Vimentin is hyperphosphorylated in primary human fibroblasts treated with okadaic acid

A1 Journal article (refereed)


Internal Authors/Editors


Publication Details

List of Authors: Yatsunami, Fujiki, Suganuma, Yoshizawa, Eriksson, Olson, Goldman
Publication year: 1991
Journal: Biochemical and Biophysical Research Communications
Journal acronym: Biochem Biophys Res Commun
Volume number: 177
Issue number: 3
Start page: 1165
End page: 1170
ISSN: 0006-291X


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.

Last updated on 2019-19-08 at 05:27