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(Received for publication, June
5, 1995; and in revised form, August 8, 1995) We have examined the mechanism for the selective down-regulation
of protein kinase C
Volume 270,
Number 42,
Issue of October 20, 1995 pp. 25115-25120
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
, in
Rat Pituitary GH
C
Cells
(nPKC
) in rat pituitary
GH
C cells responding to thyrotropin-releasing
hormone (TRH) stimulation. Among various low molecular weight protease
inhibitors examined, only a cysteine protease inhibitor (calpain
inhibitor I, N-acetyl-Leu-Leu-norleucinal) blocked the
down-regulation of nPKC. Furthermore, the introduction of a
synthetic calpastatin peptide, an exclusively specific inhibitor of
calpain, into the cells also reduced the down-regulation, suggesting
the involvement of calpain among all the intracellular cysteine
proteases in this process. In accordance, we observed TRH-induced
translocation of m-calpain from the cytosol to the membrane and the
concomitant up-regulation of calpastatin isoforms; presumably, the
former represents activation of the protease initiating the kinase
degradation, while the latter constitutes a negative feedback system
protecting the cells from activated calpain. These results suggest that
in GH
C cells, TRH mobilizes both protease
(m-calpain) and inhibitor (calpastatin) as a strictly regulating system
for the nPKC pathway mediating TRH signals.
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