Transversal and longitudinal aortic bulb strips show isometric contractions in response to the vasotocin action. The extreme sensitivity of the preparations correspond to a final hormone concentration of 8.25 X 10(-16) M.

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Structure and function of neurohypophysial hormones.

Peptides

December 2024

Health Service Center, Kochi University, Kochi Medical School, Kochi 780-8520, Japan.

Vasopressin (VP) and oxytocin (OXT) are neuropeptides that are synthesized in the hypothalamus and stored in/secreted from the neurohypophysis. Although VP and OXT were initially characterized as osmoregulatory and reproductive hormones, respectively, these peptides exert versatile actions not only in peripheral organs but also in the central nervous system via multiple G protein-coupled receptors. Orthologous peptides and receptors have been identified in various animal phyla, reflecting an ancient origin of this hormone family.

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The neuropeptide vasopressin is known for its regulation of osmotic balance in mammals. Arginine vasotocin (AVT) is a non-mammalian homolog of this neuropeptide that is present in fish. Limited information suggested that vasopressin and its homologs may also influence reproductive function.

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Intraperitoneal administration of arginine vasotocin (AVT) induces anorexigenic and anxiogenic actions via the brain V1a receptor-signaling pathway in the tiger puffer, Takifugu rubripes.

Peptides

August 2024

Laboratory of Regulatory Biology, Graduate School of Science and Engineering, University of Toyama, Toyama 930-8555, Japan; Laboratory of Regulatory Biology, Faculty of Science, Academic Assembly, University of Toyama, Toyama 930-8555, Japan. Electronic address:

Arginine vasotocin (AVT) is produced mainly in the hypothalamus and as a neurohypophyseal hormone peripherally regulates water-mineral balance in sub-mammals. In addition, AVT-containing neurons innervate several areas of the brain, and AVT also acts centrally as both an anorexigenic and anxiogenic factor in goldfish. However, it is unclear whether these central effects operate in fish in general.

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Characterization of an vasotocin signaling system and actions of posttranslational modifications and individual residues of the ligand on receptor activity.

Front Pharmacol

March 2023

State Key Laboratory of Pharmaceutical Biotechnology, Jiangsu Engineering Research Center for MicroRNA Biology and Biotechnology, Chemistry and Biomedicine Innovation Center, Institute for Brain Sciences, Advanced Institute for Life Sciences, School of Life Sciences, Chinese Academy of Medical Sciences Research Unit of Extracellular RNA, Nanjing University, Nanjing, Jiangsu, China.

Article Synopsis
  • - The study discovered a vasopressin-like peptide precursor (apVT) and two receptors (apVTR1 and apVTR2) in mollusks, which were previously unreported, using bioinformatics and molecular techniques.
  • - The apVT peptide shares a sequence with conopressin G from cone snail venom and is critical for activating the identified receptors, with specific post-translational modifications (like disulfide bonds) being essential for functionality.
  • - Different vasopressin-like peptides can activate these receptors, but their effectiveness varies based on amino acid variations, highlighting the importance of specific residues and modifications in receptor activation.
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Circulating isotocin, not angiotensin II, is the major dipsogenic hormone in eels.

J Exp Biol

June 2022

Laboratory of Physiology, Atmosphere and Ocean Research Institute, University of Tokyo, 5-1-5, Kashiwanoha, Kashiwa, Chiba, 277-8564, Japan.

Angiotensin II (AngII) is generally known as the most important dipsogenic hormone throughout vertebrates, while two other neurohypophysial hormones, vasopressin and oxytocin, are not dipsogenic in mammals. In this study, we found that systemic isotocin, but not vasotocin, is the potent dipsogenic hormone in eels. When injected intra-arterially into conscious eels, isotocin, vasotocin and AngII equally increased ventral aortic pressure dose dependently at 0.

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