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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Blotting, Western
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Ethers, Cyclic / pharmacology*
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Fibroblasts / drug effects
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Fibroblasts / metabolism
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Humans
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Kinetics
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Marine Toxins / pharmacology
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Molecular Weight
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Okadaic Acid
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Phosphoprotein Phosphatases / antagonists & inhibitors
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Phosphorylation
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Protein Phosphatase 1
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Protein Phosphatase 2
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Pyrans / pharmacology
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Vimentin / isolation & purification
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Vimentin / metabolism*
Substances
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Ethers, Cyclic
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Marine Toxins
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Pyrans
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Vimentin
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Okadaic Acid
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dinophysistoxin 1
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Phosphoprotein Phosphatases
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Protein Phosphatase 1
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Protein Phosphatase 2