Vimentin is hyperphosphorylated in primary human fibroblasts treated with okadaic acid.
Vimentin is hyperphosphorylated in primary human fibroblasts treated with okadaic acid.
复制标题
波形蛋白在用冈田酸处理的原代人成纤维细胞中过度磷酸化。
DOI：
10.1016/0006-291x(91)90662-q
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发表时间：
1991
影响因子：
3.1
通讯作者：
Goldman,RD
中科院分区：
文献类型：
--
作者：
Yatsunami,J;Fujiki,H;Suganuma,M;Yoshizawa,S;Eriksson,JE;Olson,MO;Goldman,RD
摘要冈田酸和甲藻毒素-1(35-甲基卡达酸)通过抑制蛋白磷酸酶1和2A的活性，诱导原代人成纤维细胞中一种58 kDa蛋白的过度磷酸化。该蛋白存在于胞核和胞浆中。其等电点为5.3。过度磷酸化的蛋白可与抗波形蛋白的单抗和多克隆抗体反应，但不与抗核蛋白抗体反应。在蛋白磷酸酶2A和蛋白激酶存在的情况下，DIP-1可剂量依赖地刺激Vimentin的磷酸化。
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.