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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/05/17 18:17:35」(JST)

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Vasotocin is an oligopeptide homologous to oxytocin and vasopressin found in all non-mammalian vertebrates (including birds, fishes, and amphibians) and possibly in mammals during the fetal stage of development. Arginine vasotocin (AVT), a hormone produced by neurosecretory cells within the posterior pituitary gland (neurohypophysis) of the brain, is a major endocrine regulator of water balance and osmotic homoeostasis and is involved in social and sexual behavior in non-mammalian vertebrates. In mammals, it appears to have biological properties similar to those of oxytocin (stimulating reproductive tract contraction as in egg laying or birth) and vasopressin (diuretic and antidiuretic effects). It has been found to have effects on the regulation of REM sleep.^[1] Evidence for the existence of endogenous vasotocin in mammals is limited^[2]^[3] and no mammalian gene encoding vasotocin has been confirmed.

AVT (Cys-Tyr-Ile-Gln-Asn-Cys-Pro-Arg-Gly-NH2), which occurs in the lamprey, represents the ancestral form in the phylogeny of the vertebrate neurohypophysial hormones.^[4] Gene duplication and point mutation have produced two distinct lineages, one involved in reproduction (oxytocin-like peptides) and the other in osmoregulation (vasopressin-like peptides). These hormones have remained highly conserved throughout evolution. Each is a peptide of nine amino acids derived from a preprohormone precursor by proteolytic cleavage, with an intramolecular disulfide bridge between the cysteine (Cys) residues; the C-terminal glycine (Gly) residue is amidated. Six of the residues have been found to be invariant in homologous peptides from numerous species of vertebrates. The vasopressin-like peptides, which differ in positions 3 and/or 8, include AVT and the mammalian hormones arginine vasopressin (Cys-Tyr-Phe-Gln-Asn-Cys-Pro-Arg-Gly-NH2, with isoleucine-3 of AVT changed to phenylalanine) and lysine vasopressin (isoleucine-3 changed to phenylalanine and arginine-8 changed to lysine). The oxytocin-like peptides, which differ in positions 4 and/or 8, include oxytocin (Cys-Tyr-Ile-Gln-Asn-Cys-Pro-Leu-Gly-NH2, with arginine-8 of AVT changed to leucine), mesotocin (arginine-8 changed to isoleucine), and isotocin (glutamine-4 changed to serine and arginine-8 changed to isoleucine); they differ from the vasopressin-like peptides in having a neutral amino acid in place of a basic amino acid at position 8. Oxytocin occurs in placental mammals; mesotocin occurs in amphibians, reptiles, and birds, and isotocin occurs in fishes.

Biosynthesis

AVT is synthesized as a preprohormone that includes a second peptide, neurophysin VT (neurophysins are carrier proteins that are secreted along with their passenger hormones); intracellular proteolytic processing generates the mature peptides. In the chicken (Gallus gallus), the 161-amino acid vasotocin-neurophysin VT preprohormone is encoded by the gene AVP, which is considered homologous to the mammalian genes encoding arginine vasopressin.^[5] Removal of the 19-amino acid N-terminal signal peptide generates the prohormone, which is hydrolysed to AVT (derived from amino acids 20-28) and neurophysin VT (derived from amino acids 32-161).^[6] The existence of two AVT preprohormones with different sequences in fishes (such as chum salmon, Oncorhynchus keta^[7]) is evidence for gene duplication.

Behavioral Effects

Several animal studies have been conducted that explore the behavioral effects of AVT. The main findings of these studies have revealed that AVT plays an integral role in the pair bonding behavior and social hierarchy in non-mammalian vertebrates.

In a study conducted with zebra finches,^[8] increased levels of AVT were linked to an increase in aggressive, competitive behavior in non-paired male finches, but were subsequently related to an increase in defensive behavior after the finches had been paired. However, this study also found that blocking AVT receptors did not directly affect pair bonding ability. The shift in behaviors were explained by the location of the release of AVT in the brain. Competitive aggressive behavior was found to be linked with AVT release in the BSTm, whereas defensive, nest-protecting behavior was linked with AVT release in the neurons of the Hypothalamus and Paraventricular Nucleus.

