Vasoactive intestinal peptide

VIP
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2RRI, 2RRH
Identifiers
Aliases	VIP, PHM27, vasoactive intestinal peptide
External IDs	OMIM: 192320 MGI: 98933 HomoloGene: 2539 GeneCards: VIP
Gene ontology Molecular function • hormone activity • protein binding • neuropeptide hormone activity Cellular component • extracellular region Biological process • G-protein coupled receptor signaling pathway • response to yeast • body fluid secretion • prolactin secretion • antibacterial humoral response • mRNA stabilization • defense response to Gram-negative bacterium • positive regulation of cell proliferation • innate immune response • antifungal humoral response • defense response to Gram-positive bacterium • positive regulation of adenylate cyclase activity involved in G-protein coupled receptor signaling pathway • positive regulation of protein catabolic process • regulation of protein localization Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	7432	22353
Ensembl	ENSG00000146469	ENSMUSG00000019772
UniProt	P01282	P32648
RefSeq (mRNA)	NM_003381 NM_194435	NM_011702 NM_001313969
RefSeq (protein)	NP_003372.1 NP_919416.1	NP_001300898.1 NP_035832.1
Location (UCSC)	Chr 6: 152.75 – 152.76 Mb	Chr 10: 5.64 – 5.65 Mb
PubMed search	[1]	[2]
Wikidata

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Vasoactive intestinal peptide, also known as the vasoactive intestinal polypeptide or VIP, is a peptide hormone that is vasoactive. VIP is a neuropeptide of 28 amino acid residues that belongs to a glucagon/secretin superfamily, the ligand of class II G protein–coupled receptors.^[3] VIP is produced in many tissues of vertebrates including the gut, pancreas, and suprachiasmatic nuclei of the hypothalamus in the brain.^[4][5] VIP stimulates contractility in the heart, causes vasodilation, increases glycogenolysis, lowers arterial blood pressure and relaxes the smooth muscle of trachea, stomach and gall bladder. In humans, the vasoactive intestinal peptide is encoded by the VIP gene.^[6]

VIP has a half-life (t_½) in the blood of about two minutes.

Function

VIP has an effect on several tissues:

• With respect to the digestive system, VIP seems to induce smooth muscle relaxation (lower esophageal sphincter, stomach, gallbladder), stimulate secretion of water into pancreatic juice and bile, and cause inhibition of gastric acid secretion and absorption from the intestinal lumen.^[7] Its role in the intestine is to greatly stimulate secretion of water and electrolytes,^[8] as well as relaxation of enteric smooth muscle, dilating peripheral blood vessels, stimulating pancreatic bicarbonate secretion, and inhibiting gastrin-stimulated gastric acid secretion. These effects work together to increase motility.^[9]
• It also has the function of stimulating pepsinogen secretion by chief cells.^[10]
• It is also found in the brain and some autonomic nerves. One region of the brain includes a specific area of the suprachiasmatic nuclei (SCN), the location of the 'master circadian pacemaker'. The SCN coordinates daily timekeeping in the body and VIP plays a key role in communication between individual brain cells within this region. Further, VIP is also involved in synchronising the timing of SCN function with the environmental light-dark cycle. Combined, these roles in the SCN make VIP a crucial component of the mammalian circadian timekeeping machinery.
• VIP helps to regulate prolactin secretion;^[11] it stimulates prolactin release in the domestic turkey.
• It is also found in the heart and has significant effects on the cardiovascular system. It causes coronary vasodilation^[7] as well as having a positive inotropic and chronotropic effect. Research is being performed to see if it may have a beneficial role in the treatment of heart failure.
• VIP provokes vaginal lubrication in normal women, doubling the total volume of lubrication produced.^[12]
• The growth-hormone-releasing hormone (GH-RH) is a member of the VIP family and stimulates growth hormone secretion in the anterior pituitary gland.

