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Vimentin is hyperphosphorylated in primary human fibroblasts treated with okadaic acid
J Yatsunami1, H Fujiki, M Suganuma
1Cancer Prevention Division, National Cancer Center Research Institute, Tokyo, Japan.
Biochemical and Biophysical Research Communications
|June 28, 1991
Abstract:
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.