Beta-adrenergic regulation of a myocardial actin gene via a cyclic AMP-independent pathway.
作者： N.H. Bishopric , B Sato , K.A. Webster
DOI: 10.1016/S0021-9258(19)36778-X
关键词:
摘要: The skeletal alpha-actin gene encodes a major component of the embryonic cardiac sarcomere that is strongly and selectively re-induced during beta-adrenoceptor-mediated hypertrophy in neonatal rat myocytes. We present evidence beta-adrenergic induction this mediated, not by cAMP, but calcium-dependent pathway involving ryanodine-sensitive calcium stores. Nifedipine-induced blockade plasma membrane L-type entry channel prevented mRNA isoproterenol. Activation dihydropyridine agonist Bay K8644 independently induced mRNA, as did cholera toxin-mediated activation Gs. Induction compounds directly elevate cAMP was weak relative to their effects on other cAMP-dependent phenomena required entry. In addition, selective inhibition protein kinase A with KT5720 block alpha-actin. Calcium ionophore A23187 induce actin, its Ryanodine had bimodal effects: 10(-10) M ryanodine whereas 10(-6) actin stimuli. postulate stimulation requires G-protein-coupled compartmentalized release manner independent cAMP/protein signal pathway.
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