Cytoskeletal properties and endogenous degradation of glial fibrillary acidic protein and vimentin in cultured human glioma cells.
作者： A. Paetau , I. Virtanen
DOI: 10.1007/BF00687041
关键词:
摘要: The cytoskeletal properties and endogenous degradation of intermediate filaments in cultured human glioma cells (U-251MG) were studied using monoclonal antibodies immunohistochemical immunochemical methods. Both glial fibrillary acidic protein (GFAP)- vimentin-antibodies gave a fibrillar cytoplasmic staining the cells, double immunofluorescence experiments showed presence both types same cells. GFAP vimentin could also be located to typical coiling perinuclear bundles after vinblastine treatment cultures. In detergent-resistant, adherent cytoskeletons persisted as arrays. Scanning transmission electron microscopy that only left domain. Electrophoretic analysis, combined with immunoblotting method, revealed two major detergent-resistant polypeptides molecular weights 51 kD 58 kD, vimentin, respectively. On other hand, neither nor detected detergent extracts Detergent-extraction low ionic strength medium well inclusion Ca2+ into extraction resulted rapid vimentin. These conditions produced different, partially soluble, lower MW immunoreactive by technique. Interestingly, soluble intact results indicate have closely similar physicochemical including nearly quantitative localization filaments, rearrangement upon microtubule disruption, resistance extractions detergents. Proteolytic proteins can induced protease activated Ca2+.
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