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S‐100b protein regulates the activity of skeletal muscle adenylate cyclase in vitro
Author(s) -
Fanò G.,
Fulle S.,
Torre G.Della,
Giambanco I.,
Aisa M.C.,
Donato R.,
Calissano P.
Publication year - 1988
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(88)80363-6
Subject(s) - adenylate kinase , cyclase , skeletal muscle , chemistry , gene isoform , in vitro , enzyme , growth hormone releasing hormone receptor , medicine , biochemistry , endocrinology , biology , gene , cancer , breast cancer , hormone receptor
We have investigated the effect of the b isoform of S‐100 proteins on adenylate cyclase activity of rat skeletal muscle. S‐100b inhibits the adenylate cyclase activity in the presence of Mg 2+ (5.0–50 mM), while it activates the same enzyme in the presence of Ca 2+ (0.1–1.0 mM) dose‐dependently in both cases. S‐100b counteracts the stimulatory effect of NaF on adenylate cyclase in the presence of Mg 2+ and the inhibitory effect of RMI 12330 A in the presence of Ca 2+ .