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J. Biol. Chem., Vol. 266, Issue 6, 3444-3448, Feb, 1991
PA Gruppuso, R Mikumo, DL Brautigan and L Braun
Protein phosphorylation and dephosphorylation are involved in regulation of
cell growth. We tested the hypothesis that the growth inhibitory effect of
transforming growth factor beta 1 (TGF-beta 1) involves activation of
protein phosphatases. Exposure of human keratinocytes in culture to 400 pM
TGF-beta 1 for 48 h led to 80% inhibition of DNA synthesis as measured by
nuclear labeling. Incubation of cultured keratinocytes with 400 pM TGF-beta
1 rapidly activated (within 30 min) protein serine/threonine phosphatase,
measured using phosphorylase as a substrate. Based on several criteria,
including neutralization of activity with specific antibodies and
inhibitor-2, TGF-beta 1-activated phosphorylase phosphatase was identified
as protein phosphatase 1. TGF-beta 1 did not have rapid effects on protein
serine/threonine phosphatase activity (type 2A) measured with histone
phosphorylated by protein kinase C or on protein tyrosine phosphatase
activity. However, protein tyrosine phosphatase was activated at 48 h,
coincident with growth arrest. Differentiation, induced by the combination
of TGF-beta 1 plus calcium or by serum, was not accompanied by further
serine/threonine or tyrosine phosphatase activation. We conclude that
induction of growth arrest in keratinocytes by TGF-beta 1 involves acute
activation of protein phosphatase 1, while activation of protein tyrosine
phosphatase may represent an additional mechanism for maintaining cells in
a growth-arrested state.
Growth arrest induced by transforming growth factor beta 1 is accompanied by protein phosphatase activation in human keratinocytes
Department of Pediatrics, Brown University, Providence, Rhode Island 02912.
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