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  • Molecular Cell Biology  (515)
  • 1975-1979  (515)
  • 1
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 4 (1976), S. 319-327 
    ISSN: 0091-7419
    Keywords: Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: When incoming fibers to a given brain region are damaged and degenerate, the remaining undamaged fibers can, in some cases, form new synapses, and restore physiologically functional circuitry. Synaptic membrane events underlie this reconstruction: the connection between membranes is broken and reformed. In order to understand these membrane events, it is necessary to know the molecular composition of the synapse and the nature of the interaction between pre- and postsynaptic membranes. The synaptic membranes are probably joined by proteins extending from their surfaces. The postsynaptic membrane has on its outer surface an array of lectin receptors, probably glycoproteins. On its inner surface, juxtaposed to the bilayer, the membrane has an electron-dense structure called the postsynaptic density which, from studies on the isolated structure, is composed of a few polypeptides. On the basis of the molecular composition and structure of CNS synapses and ultrastructural studies of the lesion-induced synaptogenesis, some of the underlying dynamic events at synaptic membranes are inferred. New synapses are formed either by reutilization of the old contact sites or by generation of new ones. The protein and carbohydrates in the cleft are enzymatically degraded and a new synapse is generated in response to ingrowing fibers by the addition or reutilization of the specialized proteins of postsynaptic membrane, which differentiate a small segment of the postsynaptic membrane.
    Additional Material: 4 Ill.
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  • 2
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 3 (1975), S. 80-89 
    ISSN: 0091-7419
    Keywords: Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Fluorescent polymers were obtained by oxidizing partly emulsified linolenic acid with different oxidants. The speed of formation of polymers differed for the various oxidants, and the difference was not a simple function of the oxidation potential. The speed of polymerization also depended on the nature of the emulsion.The presence of egg albumen in the emulsion enhanced polymer formation with all oxidants. When the oxidants used are arranged in the order of decreasing speed of polymer formation, the order is different in the presence of albumen from what it is in the absence of albumen.With different oxidation catalysts most antioxidants and amino acids tested enhanced polymerization. In oxidation with ferric ions, with K-dichromate, and without added oxidants the only antioxidants which delayed polymerization were “inhibitors”. “Retarders” enhanced polymerization. With KMnO4 slight delay was caused by some retarders.The findings indicate that not only oxidation catalysts, but also proteins, amino acids, and antioxidants enhance polymerization. The possibility is suggested that in animal cells lipid pigment formation might represent a mechanism for neutralizing free radicals.
    Additional Material: 7 Ill.
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  • 3
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 5 (1976), S. 65-72 
    ISSN: 0091-7419
    Keywords: cell morphology ; Con A receptors ; cytochalasin B ; ionophore ; lectin agglutination ; ligandinduced clustering ; local anesthetics ; microfilament ; microtubule, receptor capping ; vinblastine ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Tertiary amine local anesthetics (dibucaine, Tetracaine, procaine, etc.) modify cell morphology, concanavalin A (Con A)-mediated agglutinability and redistribution of Con A receptors. Con A agglutination of untransformed mouse 3T3 cells was enhanced at low concentrations of local anesthetics, and the dynamics of fluorescent-Con A indicated that ligand-induced clustering was increased in the presence of the drugs. In contast, these drugs inhibited Con A-induced receptor capping on mouse spleen cells. These effects can be duplicated by combinations of vinblastine (or colchicine) and cytochalasin B suggesting that local anesthetics act on microtubule cell surface receptor mobility and distribution. It is proposed that tertiary amine local anesthetics displace plasma membrane-bond Ca2+, resulting in disengagement of microfilament systems from the plasma membrane and increased cellular Ca2+ concentration to levels which disrupt microtubular organization. The possible involvement of cellular Ca2+ in cytoskeletal destruction by local anesthetics was investigated utilizing Ca2+-specific ionophores A23187 and X537A. In media containing Ca2+ and cytochalasin B these ionophores caused effects similar to tertiary amine local anesthetics.
    Additional Material: 2 Ill.
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  • 4
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 3 (1975), S. 261-274 
    ISSN: 0091-7419
    Keywords: Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Highly purified preparations of Streptococcus faecalis ATPase contain a similar but inactive protein detected by prolonged polyacrylamide gel electrophoresis. The inactive protein appears to arise by proteolytic cleavage of the major subunits in the enzyme. By use of a new technique, subunit analysis in SDS gels was performed on the enzyme band and the inactive protein band excised from a polyacrylamide gel after electrophoresis. The results indicated that the ATPase has the composition α3β3γ in which α = 60,000, β = 55,000, and γ = 37,000 daltons. The inactive protein appears to have the composition (f)6 in which f = 49,000 daltons. There is also evidence that the enzyme band contains some slightly modified forms of the ATPase, such as α3β2 (f)γ. The inactive protein lacks the capacity for tight nucleotide binding.Our experiments show that the tight ATPase-nucleotide complex formed in S. faecalis cells (the endogenous complex) behaves differently from the tight complex formed in vitro (the exogenous complex). We prepared a doubly labeled complex containing endogenous 32P-labeled ADP and ATP and exogenous 3H-labeled ADP. We observed that the addition of free nucelotide to the doubly labeled ATPase displaced the exogenous bound ligand from the enzyme but not the endogenous bound nucleotide. We suggest that the displaceable and nondisplaceable forms of the tight ATPase-nucleotide complex correspond to two different conformational states of the enzyme.
    Additional Material: 8 Ill.