In a study conducted with male Japanese quail, AVT was found to have an effect on later social interactions amongst the species. Immediately after injection with AVT, the quails displayed less aggressive behavior (pecking). However, the next day, the quail that were injected with AVT displayed more dominant behavior towards familiar birds, but not unfamiliar birds. This study shows that AVT may play a role in establishing social hierarchy.^[9]

A study that investigated the role of social construction and AVT compared territorial and non-territorial species of tropical coral reef fish.^[10] Experimenters administered Manning compound, an AVT agonist to the fish and found that, after treatment, non-territorial species displayed more territorial behavior whereas territorial species displayed less territorial behavior.

Research suggests that the effects of AVT on aggression may be influenced by the social construction of the species. For example, in a study done with Rainbow Trout,^[11] increased levels of AVT were associated with more subordinate behavior. It is currently hypothesized that the contrasting effects of AVT are related to the distinction between territorial versus colonial social systems. In a territorial species, such as Rainbow Trout, AVT is linked to less dominant behavior. This may be due to the differences in the distribution of AVT receptors in territorial and colonial species.

Sources

^ Kales, Anthony (1995). The Pharmacology of sleep. Berlin: Springer-Verlag. ISBN 3-540-58961-9.
^ Ervin MG, Leake RD, Ross MG, Calvario GC, Fisher DA (May 1985). "Arginine vasotocin in ovine fetal blood, urine, and amniotic fluid". J Clin Invest. 75 (5): 1696–701. doi:10.1172/JCI111878. PMID 3998151.
^ Ervin MG, Amico JA, Leake RD, Ross MG, Robinson AG, Fisher DA (1988). "Arginine vasotocin and a novel oxytocin-vasotocin-like material in plasma of human newborns". Biol Neonate 53 (1): 17–22. doi:10.1159/000242757. PMID 3355867.
^ Liu JW, Ben-Jonathan N (January 1994). "Prolactin-releasing activity of neurohypophysial hormones: structure-function relationship". Endocrinology 134 (1): 114–18. doi:10.1210/en.134.1.114. PMID 8275925.
^ "AVP arginine vasopressin (neurophysin II, antidiuretic hormone, diabetes insipidus, neurohypophyseal) [ Gallus gallus (chicken) ], Entrez Gene ID 396101".
^ "Vasotocin-neurophysin VT, UniProtKB/Swiss-Prot P24787 (NEUV_CHICK)".
^ Heierhorst J, Mahlmann S, Morley SD, Coe IR, Sherwood NM, Richter D (January 1990). "Molecular cloning of two distinct vasotocin precursor cDNAs from chum salmon (Oncorhynchus keta) suggests an ancient gene duplication". FEBS Lett. 260 (2): 301–4. doi:10.1016/0014-5793(90)80129-7. PMID 2298304.
^ Kabelik D, Klatt JD, Kingsbury MA, Goodson JL. Endogenous vasotocin exerts contexts-dependent behavioral effects in semi-naturalistic colony environment. Hormones and Behavior. 2009;56(1): 101-107.
^ Riters LV, and Panksepp J. Effects of vasotocin on aggressive behavior in male Japanese quail. Annals of the New York Academy of Sciences. 2006; 807(1): 478-480.
^ Semsar K, Kandel FLM, Godwin J. Manipulations of the AVT system shift social status and related courtship behavior in the Bluehead Wrasse. Hormones and Behavior. 2001; 40(1): 21-31.
^ Backström T, and Winberg S. Arginine vasotocin influence on aggressive behavior and dominance in rainbow trout. Physiology and Behavior. 2009; 96(3): 470-475.

External links

Vasotocin at the US National Library of Medicine Medical Subject Headings (MeSH)

English Journal

Identification of antagonists to the vasotocin receptor sub-type 4 (VT4R) involved in stress by molecular modelling and verification using anterior pituitary cells.

