vasopressin vasopressin human vasopressin, also called antidiuretic hormone (adh), arginine vasopressin (avp) or argipressin, is a hormone synthesized from the avp gene as a peptide prohormone in neurons in the hypothalamus, and is converted to avp. it then travels down the axon terminating in the posterior pituitary, and is released from vesicles into the circulation in response to extracellular fluid hypertonicity (hyperosmolality). avp has two primary functions. first, it increases the amount of solute-free water reabsorbed back into the circulation from the filtrate in the kidney tubules of the nephrons. second, avp constricts arterioles, which increases peripheral vascular resistance and raises arterial blood pressure. this article is about the natural peptide in humans. for the medication, see vasopressin (medication). not to be confused with vasopressors generally, of which it is but one example. vasopressinclinical datapronunciation/ˌveɪzoʊˈprɛsɪn/ other namesantidiuretic hormone (adh); arginine vasopressin (avp); argipressinatc codeh01ba01 (who) physiological datasource tissuessupraoptic nucleus; paraventricular nucleus of hypothalamustarget tissuessystem-widereceptorsv1a, v1b, v2, oxtragonistsfelypressin, desmopressinantagonistsdiureticsmetabolismpredominantly in the liver and kidneyspharmacokinetic dataprotein binding1%metabolismpredominantly in the liver and kidneyselimination half-life10–20 minutesexcretionurineidentifiers iupac name 1--l-p rolyl-l-arginylglycinamide cas number11000-17-2 ypubchem cid644077iuphar/bps2168drugbankdb00067 ychemspider559126 yuniiy87y826h08keggd00101 ychebichebi:9937 ychemblchembl373742 ychemical and physical dataformulac46h65n15o12s2molar mass1084.24 g·mol−13d model (jsmol)interactive imagedensity1.6±0.1 g/cm3 smiles c1ccc(cc1)c2c(=o)n(c(=o)n(c(=o)n(cssc(c(=o)n(c(=o)n2)cc3ccc(cc3)o)n)c(=o)n4ccc4c(=o)n(cccn=c(n)n)c(=o)ncc(=o)n)cc(=o)n)ccc(=o)n inchi inchi=1s/c46h65n15o12s2 /c47-27-22-74-75-23-33(45(73)61-17-5-9-34(61)44(72)56-28(8-4-16-53-46(51)52)39(67)54-21-37(50)65)60-43(71)32(20-36(49)64)59-40(68)29(14-15-35(48)63)55-41(69)31(18-24-6-2-1-3-7-24)58-42(70)30(57-38(27)66)19-25-10-12-26(62)13-11-25/h1-3,6-7,10-13,27-34,62h,4-5,8-9,14-23,47h2,(h2,48,63)(h2,49,64)(h2,50,65)(h,54,67)(h,55,69)(h,56,72)(h,57,66)(h,58,70)(h,59,68)(h,60,71)(h4,51,52,53)/t27-,28-,29-,30-,31-,32-,33-,34-/m0/s1 ykey:kbzoirjilgzlej-lgyyrgkssa-n y avpidentifiersaliasesavp, adh, arvp, avp-npii, avrp, vp, arginine vasopressin, vasopressinexternal idsomim: 192340 mgi: 88121 homologene: 417 genecards: avp gene location (human)chr.chromosome 20 (human)band20p13start3,082,556 bpend3,084,724 bpgene location (mouse)chr.chromosome 2 (mouse)band2 f1|2 63.24 cmstart130,422,540 bpend130,424,474 bprna expression patternbgeehumanmouse (ortholog)top expressed inhypothalamusinternal globus pallidusgastric mucosakidneymonocyteamygdalaanterior pituitarysubcutaneous adipose tissuesubstantia nigraleft adrenal glandtop expressed inparaventricular nucleus of hypothalamussupraoptic nucleusarcuate nucleusoptic nervemedian eminencesuprachiasmatic nucleusventromedial nucleuslateral hypothalamusmirrortonguemore reference expression databiogpsmore reference expression datagene ontologymolecular function protein kinase activity hormone activity cysteine-type endopeptidase inhibitor activity involved in apoptotic process neurohypophyseal hormone activity signaling receptor binding v1a vasopressin receptor binding v1b vasopressin receptor binding neuropeptide hormone activity cellular component extracellular region cytosol clathrin-coated vesicle membrane extracellular space secretory granule dendrite biological process negative regulation of cysteine-type endopeptidase activity involved in apoptotic process vasoconstriction negative regulation of release of cytochrome c from mitochondria erk1 and erk2 cascade water transport cell-cell signaling negative regulation of apoptotic process protein kinase c signaling generation of precursor metabolites and energy positive regulation of peptidyl-serine phosphorylation positive regulation of gene expression renal water homeostasis signal transduction apoptotic process membrane organization regulation of signaling receptor activity g protein-coupled receptor signaling pathway maternal aggressive behavior