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  • 1
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 53 (1993), S. 161-168 
    ISSN: 0730-2312
    Keywords: vimentin ; intermediate filament ; protein phosphorylation ; immunoblotting ; scanning densitometry ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The vimentin contents of four mammalian cell lines originating from rat and human tissues were determined by immunoblotting and scanning densitometry. On per cell volume basis, vimentin content in 9L, KD, and HeLa cells was found to be 206.6, 151.6, and 19.1 ng/μl, respectively. A431 cells were devoid of vimentin. Protein phosphorylation was augmented by treatment of 600 nM okadaic acid for 1 h in these cells. During the apparent activation of protein kinases, vimentin became hyperphosphorylated and the phosphorylation level of other nonvimentin phosphoproteins was relatively little affected in 9L and KD cells. In contrast, cytokeratins and other nonvimentin proteins were heavily phosphorylated in OA-treated HeLa and A431 cells. Regression analysis indicated that the relative increase in phosphorylation level of nonvimentin phosphoproteins was inversely correlated to the contents of vimentin in the four cell lines [r2 = -0.985]. These observations strongly suggest that vimentin acts as a phosphate sink by which the effects of “excess kinase activity” inflicted by phosphatases inhibition was attenuated.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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