Vimentin is hyperphosphorylated in primary human fibroblasts treated with okadaic acid

Jun Yatsunami, Hirota Fujiki*, Masami Suganuma, Seiji Yoshizawa, John E. Eriksson, Mark O.J. Olson, Robert D. Goldman

*Corresponding author for this work

Research output: Contribution to journalArticle

66 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)1165-1170
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume177
Issue number3
DOIs
StatePublished - Jun 28 1991

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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