Pathology

VIP is overproduced in VIPoma.^[7] Can be associated with Multiple Endocrine Neoplasia Type 1 (Pituitary, parathyroid and pancreatic tumors). Symptoms are typically:

• Profuse non-bloody/non-mucoid diarrhea (3L+) causing dehydration and the associated electrolyte disturbances such as hypokalemia and metabolic acidosis.
• Lethargy and exhaustion may ensue

See also

• Vasoactive intestinal peptide receptor

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Umetsu Y, Tenno T, Goda N, Shirakawa M, Ikegami T, Hiroaki H (May 2011). "Structural difference of vasoactive intestinal peptide in two distinct membrane-mimicking environments". Biochimica et Biophysica Acta. 1814 (5): 724–30. doi:10.1016/j.bbapap.2011.03.009. PMID 21439408.
4. Fahrenkrug J, Emson PC (Sep 1982). "Vasoactive intestinal polypeptide: functional aspects". British Medical Bulletin. 38 (3): 265–70. PMID 6129023.
5. Said SI (Apr 1986). "Vasoactive intestinal peptide". Journal of Endocrinological Investigation. 9 (2): 191–200. doi:10.1007/bf03348097. PMID 2872248.
6. Linder S, Barkhem T, Norberg A, Persson H, Schalling M, Hökfelt T, Magnusson G (Jan 1987). "Structure and expression of the gene encoding the vasoactive intestinal peptide precursor". Proceedings of the National Academy of Sciences of the United States of America. 84 (2): 605–9. doi:10.1073/pnas.84.2.605. PMC 304259. PMID 3025882.
7. Bowen R (1999-01-24). "Vasoactive Intestinal Peptide". Pathophysiology of the Endocrine System: Gastrointestinal Hormones. Colorado State University. Retrieved 2009-02-06.
8. "Vasoactive intestinal polypeptide". General Practice Notebook. Retrieved 2009-02-06.
9. Bergman RA, Afifi AK, Heidger PM. "Plate 6.111 Vasoactive Intestinal Polypeptide (VIP)". Atlas of Microscopic Anatomy: Section 6 - Nervous Tissue. www.anatomyatlases.org. Retrieved 2009-02-06.
10. Sanders MJ, Amirian DA, Ayalon A, Soll AH (Nov 1983). "Regulation of pepsinogen release from canine chief cells in primary monolayer culture". The American Journal of Physiology. 245 (5 Pt 1): G641–6. PMID 6195927.
11. Kulick RS, Chaiseha Y, Kang SW, Rozenboim I, El Halawani ME (Jul 2005). "The relative importance of vasoactive intestinal peptide and peptide histidine isoleucine as physiological regulators of prolactin in the domestic turkey". General and Comparative Endocrinology. 142 (3): 267–73. doi:10.1016/j.ygcen.2004.12.024. PMID 15935152.
12. Ottesen B, Pedersen B, Nielsen J, Dalgaard D, Wagner G, Fahrenkrug J (1987). "Vasoactive intestinal polypeptide (VIP) provokes vaginal lubrication in normal women". Peptides. 8 (5): 797–800. doi:10.1016/0196-9781(87)90061-1. PMID 3432128.

