed by immunofluorescence. These results demonstrate that phosphorylated proteins are associated with all the known active microtubule organizing centers present in the cortex throughout the cell cycle of Paramecium. Furthermore they indicate that in Paramecium phosphorylation of proteins could also be involved in the cell cycle dependent dynamics of cortical cytoskeletal structures other than microtubules.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970080107
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  • 8
    Electronic Resource
    Electronic Resource
    Management of polyamine pools and the regulation of ornithine decarboxylase (1990)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 44 (1990), S. 199-205 
    Details
    ISSN: 0730-2312
    Keywords: polyamine synthesis ; polyamine transport ; ornithine decarboxylase control ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The management of polyamine synthesis and polyamine pools differs fundamentally from that of most other small molecular-weight endproducts. The polyamines are vital to growth and important cellular functions, but they are toxic in excess. I argue here that their multivalent cationic character, leading to binding to cell constituents, precludes fluent feedback inhibition of synthesis. This has led to the development of elaborate alternative regulatory mechanisms controlling ornithine decarboxylase, the key initial enzyme of the pathway. Poorly regulated polyamine synthesis and the toxicity of polyamines impose upon cells a need to control uptake and to dispose of excess polyamines. Recent data on polyamine transport suggest unorthodox mechanisms of accomplishing these functions.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240440402
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  • 9
    Electronic Resource
    Electronic Resource
    Modulation of type α transforming growth factor receptors by a phorbol ester tumor promoter (1985)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 27 (1985), S. 23-30 
    Details
    ISSN: 0730-2312
    Keywords: receptor ; epidermal growth factor ; transforming growth factors ; receptor regulation ; tumor-promoting phorbol esters ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Epidermal growth factor (EGF) and an EGF-like transforming growth factor (eTGF) from retrovirally transformed cells bind to a common receptor type in A431 cells. We have investigated the effects of the tumor promoter phorbol myristate acetate [PMA] on EGF/eTGF receptors in intact A431 cells. Treatment with PMA at 37°C induces a complete loss of high-affinity (Kd = 35-50 pM) binding sites for eTGF and EGF on the cell surface of A431 cells. This effect is half-maximal at 0.1 nM PMA, exhibits rapid kinetics, and persists for at least 4 hr in the presence of PMA. eTGF and PMA added to intact A431 cells induce the phosphorylation of immunoprecipitable 170kd EGF /eTGF receptors. The EGF/ eTGF receptor isolated from control cells was found to contain phosphoserine and phosphothreonine. PMA and eTGF caused a marked increase in the level of these two phosphoamino acids. In addition, eTGF but not PMA caused the appearance of phosphotyrosine in the EGF/eTGF receptor in vivo. We conclude that the tumor-promoting phorbol diester regulates both the affinity and phosphorylation state of the A431 cell receptor for the type α transforming growth factors, eTGF and EGF.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240270104
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  • 10
    Electronic Resource
    Electronic Resource
    Ankyrin and synapsin: Spectrin-binding proteins associated with brain membranes (1985)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 29 (1985), S. 157-169 
    Details
    ISSN: 0730-2312
    Keywords: spectrin ; ankyrin ; synapsin ; membrane skeleton ; tubulin ; secretion ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Brain membranes contain an actin-binding protein closely related in structure and function to erythrocyte spectrin. The proteins that attach brain spectrin to membranes are not established, but, by analogy with the erythrocyte membrane, may include ankyrin and protein 4.1. In support of this idea, proteins closely related to ankyrin and 4.1 have been purifed from brain and have been demonstrated to associate with brain spectrin. Brain ankyrin binds with high affinity to the spectrin beta subunit at the midregion of spectrin tetramers. Brain ankyrin also has binding sites for the cytoplasmic domain of the erythrocyte anion channel (band 3), as well as for tubulin. Ankyrins from brain and erythrocytes have a similar domain structure with protease-resistant domains of Mr = 72,000 that contain spectrin-binding activity, and domains of Mr = 95,000 (brain ankyrin) or 90,000 (erythrocyte ankyrin) that contain binding sites for both tubulin and the union channel. Brain ankyrin is present at about 100 pmol/mg membrane protein, or about twice the number of copies of spectrin beta chains. Brain ankyrin thus is present in sufficient amounts to attach spectrin to membranes, and it has the potential to attach microtubules to membranes as well as to interconnect microtubules with spectrin-associated act in filaments.Another spectrin-binding protein has been purified from brain membranes, and this protein cross-reacts with erythrocyte 4.1. Brain 4.1 is identical to the membrane protein synapsin, which is one of the brain's major substrates for cAMP-dependent and Ca/calmodulin-dependent protein kinases with equivalent physical properties, immunological cross-reaction, and peptide maps. Synapsin (4.1) is present at about 60 pmol/mg membrane protein, and thus is a logical candidate to regulate certain protein linkages involving spectrin.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240290210
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