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- W1966555000 abstract "Previously, cardioexcitation by serotonin (5-hydroxytryptamine, 5-HT) was believed to be confined to atria in mammals including man, and mediated through 5-HT4 receptors in pig and man, but 5-HT2A receptors in rat. Recent studies, reviewed here, demonstrate that functional 5-HT4 receptors can be revealed in porcine and human ventricular myocardium during phosphodiesterase inhibition, and that 5-HT4 receptor mRNA is increased in human heart failure. In rats, functional 5-HT4 and 5-HT2A receptors appear in the cardiac ventricle during heart failure and mediate inotropic responses through different mechanisms. 5-HT2A receptor signalling resembles that from α1-adrenoceptors and causes inotropic effects through increased myosin light chain phosphorylation, resulting in Ca2+ sensitisation. 5-HT4 receptor signalling resembles that from β-adrenoceptors and causes inotropic effects through a pathway involving cAMP and PKA-mediated phosphorylation of proteins involved in Ca2+ handling, resulting in enhanced contractility through increased Ca2+ availability. Cyclic AMP generated through 5-HT4 receptor stimulation seems more efficiently coupled to increased contractility than cAMP generated through β-adrenoceptor stimulation. Increasing contractility through cAMP is considered less energy efficient than Ca2+ sensitisation and this may be one reason why β-adrenoceptor antagonism is beneficial in heart failure patients. Treatment of heart failure rats with the 5-HT4 antagonist SB207266 (piboserod) resulted in potentially beneficial effects, although small. Further studies are needed to clarify if such treatment will be useful for patients with heart failure." @default.
- W1966555000 created "2016-06-24" @default.
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- W1966555000 date "2008-11-01" @default.
- W1966555000 modified "2023-10-18" @default.
- W1966555000 title "Effects of serotonin in failing cardiac ventricle: Signalling mechanisms and potential therapeutic implications" @default.
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- W1966555000 doi "https://doi.org/10.1016/j.neuropharm.2008.07.010" @default.
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