Further reading

• Fahrenkrug J (2001). "Gut/brain peptides in the genital tract: VIP and PACAP". Scandinavian Journal of Clinical and Laboratory Investigation. Supplementum. 234: 35–9. PMID 11713978.
• Delgado M, Pozo D, Ganea D (Jun 2004). "The significance of vasoactive intestinal peptide in immunomodulation". Pharmacological Reviews. 56 (2): 249–90. doi:10.1124/pr.56.2.7. PMID 15169929.
• Conconi MT, Spinazzi R, Nussdorfer GG (2006). "Endogenous ligands of PACAP/VIP receptors in the autocrine-paracrine regulation of the adrenal gland". International Review of Cytology. 249: 1–51. doi:10.1016/S0074-7696(06)49001-X. ISBN 978-0-12-364653-8. PMID 16697281.
• Hill JM (2007). "Vasoactive intestinal peptide in neurodevelopmental disorders: therapeutic potential". Current Pharmaceutical Design. 13 (11): 1079–89. doi:10.2174/138161207780618975. PMID 17430171.
• Gonzalez-Rey E, Varela N, Chorny A, Delgado M (2007). "Therapeutical approaches of vasoactive intestinal peptide as a pleiotropic immunomodulator". Current Pharmaceutical Design. 13 (11): 1113–39. doi:10.2174/138161207780618966. PMID 17430175.
• "[Quaternary structure of rabbit skeletal muscle glycogen synthetase]". Doklady Akademii Nauk SSSR (in Russian). 222 (4): 997–1000. Jun 1975. PMID 807467.
• Kitamura K, Kangawa K, Kawamoto M, Ichiki Y, Matsuo H, Eto T (May 1992). "Isolation and characterization of peptides which act on rat platelets, from a pheochromocytoma". Biochemical and Biophysical Research Communications. 185 (1): 134–41. doi:10.1016/s0006-291x(05)80966-0. PMID 1318039.
• Glowa JR, Panlilio LV, Brenneman DE, Gozes I, Fridkin M, Hill JM (Jan 1992). "Learning impairment following intracerebral administration of the HIV envelope protein gp120 or a VIP antagonist". Brain Research. 570 (1-2): 49–53. doi:10.1016/0006-8993(92)90562-n. PMID 1617429.
• Theriault Y, Boulanger Y, St-Pierre S (Mar 1991). "Structural determination of the vasoactive intestinal peptide by two-dimensional H-NMR spectroscopy". Biopolymers. 31 (4): 459–64. doi:10.1002/bip.360310411. PMID 1863695.
• Gozes I, Giladi E, Shani Y (Apr 1987). "Vasoactive intestinal peptide gene: putative mechanism of information storage at the RNA level". Journal of Neurochemistry. 48 (4): 1136–41. doi:10.1111/j.1471-4159.1987.tb05638.x. PMID 2434617.
• Yamagami T, Ohsawa K, Nishizawa M, Inoue C, Gotoh E, Yanaihara N, Yamamoto H, Okamoto H (1988). "Complete nucleotide sequence of human vasoactive intestinal peptide/PHM-27 gene and its inducible promoter". Annals of the New York Academy of Sciences. 527: 87–102. doi:10.1111/j.1749-6632.1988.tb26975.x. PMID 2839091.
• Bodner M, Fridkin M, Gozes I (Jun 1985). "Coding sequences for vasoactive intestinal peptide and PHM-27 peptide are located on two adjacent exons in the human genome". Proceedings of the National Academy of Sciences of the United States of America. 82 (11): 3548–51. doi:10.1073/pnas.82.11.3548. PMC 397822. PMID 2987932.
• DeLamarter JF, Buell GN, Kawashima E, Polak JM, Bloom SR (1985). "Vasoactive intestinal peptide: expression of the prohormone in bacterial cells". Peptides. 6 Suppl 1 (Suppl 1): 95–102. doi:10.1016/0196-9781(85)90016-6. PMID 2995945.
• Linder S, Barkhem T, Norberg A, Persson H, Schalling M, Hökfelt T, Magnusson G (Jan 1987). "Structure and expression of the gene encoding the vasoactive intestinal peptide precursor". Proceedings of the National Academy of Sciences of the United States of America. 84 (2): 605–9. doi:10.1073/pnas.84.2.605. PMC 304259. PMID 3025882.
• Gotoh E, Yamagami T, Yamamoto H, Okamoto H (Sep 1988). "Chromosomal assignment of human VIP/PHM-27 gene to 6q26----q27 region by spot blot hybridization and in situ hybridization". Biochemistry International. 17 (3): 555–62. PMID 3202886.
• Yiangou Y, Di Marzo V, Spokes RA, Panico M, Morris HR, Bloom SR (Oct 1987). "Isolation, characterization, and pharmacological actions of peptide histidine valine 42, a novel prepro-vasoactive intestinal peptide-derived peptide". The Journal of Biological Chemistry. 262 (29): 14010–3. PMID 3654650.
• Gozes I, Bodner M, Shani Y, Fridkin M (1986). "Structure and expression of the vasoactive intestinal peptide (VIP) gene in a human tumor". Peptides. 7 Suppl 1 (Suppl 1): 1–6. doi:10.1016/0196-9781(86)90156-7. PMID 3748844.
• Tsukada T, Horovitch SJ, Montminy MR, Mandel G, Goodman RH (Aug 1985). "Structure of the human vasoactive intestinal polypeptide gene". Dna. 4 (4): 293–300. PMID 3899557.
• Heinz-Erian P, Dey RD, Flux M, Said SI (Sep 1985). "Deficient vasoactive intestinal peptide innervation in the sweat glands of cystic fibrosis patients". Science. 229 (4720): 1407–8. doi:10.1126/science.4035357. PMID 4035357.
• Bloom SR, Christofides ND, Delamarter J, Buell G, Kawashima E, Polak JM (Nov 1983). "Diarrhoea in vipoma patients associated with cosecretion of a second active peptide (peptide histidine isoleucine) explained by single coding gene". Lancet. 2 (8360): 1163–5. doi:10.1016/S0140-6736(83)91215-1. PMID 6139527.

External links

• Pathway at biocarta.com
• Physiology: 6/6ch2/s6ch2_34 - Essentials of Human Physiology