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  • 5
    ISSN: 0091-7419
    Keywords: Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: We have recently described a cell type-specific surface (SF) antigen that is deleted in chick fibroblasts transformed by Rous sarcoma virus. SF antigen is a major surface component and makes up about 0.5% of the total protein on normal cultured fibroblasts. The antigen is shed from normal cells and is present in circulation (serum, plasma), and in vivo, also, in tissue boundary membranes. The molecular equivalents of both cellular and serum SF antigen are distinct, large polypeptides, one of which (SF210, MW 210,000) is glycosylated and, on the cell surface, highly susceptible to proteases and accessible to surface iodination. Immunofluorescence and scanning electron microscopy have indicated that the antigen is located in fibrillar structures of the cell surface, membrane ridges, and processes.Human SF antigen is present in human fibroblasts and in human serum. We have recently shown that human SF antigen is identical to what has been known as the “cold-insoluble globulin” and that it shows affinity toward fibrin and fibrinogen. Our results also indicate that loss of the transformation-sensitive surface proteins is due not to loss of synthesis but to lack of insertion of the protein in the neoplastic cell surface. Both normal and transformed cells produce the SF antigen, but the latter do not retain it in the cell surface.The loss of SF antigen, a major cell surface component, from malignant cells creates an impressive difference between the surface properties of normal and malignant cells. The possible significance of SF antigen to the integrity of the normal membrane and its interaction to surrounding structures is discussed.
    Additional Material: 1 Tab.
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  • 6
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 4 (1976), S. 141-159 
    ISSN: 0091-7419
    Keywords: Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The specificity of lactoperoxidase-catalyzed iodination for the proteins of the hepatoma tissue culture cell plasma membrane was examined by histochemical, biochemical, and cell fractionation techniques. Light microscope autoradiography of sectioned cells shows the incorporated label to be localized primarily at the periphery of the cell. Most of this label can be released from the cell by trypsin but not by collagenase or hyaluronidase. The label is recovered from the cells as either monoiodotyrosine or diiodotyrosine after hydrolysis of cell extracts with a mixture of proteolytic enzymes. The label co-purifies during cell fractionation with an authentic liver cell plasma membrane marker enzyme, 5′-nucleotidase. Thus, the incorporated iodide is itself a valid marker for those membrane polypeptides having tyrosine residues accessible to the lactoperoxidase. The polypeptide complexity of the purified plasma membrane was examined by high resolution dodecyl sulfate-polyacrylamide gel electrophoresis. At least 50 polypeptides in the membrane are accessible to iodination. These polypeptides probably represent the bulk of the protein mass of the membrane and iodinating them does not affect cell viability, growth rate, or cell function. Labeling experiments with fucose and glucosamine show that at least nine of the iodinated peptides may be glycoproteins.
    Additional Material: 7 Ill.
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  • 7
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 5 (1976) 
    ISSN: 0091-7419
    Keywords: Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 5 (1976), S. 453-456 
    ISSN: 0091-7419
    Keywords: gating currents ; sodium channels ; pore populations ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Sodium-channel behavior has been modeled in order to determine the answer to the following question: How large must a population of “on-off” Sodium pores be before the inherently random behavior of the individual channels becomes smoothed to yield the expected gating current-conductance relationships which would be predicted from an infinite pore array? Results of this analysis show that for the “opening” situation, an excellent fit was obtained whenever more than about 10 pores were considered. Significant discrepanciesd were observed in the “Closeing” situation, however, for pore arrays of 50 or less. Marked hysteresis is apparent in the behavior of small pore populations.
    Additional Material: 1 Ill.
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  • 9
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 7 (1977), S. 435-442 
    ISSN: 0091-7419
    Keywords: lipoprotein structure ; x-ray scattering ; thermal trasnsitions ; interaction arterial proteoglycans ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The structure and thermal behavior of human serum low-density lipoproteins showing either a high or a low reactivity against a proteoglycan isolated from human arteries have been found to be different from each other. It is suggested that modifcations in the lipoprotein surface structure induced by the physical state of the neutral lipids could modulate the affinity of the macromolecule for the arterial component.
    Additional Material: 4 Ill.
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  • 10
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 7 (1977), S. 515-530 
    ISSN: 0091-7419
    Keywords: breast ; prostate ; carcinoma ; glycoproteins ; organ culture ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: We demonstrate that a technique is available to investigate glycoprotein synthesis in organ cultures of human breast and prostate surgical specimens where the 3-dimensional epithelial cell arrangement remains intact. Malignant breast and prostate epithelium maintained their capacity to synthesize glycoproteins for at least 3 days as followed by the incorporation of [3H] glucosamine into macromolecules. Over 70% of incorporation was by malignant cells as judged by autoradiography. Labeled glycoproteins were released into glandular lumina and consequently into the culture fluid. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed predominantly one group of macromolecules released with an apparent molecular weight of 48,000 ± 6,000 daltons. This glycoprotein was found in all of the breast specimens studied, which included 1 medullary, 1 infiltrating lobular, and 8 infiltrating duct carcinomas. The pattern was independent of the availability of estrogen receptors. A similar glycoprotein was also observed in the culture media from a Grade I and a Grade II well-differentiated infiltrating prostate carcinoma. Incorporation was below the level of detection in 4 of 6 cases of benign prostatic hyperplasia. A more complex pattern of labeled glycoproteins was found in the media of a Grade II and a Grade III poorly-differentiated prostate carcinoma. The established human mammary carcinoma cell line MCF-7 synthesized and released a similar 48,000 molecular weight glycoprotein but additional components with larger molecular weights were also released. An intriguing interpretation that 3-dimensional tissue integrity restricts some glycorprotein synthesis is discussed. Cells grown in 2-dimensional monolayers could escape from such a topographic restriction and express additional families of glycoproteins.
    Additional Material: 9 Ill.
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