Arginine vasopressin: Critical regulator of circadian homeostasis

Circadian rhythms optimally regulate numerous physiological processes in an organism and synchronize them with the external environment. The suprachiasmatic nucleus (SCN), the center of the circadian clock in mammals, is composed of multiple cell types that form a network that provides the basis for...

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Veröffentlicht in:Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2024-07, Vol.177, p.171229, Article 171229
1. Verfasser: Yamaguchi, Yoshiaki
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Sprache:eng
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Zusammenfassung:Circadian rhythms optimally regulate numerous physiological processes in an organism and synchronize them with the external environment. The suprachiasmatic nucleus (SCN), the center of the circadian clock in mammals, is composed of multiple cell types that form a network that provides the basis for the remarkable stability of the circadian clock. Among the neuropeptides expressed in the SCN, arginine vasopressin (AVP) has attracted much attention because of its deep involvement in the function of circadian rhythms, as elucidated in particular by studies using genetically engineered mice. This review briefly summarizes the current knowledge on the peptidergic distribution and topographic neuronal organization in the SCN, the molecular mechanisms of the clock genes, and the relationship between the SCN and peripheral clocks. With respect to the physiological roles of AVP and AVP-expressing neurons, in addition to a sex-dependent action of AVP in the SCN, studies using AVP receptor knockout mice and mice genetically manipulated to alter the clock properties of AVP neurons are summarized here, highlighting its importance in maintaining circadian homeostasis and its potential as a target for therapeutic interventions. •Topographic neuronal organization in the suprachiasmatic nucleus.•Molecular mechanisms of the clock genes.•Sex-dependent effects of AVP on circadian rhythms.•Circadian homeostasis mediated by AVP neurons.•Drug discovery for jet lag targeting AVP receptors.
ISSN:0196-9781
1873-5169
1873-5169
DOI:10.1016/j.peptides.2024.171229