Jayanthi S, Kang SW, Bingham D, Tessaro BA, Suresh Kumar TK, Kuenzel WJ.Author information a Department of Chemistry and Biochemistry , University of Arkansas , Fayetteville , AR , 72701 , USA .AbstractThe vasotocin receptor family is homologous to the mammalian vasopressin G-protein coupled receptor (GPCR) family. The vasotocin receptor 2 (VT2R) and 4 (VT4R) have recently been shown to play important role(s) in the neuroendocrine regulation of stress in birds. A homology-based structural model of VT4R of the domestic chicken, Gallus gallus, was built using the sophisticated SYBYL-X suite. The structure of VT4R built with and without extra- and intracellular unstructured loops showed a seven-helix transmembrane domain, which is a characteristic feature of GPCRs. Several agonists and antagonists were screened by molecular docking to map their potential binding sites on the structure of VT4R. Interestingly, the presence of the N-terminal, intracellular and extracellular loops and C-terminal amino acid sequences emerging from the transmembrane domains during molecular docking appeared to influence the binding interface of the peptide agonists and peptide/non-peptide antagonists on the VT4R. The presence of unstructured loops, however, did not affect the relative binding affinity ranking of the peptide antagonists to VT4R. In general, the natural ligand, arginine vasotocin and the peptide/non-peptide antagonists were observed to be more deeply buried in the receptor. Results of in vitro inhibition experiments, using cultured anterior pituitary cells, showed excellent agreement with the binding affinity of the antagonists predicted by molecular docking. The results of this study provide valuable clues for the rational design of novel pharmaceutical compounds capable of blocking or attenuating the stress response.
Journal of biomolecular structure & dynamics.J Biomol Struct Dyn.2014 Apr;32(4):648-60. doi: 10.1080/07391102.2013.787025. Epub 2013 May 15.
The vasotocin receptor family is homologous to the mammalian vasopressin G-protein coupled receptor (GPCR) family. The vasotocin receptor 2 (VT2R) and 4 (VT4R) have recently been shown to play important role(s) in the neuroendocrine regulation of stress in birds. A homology-based structural model of
PMID 23672311

Sex or candy? Neuroendocrine regulation of the seasonal transition from courtship to feeding behavior in male red-sided garter snakes (Thamnophis sirtalis parietalis).

Lutterschmidt DI1, Maine AR2.Author information 1Department of Biology, Portland State University, 1719 SW 10th Ave., Portland, OR 97201, USA. Electronic address: d.lutterschmidt@pdx.edu.2Department of Biology, Portland State University, 1719 SW 10th Ave., Portland, OR 97201, USA.AbstractThis article is part of a Special Issue "Energy Balance". Seasonal modulation of glucocorticoids plays an important role in supporting critical life-history events, and probably facilitates transitions between different life-history stages. In a well-studied population of red-sided garter snakes (Thamnophis sirtalis parietalis), glucocorticoids are elevated during the mating season, but males dispersing to summer feeding grounds have significantly lower baseline glucocorticoids than courting males at the den. We tested the hypothesis that decreased plasma glucocorticoids mediate the behavioral switch between reproduction and foraging in this species. Using a two-choice Y-maze paradigm, we demonstrate that males treated with the glucocorticoid synthesis inhibitor metyrapone (1 and 3mg implants) prefer feeding cues (worm trail) over reproductive cues (female pheromone trail) significantly earlier than control-treated snakes. The metyrapone-induced changes in appetitive feeding behavior were independent of changes in plasma androgens and body mass loss. Metyrapone-treated males continued to court females at levels similar to those of control-treated snakes, suggesting that appetitive reproductive and ingestive behaviors are not mutually exclusive during this life-history transition. Consistent with this hypothesis, metyrapone treatment did not alter the number of arginine vasotocin-immunoreactive cells in any brain region, while it significantly increased neuropeptide Y-immunoreactive cell number in both the cortex and nucleus sphericus (homologues of the mammalian hippocampus and amygdala, respectively). Our results suggest that male red-sided garter snakes have the potential to maximize reproductive opportunities by continuing to court females they encounter even as they disperse from the den in search of food. Taken together, these data have important implications for understanding the neuroecology of seasonal life-history transitions.
Hormones and behavior.Horm Behav.2014 Feb 5. pii: S0018-506X(14)00021-X. doi: 10.1016/j.yhbeh.2014.01.011. [Epub ahead of print]
This article is part of a Special Issue "Energy Balance". Seasonal modulation of glucocorticoids plays an important role in supporting critical life-history events, and probably facilitates transitions between different life-history stages. In a well-studied population of red-sided garter snakes (Th
PMID 24508620

The formation and maintenance of social relationships increases nonapeptide mRNA in zebra finches of both sexes.

