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Activation of protein kinase C attenuates the cyclic GMP responses to C‐type natriuretic peptide in cultured mouse astrocytes
Author(s) -
Yeung V.T.F.,
Ho S.K.S.,
Cockram C.S.,
Lee C.M.,
Nicholls M.G.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81298-z
Subject(s) - protein kinase c , staurosporine , activator (genetics) , phorbol , natriuretic peptide , npr2 , tetradecanoylphorbol acetate , inhibitory postsynaptic potential , peptide , endocrinology , medicine , chemistry , protein kinase a , neuropeptide , npr1 , kinase , biology , biochemistry , receptor , heart failure
C‐type natriuretic peptide (CNP), a recently discovered natriuretic peptide, has a potent stimulatory effect on cyclic GMP (cGMP) formation in cultured mouse astrocytes. Pretreatment of astrocytes with phorbol 12‐myristate 13‐acetate (PMA), an activator of protein kinase C (PKC). attenuated CNP‐induced cGMP responses in a dose‐dependent manner, with a half‐maximal inhibitory concentration of 6 nM, whereas the inactive phorbol ester analog, 4α‐phorbol 12,13‐didecanoate, was without effect. In the presence of staurosporine, a PKC inhibitor, the inhibitory effect of PMA on CNP‐stimulated cGMP production was reversed. These results suggest that PKC is an inhibitory modulator of CNP‐stimulated cGMP responses in astrocytes and that CNP may interact with neuropeptides which stimulate PKC.