positive regulation of systemic arterial blood pressure positive regulation of cytosolic calcium ion concentration negative regulation of female receptivity grooming behavior locomotory behavior positive regulation of cell population proliferation positive regulation of glutamate secretion response to organic cyclic compound positive regulation of cell growth positive regulation of prostaglandin biosynthetic process positive regulation of cellular ph reduction response to testosterone response to nicotine social behavior regulation of renal sodium excretion hyperosmotic salinity response maternal behavior penile erection response to ethanol positive regulation of vasoconstriction multicellular organismal water homeostasis negative regulation of transmission of nerve impulse sources:amigo / quickgoorthologsspecieshumanmouseentrez55111998ensemblensg00000101200ensmusg00000037727uniprotp01185p35455refseq (mrna)nm_000490nm_009732refseq (protein)np_000481np_033862location (ucsc)chr 20: 3.08 – 3.08 mbchr 2: 130.42 – 130.42 mbpubmed searchwikidataview/edit humanview/edit mouse a third function is possible. some avp may be released directly into the brain from the hypothalamus, and may play an important role in social behavior, sexual motivation and pair bonding, and maternal responses to stress. vasopressin induces differentiation of stem cells into cardiomyocytes and promotes heart muscle homeostasis. it has a very short half-life, between 16 and 24 minutes. physiology further information: renal physiology function vasopressin regulates the tonicity of body fluids. it is released from the posterior pituitary in response to hypertonicity and causes the kidneys to reabsorb solute-free water and return it to the circulation from the tubules of the nephron, thus returning the tonicity of the body fluids toward normal. an incidental consequence of this renal reabsorption of water is concentrated urine and reduced urine volume. avp released in high concentrations may also raise blood pressure by inducing moderate vasoconstriction. avp also may have a variety of neurological effects on the brain. it may influence pair-bonding in voles. the high-density distributions of vasopressin receptor avpr1a in prairie vole ventral forebrain regions have been shown to facilitate and coordinate reward circuits during partner preference formation, critical for pair bond formation. a very similar substance, lysine vasopressin (lvp) or lypressin, has the same function in pigs and its synthetic version was used in human avp deficiency, although it has been largely replaced by desmopressin. kidney vasopressin has three main effects which are: increasing the water permeability of distal convoluted tubule (dct) and cortical collecting tubules (cct), as well as outer and inner medullary collecting duct (omcd & imcd) in the kidney, thus allowing water reabsorption and excretion of more concentrated urine, i.e., antidiuresis. this occurs through increased transcription and insertion of water channels (aquaporin-2) into the apical membrane of collecting tubule and collecting duct epithelial cells. aquaporins allow water to move down their osmotic gradient and out of the nephron, increasing the amount of water re-absorbed from the filtrate (forming urine) back into the bloodstream. this effect is mediated by v2 receptors. vasopressin also increases the concentration of calcium in the collecting duct cells, by episodic release from intracellular stores. vasopressin, acting through camp, also increases transcription of the aquaporin-2 gene, thus increasing the total number of aquaporin-2 molecules in collecting duct cells. increasing permeability of the inner medullary portion of the collecting duct to urea by regulating the cell surface expression of urea transporters, which facilitates its reabsorption into the medullary interstitium as it travels down the concentration gradient created by removing water from the connecting tubule, cortical collecting duct, and outer medullary collecting duct. acute increase of sodium absorption across the ascending loop of henle. this adds to the countercurrent multiplication which aids in proper water reabsorption later in the distal tubule and collecting duct. central nervous system vasopressin released within the brain may have