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The antilipolytic effect of insulin does not require adenylate cyclase or phosphodiesterase action
Author(s) -
Gabbay Robert A.,
Lardy Henry A.
Publication year - 1985
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(85)80179-4
Subject(s) - lipolysis , cyclase , phosphodiesterase , adenylate kinase , medicine , endocrinology , adenosine , adenosine deaminase , insulin , phosphodiesterase inhibitor , biology , chemistry , enzyme , biochemistry , adipose tissue , stimulation , receptor
Insulin antagonized the lipolytic actions of epinephrine in rat epididymal adipocytes when the phosphodiesterase inhibitor, Ro 20‐1724, was present. Adipocytes were depleted of functional cAMP by inhibiting adenylate cyclase with N 6 ‐phenylisopropyladenosine in the presence of adenosine deaminase such that Ro 20‐1724 no longer stimulated lipolysis. The cAMP analogs 8‐thioisopropyl‐cAMP or 8‐thiomethyl‐cAMP, which are resistant to phosphodiesterase hydrolysis, were subsequently added to bypass adenylate cyclase and phosphodiesterase action. Under these conditions, insulin antagonized the lipolytic effects of these analogs, even in the presence of Ro 20‐1724.