Anti-adrenergic effects of nitric oxide donor SIN-1 in rat cardiac myocytes
Autor: | Gordon M. Wahler, Miroslav O. Stojanovic, Beata M. Wolska, Mark T. Ziolo |
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Rok vydání: | 2001 |
Předmět: |
medicine.medical_specialty
Myosin Light Chains Physiology chemistry.chemical_element Adrenergic Stimulation Calcium Nitric oxide Superoxide dismutase chemistry.chemical_compound Internal medicine medicine Animals Humans Myocyte Nitric Oxide Donors Enzyme Inhibitors Phosphorylation Oxadiazoles biology Superoxide Dismutase Chemistry Myocardium Calcium-Binding Proteins Troponin I Isoproterenol Free Radical Scavengers Cell Biology Adrenergic beta-Agonists Rats Phospholamban Endocrinology Molsidomine Circulatory system biology.protein Muscle Contraction |
Zdroj: | American Journal of Physiology-Cell Physiology. 281:C342-C349 |
ISSN: | 1522-1563 0363-6143 |
DOI: | 10.1152/ajpcell.2001.281.1.c342 |
Popis: | We studied how the nitric oxide (NO·) donor 3-morpholinosydnonimine (SIN-1) alters the response to β-adrenergic stimulation in cardiac rat myocytes. We found that SIN-1 decreases the positive inotropic effect of isoproterenol (Iso) and decreases the extent of both cell shortening and Ca2+transient. These effects of SIN-1 were associated with an increased intracellular concentration of cGMP, a decreased intracellular concentration of cAMP, and a reduction in the levels of phosphorylation of phospholamban (PLB) and troponin I (TnI). The guanylyl cyclase inhibitor 1 H-8-bromo-1,2,4-oxadiazolo (3,4-d)benz(b)(1,4)oxazin-1-one (ODQ) was not able to prevent the SIN-1-induced reduction of phosphorylation levels of PLB and TnI. However, the effects of SIN-1 were abolished in the presence of superoxide dismutase (SOD) or SOD and catalase. These data suggest that, in the presence of Iso, NO-related congeners, rather than NO·, are responsible for SIN-1 effects. Our results provide new insights into the mechanism by which SIN-1 alters the positive inotropic effects of β-adrenergic stimulation. |
Databáze: | OpenAIRE |
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