Vimentin is hyperphosphorylated in primary human fibroblasts treated with okadaic acid

Yatsunami, Fujiki, Suganuma, Yoshizawa, John Eriksson, Olson, Goldman

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    Okadaic acid and dinophysistoxin-1 (35-methylokadaic acid) induced hyperphosphorylation of a 58 kDa protein in primary human fibroblasts, due to inhibition of protein phosphatase 1 and 2A activities. The protein was present in the nuclear and cytosolic fractions. Its pI was 5.3. The hyperphosphorylated protein reacted with monoclonal and polyclonal anti-vimentin antibodies, but not with anti-nucleolin antibody. Phosphorylation of vimentin was stimulated in vitro by dinophysistoxin-1 dose-dependently in the presence of protein phosphatase 2A and protein kinases.
    Original languageUndefined/Unknown
    Pages (from-to)1165–1170
    JournalBiochemical and Biophysical Research Communications
    Issue number3
    Publication statusPublished - 1991
    MoE publication typeA1 Journal article-refereed

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