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  • Cell & Developmental Biology  (2)
  • 1
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 3 (1983), S. 671-682 
    ISSN: 0886-1544
    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.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    BioEssays 7 (1987), S. 173-175 
    ISSN: 0265-9247
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The calpactins are a novel group of proteins associated with the membrane skeleton. The two main forms, calpactin I and II, have been shown to bind to the cytoskeletal proteins actin and spectrin, as well as to anionic phospholipids, which may imply some sort of bridging role. By raising monoclonal antibodies to the heavy and light chains of calpactin I, and to calpactin II, the protein subunits were shown to be coordinately expressed, and the existence of separate calpactin pools hypothesized. Calcium-binding studies suggest that the calpactins may translate Ca2+ signals into cellular responses at the membrane. Structural studies have revealed two distinct domains and are beginning to throw light on heavy--light chain interaction and cytoskeletal attachment.
    Type of Medium: Electronic Resource
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