{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T04:50:39Z","timestamp":1790311839959,"version":"4.1.0"},"reference-count":57,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2013,9,24]],"date-time":"2013-09-24T00:00:00Z","timestamp":1379980800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Experimental Physiology"],"published-print":{"date-parts":[[2014,1]]},"abstract":"<jats:title>New findings<\/jats:title><jats:p><jats:list list-type=\"explicit-label\">\n<jats:list-item><jats:p><jats:bold>What is the topic of this review?<\/jats:bold><\/jats:p><jats:p>This article describes the discovery and function of invertebrate oxytocin and vasopressin neuropeptides.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p><jats:bold>What advances does it highlight?<\/jats:bold><\/jats:p><jats:p>The novel discovery of oxytocin\u2010like peptides in arthropods is described. An up\u2010to date overview is gven of the functional role (physiology and behaviour) of oxytocin and vasopressin signalling. The application of natural peptides for drug development is discussed.<\/jats:p><\/jats:list-item>\n<\/jats:list><\/jats:p><jats:p>Neuropeptides and regulatory peptide hormones control many developmental, physiological and behavioural processes in animals, including humans. The nonapeptides oxytocin and arginine vasopressin are produced and released by the pituitary gland and have actions on many organs and tissues. Receptive cells possess particular receptors to which the peptides bind as ligands, leading to activation of G\u2010protein\u2010coupled receptors, hence cellular responses. In humans and other mammalian species, oxytocin and vasopressin mediate a range of peripheral and central physiological functions that are important for osmoregulation, reproduction, complex social behaviours, memory and learning. The origin of the oxytocin\/vasopressin signalling system is thought to date back more than 600 million years. All vertebrate oxytocin\u2010 and vasopressin\u2010like peptides have presumably evolved from the ancestral nonapeptide vasotocin by gene duplication and today are present in vertebrates, including mammals, birds, reptiles, amphibians and fish. Oxytocin\u2010 and vasopressin\u2010like peptides have been identified in several invertebrate species, including molluscs, annelids, nematodes and arthropods. Members of this peptide family share high sequence similarity, and it is possible that they are functionally related across the entire animal kingdom. However, it is evident that not all animals express oxytocin\/vasopressin neuropeptides and that there is little information available about the biology and physiology of this signalling system of invertebrates and, in particular, of insects, which represent more than half of all known living organisms. This report describes the discovery of novel oxytocin\u2010 and vasopressin\u2010like peptides in arthropods and summarizes the status quo of the functional relevance of this neuropeptide signalling system in invertebrates, which will have beneficial implications for the design of selective and potent ligands to human oxytocin and vasopressin receptors.<\/jats:p>","DOI":"10.1113\/expphysiol.2013.072561","type":"journal-article","created":{"date-parts":[[2013,8,17]],"date-time":"2013-08-17T00:16:57Z","timestamp":1376698617000},"page":"55-61","source":"Crossref","is-referenced-by-count":100,"title":["Physiology of invertebrate oxytocin and vasopressin neuropeptides"],"prefix":"10.1113","volume":"99","author":[{"given":"Christian W.","family":"Gruber","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2013,9,24]]},"reference":[{"key":"e_1_2_5_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/0006-3002(53)90173-5"},{"key":"e_1_2_5_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/0006-3002(60)90814-3"},{"key":"e_1_2_5_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.ibmb.2008.04.006"},{"key":"e_1_2_5_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.nlm.2009.10.004"},{"key":"e_1_2_5_6_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.1226860"},{"key":"e_1_2_5_7_1","doi-asserted-by":"publisher","DOI":"10.1124\/jpet.113.202994"},{"key":"e_1_2_5_8_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M111.277178"},{"key":"e_1_2_5_9_1","doi-asserted-by":"publisher","DOI":"10.1042\/BST0350737"},{"key":"e_1_2_5_10_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.coph.2009.10.003"},{"key":"e_1_2_5_11_1","doi-asserted-by":"crossref","first-page":"15821","DOI":"10.1016\/S0021-9258(18)47661-2","article-title":"Invertebrate vasopressin\/oxytocin homologs. 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