Compartmentalization of Cardiac β-Adrenergic Inotropy Modulation by Phosphodiesterase Type 5 | Zendy

Eiki Takimoto | Zendy; Diego Belardi | Zendy; Carlo G. Tocchetti | Zendy; Susan Vahebi | Zendy; Gianfrancesco Cormaci | Zendy; Elizabeth Ketner | Zendy; An L. Moens | Zendy; Hunter C. Champion | Zendy; David A. Kass | Zendy

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Compartmentalization of Cardiac β-Adrenergic Inotropy Modulation by Phosphodiesterase Type 5

Author(s) -

Eiki Takimoto,

Diego Belardi,

Carlo G. Tocchetti,

Susan Vahebi,

Gianfrancesco Cormaci,

Elizabeth Ketner,

An L. Moens,

Hunter C. Champion,

David A. Kass

Publication year - 2007

Publication title -

circulation

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 7.795

H-Index - 607

eISSN - 1524-4539

pISSN - 0009-7322

DOI - 10.1161/circulationaha.106.643536

Subject(s) - medicine , inotrope , phosphodiesterase , adrenergic , compartmentalization (fire protection) , adrenergic agent , intracellular , endocrinology , adrenergic receptor , pharmacology , receptor , microbiology and biotechnology , enzyme , biochemistry , biology

Recent cell-based studies have found that cGMP synthesis and hydrolysis by phosphodiesterase (PDE) appear compartmentalized, with nitric oxide synthase-derived and/or PDE type 5 (PDE-5)-hydrolyzable cGMP undetected at the sarcolemmal membrane in contrast to cGMP stimulated by natriuretic peptide. In the present study, we determine the functional significance of such compartments with a comparison of beta-adrenergic modulation by PDE-5 inhibition to that of natriuretic peptide stimulation in both cardiomyocytes and intact hearts. The potential role of differential cGMP and protein kinase G stimulation by these 2 modulators was also studied.

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