Lowrey EM, Tomaszycki ML.Author information Department of Psychology.AbstractThe nonapeptides oxytocin and vasopressin are believed to be involved in affiliation across species, but converging evidence is lacking. In monogamous zebra finches, oxytocin antagonists decrease pairing. The goal of the present study was to test if this relationship is bidirectional. We predicted that pairing would increase mesotocin (MT) and vasotocin (VT) mRNA (avian homologues of oxytocin and vasopressin) at nonapeptide neurosecretory sites: the paraventrivular nucleus (PVN) of the hypothalamus, which contains both MT and VT, and the bed nucleus of the stria terminalis (BSTm), which contains VT. To test our hypotheses, zebra finches of both sexes paired for 48 hr or 2 weeks in a naturalistic choice paradigm. Birds that did not pair or were not given the opportunity to pair were included as control groups. Pairing increased VT and MT mRNA in the PVN compared to both control groups. In the BSTm, animals paired for 48 hr had more cells expressing VT mRNA than did animals not given the opportunity to pair, and males had higher VT mRNA than did females. In males, singing primarily explained variations in MT mRNA, as well as VT mRNA in both the PVN and BSTm. In females, pairing behaviors explained variations in MT, but did not explain variations in VT in either brain region. Our results provide evidence that the relationship between nonapeptides and pairing are bidirectional and may be sexually differentiated. (PsycINFO Database Record (c) 2014 APA, all rights reserved).
Behavioral neuroscience.Behav Neurosci.2014 Feb;128(1):61-70. doi: 10.1037/a0035416.
The nonapeptides oxytocin and vasopressin are believed to be involved in affiliation across species, but converging evidence is lacking. In monogamous zebra finches, oxytocin antagonists decrease pairing. The goal of the present study was to test if this relationship is bidirectional. We predicted t
PMID 24512066

Japanese Journal

産卵鶏の卵管における子宮部(卵殻腺部)および膣部と比較した膨大部と峡部のバソトシンに対する結合親和性と結合容量について

高橋哲也,渡辺雄貴,田中ゆりこ [他]
医学と生物学 155(12), 987-991, 2011-12
NAID 40019131358

産卵鶏の卵管における子宮部(卵殻腺部)および膣部と比較した膨大部と峡部のバソトシンに対する結合親和性と結合容量について

高橋哲也,渡辺雄貴,田中ゆりこ [他]
医学と生物学 155(11), 830-834, 2011-11
NAID 40019061876

Related Pictures

★リンクテーブル★

リンク元	「VT」「バソトシン」
拡張検索	「arginine vasotocin」

「VT」

Vasotocin
Names
	IUPAC name 1-[(1R,4S,7S,13S,16R)-16-amino-4-(2-amino-2-oxoethyl)-7-(3-amino-3-oxopropyl)-10-[(2S)-butan-2-yl]-13-[(4-hydroxyphenyl)methyl]-3,6,9,12,15-pentaoxo-18,19-dithia-2,5,8,11,14-pentazacycloicosane-1-carbonyl]-N-[(2S)-1-[(2-amino-2-oxoethyl)amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]pyrrolidine-2-carboxamide
	Other names Argiprestocin; Arg-vasotocin; 8-Arg-vasotocin; Arginine vasotocin
Identifiers
CAS Registry Number	113-80-4
ChEBI	CHEBI:78364
Jmol-3D images	Image
PubChem	68649
	SMILES CC[C@H](C)C1C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](CSSC[C@@H](C(=O)N[C@H](C(=O)N1)CC2=CC=C(C=C2)O)N)C(=O)N3CCCC3C(=O)N[C@@H](CCCN=C(N)N)C(=O)NCC(=O)N)CC(=O)N)CCC(=O)N ;
Properties
Molecular formula	C43H67N15O12S2
Molar mass	1,050.22 g·mol−1
	Except where noted otherwise, data is given for materials in their standard state (at 25 °C (77 °F), 100 kPa)
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	Infobox references