Vimentin is hyperphosphorylated in primary human fibroblasts treated with okadaic acid

Biochem Biophys Res Commun. 1991 Jun 28;177(3):1165-70. doi: 10.1016/0006-291x(91)90662-q.

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

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Blotting, Western
  • Ethers, Cyclic / pharmacology*
  • Fibroblasts / drug effects
  • Fibroblasts / metabolism
  • Humans
  • Kinetics
  • Marine Toxins / pharmacology
  • Molecular Weight
  • Okadaic Acid
  • Phosphoprotein Phosphatases / antagonists & inhibitors
  • Phosphorylation
  • Protein Phosphatase 1
  • Protein Phosphatase 2
  • Pyrans / pharmacology
  • Vimentin / isolation & purification
  • Vimentin / metabolism*

Substances

  • Ethers, Cyclic
  • Marine Toxins
  • Pyrans
  • Vimentin
  • Okadaic Acid
  • dinophysistoxin 1
  • Phosphoprotein Phosphatases
  • Protein Phosphatase 1
  • Protein Phosphatase 2