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Inhibitory effects of cyclic‐AMP dependent protein kinase on guanylate cyclase activity in rat cerebellum
Author(s) -
Kumakura Konosuke,
Battaini Fiorenzo,
Hofmann Madeleine,
Spano Pier Franco,
Trabucchi Marco
Publication year - 1978
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(78)81110-7
Subject(s) - clinical pharmacology , pharmacology , molecular pharmacology , medicine , receptor
Guanylate cyclase (EC 4.6.1.2) the enzyme responsible for the formation of cyclic GMP from GTP, has been studied in homogenates or both supernatant and particulate fractions of several tissues [l-8]. Recently, various authors suggested that soluble and particulate guanylate cyclase have different kinetic properties and molecular size [9-l I] , and that the different forms of the enzyme may be independently regulated. Nevertheless, the regulatory mechanisms of guanylate cyclase activity remain unclear, although the importance of Ca2+ has been demonstrated in many tissues [12-l 51. In the present study we observed an inhibitory effect of 3’,5’cyclic adenosine monophosphate (cyclic AMP) dependent protein kinase (ATP, protein phosphotransferase (EC 2.7.1.37)) on guanylate cyclase activity in rat cerebellar homogenates. A possible regulatory mechanism of guanylate cyclase is proposed.