several actions: vasopressin is released into the brain in a circadian rhythm by neurons of the suprachiasmatic nucleus. vasopressin released from posterior pituitary is associated with nausea. recent evidence suggests that vasopressin may have analgesic effects. the analgesia effects of vasopressin were found to be dependent on both stress and sex. gene regulation further information: avp gene vasopressin is regulated by avp gene expression which is managed by major clock controlled genes. in this circadian circuit known as the transcription-translation feedback loop (ttfl), per2 protein accumulates and is phosphorylated by ck1e. per2 subsequently inhibits the transcription factors clock and bmal1 in order to reduce per2 protein levels in the cell. at the same time, per2 also inhibits the transcription factors for the avp gene in order to regulate its expression, the expression of vasopressin, and other avp gene products. many factors influence the secretion of vasopressin: ethanol (alcohol) reduces the calcium-dependent secretion of avp by blocking voltage-gated calcium channels in neurohypophyseal nerve terminals in rats. angiotensin ii stimulates avp secretion, in keeping with its general pressor and pro-volumic effects on the body. atrial natriuretic peptide inhibits avp secretion, in part by inhibiting angiotensin ii-induced stimulation of avp secretion. cortisol inhibits secretion of antidiuretic hormone. production and secretion the physiologic stimulus for secretion of vasopressin is increased osmolality of the plasma, monitored by the hypothalamus. a decreased arterial blood volume, (such as can occur in cirrhosis, nephrosis and heart failure), stimulates secretion, even in the face of decreased osmolality of the plasma: it supersedes osmolality, but with a milder effect. in other words, vasopressin is secreted in spite of the presence of hypoosmolality (hyponatremia) when the arterial blood volume is low. the avp that is measured in peripheral blood is almost all derived from secretion from the posterior pituitary gland (except in cases of avp-secreting tumours). vasopressin is produced by magnocellular neurosecretory neurons in the paraventricular nucleus of hypothalamus (pvn) and supraoptic nucleus (son). it then travels down the axon through the infundibulum within neurosecretory granules that are found within herring bodies, localized swellings of the axons and nerve terminals. these carry the peptide directly to the posterior pituitary gland, where it is stored until released into the blood. there are other sources of avp, beyond the hypothalamic magnocellular neurons. for example, avp is also synthesized by parvocellular neurosecretory neurons of the pvn, transported and released at the median eminence, from which it travels through the hypophyseal portal system to the anterior pituitary, where it stimulates corticotropic cells synergistically with crh to produce acth (by itself it is a weak secretagogue). vasopressin during surgery and anaesthesia vasopressin concentration is used to measure surgical stress for evaluation of surgical techniques. plasma vasopressin concentration is elevated by noxious stimuli, predominantly during abdominal surgery, especially at gut manipulation, traction of viscera, as well as abdominal insufflation with carbon dioxide during laparoscopic surgery. receptors types of avp receptors and their actions: typesecond messenger system locationsactions agonists antagonists avpr1aphosphatidylinositol/calciumliver, kidney, peripheral vasculature, brainvasoconstriction, gluconeogenesis, platelet aggregation, and release of factor viii and von willebrand factor; social recognition, circadian tau felypressin avpr1b or avpr3phosphatidylinositol/calciumpituitary gland, brainadrenocorticotropic hormone secretion in response to stress; social interpretation of olfactory cues avpr2adenylate cyclase/campbasolateral membrane of the cells lining the collecting ducts of the kidneys (especially the cortical and outer medullary collecting ducts)insertion of aquaporin-2 (aqp2) channels (water channels). this allows water to be reabsorbed down an osmotic gradient, and so the urine is more concentrated. release of von willebrand factor and surface expression of p-selectin through exocytosis of weibel-palade