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  • 1
    Digitale Medien
    Digitale Medien
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 29 (1994), S. 167-176 
    ISSN: 0886-1544
    Schlagwort(e): NuMA ; spindle ; nuclear matrix ; core filaments ; Life and Medical Sciences ; Cell & Developmental Biology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Medizin
    Notizen: Using a monoclonal antibody 2D3 generated against a kinetochore-enriched human chromosome preparation, we identified a high molecular mass protein with nuclear staining in interphase and polar staining of the pericentriolar region in the mitotic spindle. Initially termed centrophilin, this protein associates with the minus-ends of spindle microtubules (MT) and appears to be important in spindle organization [Tousson et al., 1991: J. Cell Biol. 112:427-440]. Comparison of a partial cDNA sequence obtained for centrophilin with the full length cDNA sequence of nuclear mitotic apparatus protein (NuMA) [Compton et al., 1992: J. Cell Biol. 116:1395-1408; Yang et al., 1992: J. Cell Biol. 116:1303-1317] has indicated that NuMA and centrophilin are the same protein. Using a polyclonal NuMA antibody, we have provided further evidence that NuMA exists as iso-forms as shown by peptide mapping and immunoblots. Sequential fractionation experiments along with immunofluorescence, immunoblotting, and EM immunogold labeling have demonstrated that NuMA isoforms are novel components of nuclear core filaments. Thus, NuMA, a long coiled-coil protein, appears to have dual functions in interphase and mitosis during the cell cycle. In interphase, NuMA likely plays a structural role in the nucleoskeleton that may be important in nuclear organization and functions, whereas in mitosis, NuMA appears to be associated with spindle MT organization and chromosome positioning. © 1994 Wiley-Liss, Inc.
    Zusätzliches Material: 6 Ill.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 5 (1976), S. 497-514 
    ISSN: 0091-7419
    Schlagwort(e): Cytoplasmic microtubule complex ; calcium ; normal and transformed cells ; in vivo control ; effects of trypsin ; Life Sciences ; Molecular Cell Biology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Chemie und Pharmazie , Medizin
    Notizen: Indirect immunoflurescence analyses using antibodieis directed against 6S tubulin have shown an elaborate cytoplasmic microtubule complex (CMTC) in nontransformed cells in culture. The CMTC is strikingly altered in cells that have been transformed spontaneously by viruses or by chemicals. Assembly of microtubules in vitro and in vivo is markedly inhibited in the presence of elevated levels of calcium. Alteration of the surface of normal cells by brief treatment with low concentrations of trypsin initiate a rapid breakdown of cytoplasmic microtubules. Finally, a hypothesis is presented relating microtubule assembly and surface membrane modulation suggesting that calcium is the primary modulating signal.
    Zusätzliches Material: 19 Ill.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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