Vimentin is hyperphosphorylated in primary human fibroblasts treated with okadaic acid. |
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| Authors: | J Yatsunami H Fujiki M Suganuma S Yoshizawa J E Eriksson M O Olson R D Goldman |
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| Institution: | Cancer Prevention Division, National Cancer Center Research Institute, Tokyo, Japan. |
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| 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. |
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