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Protein phosphatase 2A in stretch‐induced endothelial cell proliferation
Author(s) -
Murata Kohei,
Mills Ira,
Sumpio Bauer E.
Publication year - 1996
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/(sici)1097-4644(19961201)63:3<311::aid-jcb6>3.0.co;2-#
Subject(s) - okadaic acid , phosphatase , cell growth , microbiology and biotechnology , protein kinase a , protein phosphatase 1 , cytosol , chemistry , protein phosphatase 2 , biochemistry , kinase , biology , enzyme , phosphorylation
We previously proposed that activation of protein kinase C is a key mechanism for control of cell growth enhanced by cyclic strain [Rosales and Sumpio (1992): Surgery 112:459–466]. Here we examined protein phosphatase 1 and 2A activity in bovine aortic endothelial cells exposed to cyclic strain. Protein phosphatase 2A activity in the cytosol was decreased by 36.1% in response to cyclic strain for 60 min, whereas the activity in the membrane did not change. Treatment with low concentration (0.1 nM) of okadaic acid enhanced proliferation of both static and stretched endothelial cells in 10% fetal bovine serum. These data suggest that protein phosphatase 2A acts as a growth suppressor and cyclic strain may enhance cellular proliferation by inhibiting protein phosphatase 2A as well as stimulating protein kinase C. © 1996 Wiley‐Liss, Inc.