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 language | English (US) |
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Pages (from-to) | 1165-1170 |
Number of pages | 6 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 177 |
Issue number | 3 |
DOIs | |
State | Published - 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