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 journalArticlepeer-review

68 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

Funding

in part by Grants-in-Aid for Cancer Research Science and Culture and a grant from the for a Comprehensive lo-Year Strategy for from the Foundation for Promotion of Takamatsu Cancer Research Fund and the Foundation. J. Yatsunami thanks the Cancer Research, Japan for support of his work at the National Cancer Center Dr. T. Sugimura, National Cancer work and for stimulating discussion. N.I.H. grant GM 28349. This work was supported from the Ministry of Education, Ministry of Health and Welfare Cancer Control, Japan and grants Cancer Research, the Princess Uehara Memorial Life Science Foundation for Promotion of

ASJC Scopus subject areas

  • Molecular Biology
  • Biophysics
  • Biochemistry
  • Cell Biology

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