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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 3 (1983), S. 405-417 
    ISSN: 0886-1544
    Keywords: vinculin ; focal contacts ; microfilaments ; transformation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Talin is a recently identified cytoskeletal protein with a polypeptide molecular weight of 215,000 daltons. In cultured fibroblasts talin has been localized by immunofluorescence in adhesion plaques (focal contacts), in the ruffling membranes and leading lamellae of the cell periphery, and in fibrillar patterns that align with microfilament bundles and/or with cell surface fibronectin. These cellular locations suggest that the protein could function either in the attachment of microfilaments to the plasma membane or in the organization of microfilaments close to membrane attachment sites. Cell transformation by viruses such as Rous sarcoma virus disrupts the normal organization of talin, and in most transformed cells talin appears distributed diffusely through the cytoplasm. In a few cells talin is detected in doughnut-shaped aggregates, as a ring surrounding a central core of actin. The significance of these structures is uncertain, but in some cells the individual structures will condense to form much larger aggregates with a striking appearance when viewed by immunofluoresence microscopy.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-0878
    Keywords: Brain spectrin ; Cell interactions ; Cytoskeleton ; Neural cell adhesion molecule N-CAM ; Neural cell culture
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary N-CAM180, the molecular form of the three neural cell adhesion molecules (N-CAM) with the largest cytoplasmic domain, is accumulated at sites of cell-cell contact (cell bodies, neurites, growth cones) in cultures of neuroblastoma and cerebellum. At these sites the cytoskeletonmembrane linker protein brain spectrin and actin are also accumulated. Brain spectrin copurifies with N-CAM180 by immunoaffinity chromatography and binds specifically to N-CAM180 but not to N-CAM140 or N-CAM120 in a solid-phase binding test. These observations indicate an association of N-CAM180 with the cytoskeleton in vivo. This association may underlie the reduced lateral mobility of N-CAM180 in the surface membrane compared to N-CAM140 (Pollerberg et al. 1986). Together with the fact that N-CAM180 is only expressed after termination of neuron migration in vivo (Persohn and Schachner, unpublished) these results suggest a role for N-CAM180 in stabilization of cell contacts.
    Type of Medium: Electronic Resource
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