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cGMP-dependent protein kinase (cGMP kinase) has been implicated
in the regulation of the cytosolic calcium level
([Ca
Volume 270,
Number 16,
Issue of April 21, pp. 9052-9059, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
]
). In Chinese
hamster ovary (CHO) cells stably transfected with the cGMP kinase
I
(CHO-cGK cells), cGMP kinase suppressed the thrombin-induced
increase in inositol 1,4,5-trisphosphate and
[Ca]
(Ruth, P., Wang,
G.-X., Boekhoff, I., May, B., Pfeifer, A., Penner, R., Korth, M.,
Breer, H., and Hofmann, F. (1993) Proc. Natl. Acad. Sci. U. S. A. 90, 2623-2627). Cholecystokinin activated intracellular
calcium release via a pertussis toxin (PTX)-insensitive pathway in
CHO-cGK cells. cGMP kinase did not attenuate the CCK-stimulated
[Ca
]
. In contrast,
cGMP kinase suppressed calcium influx stimulated by insulin-like growth
factors 1 and 2 (IGF-1 and IGF-2) via PTX-sensitive pathways. The
effects of PTX and cGMP kinase on
[Ca
]
were not
additive. 8-Bromo-cGMP had no effect on
[Ca
]
stimulated by
IGF-1 or IGF-2 in wild type CHO cells. These results suggested that
cGMP kinase inhibited the different signaling pathways by the
phosphorylation of a PTX-sensitive G protein. cGMP kinase
phosphorylated the
subunits of G, G
,
and G
in vitro. Phosphorylation stoichiometry was
0.4 mol of phosphate/mol of G
after reconstitution of
heterotrimeric G
in phospholipid vesicles. The
subunit of G
was also phosphorylated in vivo.
These results show that cGMP kinase blocks transduction of distinct
hormone pathways that signal via PTX-sensitive Gproteins.
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