bodies from endothelial cells avp, desmopressin "-vaptan" diuretics, i.e. tolvaptan structure and relation to oxytocin chemical structure of the arginine vasopressin (argipressin) with an arginine at the 8th amino acid position. lysine vasopressin differs only in having a lysine in this position. chemical structure of oxytocin. differs from avp at only the 3rd and 8th position. the vasopressins are peptides consisting of nine amino acids (nonapeptides). the amino acid sequence of arginine vasopressin (argipressin) is cys-tyr-phe-gln-asn-cys-pro-arg-gly-nh2, with the cysteine residues forming a disulfide bond and the c-terminus of the sequence converted to a primary amide. lysine vasopressin (lypressin) has a lysine in place of the arginine as the eighth amino acid, and is found in pigs and some related animals, whereas arginine vasopressin is found in humans. the structure of oxytocin is very similar to that of the vasopressins: it is also a nonapeptide with a disulfide bridge and its amino acid sequence differs at only two positions. the two genes are located on the same chromosome separated by a relatively small distance of less than 15,000 bases in most species. the magnocellular neurons that secrete vasopressin are adjacent to magnocellular neurons that secrete oxytocin, and are similar in many respects. the similarity of the two peptides can cause some cross-reactions: oxytocin has a slight antidiuretic function, and high levels of avp can cause uterine contractions. comparison of vasopressin and oxytocin neuropeptide families: vertebrate vasopressin family cys-tyr-phe-gln-asn-cys-pro-arg-gly-nh2argipressin (avp, adh)most mammals cys-tyr-phe-gln-asn-cys-pro-lys-gly-nh2lypressin (lvp)pigs, hippos, warthogs, some marsupials cys-phe-phe-gln-asn-cys-pro-arg-gly-nh2phenypressinsome marsupials cys-tyr-ile-gln-asn-cys-pro-arg-gly-nh2vasotocin†non-mammals vertebrate oxytocin family cys-tyr-ile-gln-asn-cys-pro-leu-gly-nh2oxytocin (oxt)most mammals, ratfish cys-tyr-ile-gln-asn-cys-pro-pro-gly-nh2prol-oxytocinsome new world monkeys, northern tree shrews cys-tyr-ile-gln-asn-cys-pro-ile-gly-nh2mesotocinmost marsupials, all birds, reptiles, amphibians, lungfishes, coelacanths cys-tyr-ile-gln-ser-cys-pro-ile-gly-nh2seritocinfrogs cys-tyr-ile-ser-asn-cys-pro-ile-gly-nh2isotocinbony fishes cys-tyr-ile-ser-asn-cys-pro-gln-gly-nh2glumitocinskates cys-tyr-ile-asn/gln-asn-cys-pro-leu/val-gly-nh2various tocinssharks invertebrate vp/ot superfamily cys-leu-ile-thr-asn-cys-pro-arg-gly-nh2inotocinlocust cys-phe-val-arg-asn-cys-pro-thr-gly-nh2annetocinearthworm cys-phe-ile-arg-asn-cys-pro-lys-gly-nh2lys-connopressingeography & imperial cone snail, pond snail, sea hare, leech cys-ile-ile-arg-asn-cys-pro-arg-gly-nh2arg-connopressinstriped cone snail cys-tyr-phe-arg-asn-cys-pro-ile-gly-nh2cephalotocinoctopus cys-phe-trp-thr-ser-cys-pro-ile-gly-nh2octopressinoctopus †vasotocin is the evolutionary progenitor of all the vertebrate neurohypophysial hormones. medical use main article: vasopressin (medication) vasopressin is used to manage anti-diuretic hormone deficiency. vasopressin is used to treat diabetes insipidus related to low levels of antidiuretic hormone. it is available as pressyn. vasopressin has off-label uses and is used in the treatment of vasodilatory shock, gastrointestinal bleeding, ventricular tachycardia and ventricular fibrillation. vasopressin agonists are used therapeutically in various conditions, and its long-acting synthetic analogue desmopressin is used in conditions featuring low vasopressin secretion, as well as for control of bleeding (in some forms of von willebrand disease and in mild haemophilia a) and in extreme cases of bedwetting by children. terlipressin and related analogues are used as vasoconstrictors in certain conditions. use of vasopressin analogues for esophageal varices commenced in 1970. vasopressin infusions are also used as second line therapy for septic shock patients not responding to fluid resuscitation or infusions of catecholamines (e.g., dopamine or norepinephrine) to increase the blood pressure while sparing the use of catecholamines. these argipressins have much shorter elimination half-life (around 20 minutes) comparing to synthetic non-arginine vasopresines with much longer elimination half-life of many