ITGAV

Integrin, alpha V
Rendering of 1JV2​
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1JV2​, 1L5G​, 1M1X​, 1U8C​, 3IJE​, 4G1E​, 4G1M​, 4MMX​, 4MMY​, 4MMZ​, 4O02​, 4UM8​, 4UM9​
Identifiers
Symbols	ITGAV ; CD51; MSK8; VNRA; VTNR
External IDs	OMIM: 193210 MGI: 96608 HomoloGene: 20510 ChEMBL: 3660 GeneCards: ITGAV Gene
Gene ontology Molecular function • virus receptor activity • opsonin binding • fibronectin binding • protease binding • protein kinase C binding • voltage-gated calcium channel activity • protein binding • insulin-like growth factor I binding • metal ion binding • transforming growth factor beta binding • extracellular matrix binding • extracellular matrix protein binding Cellular component • plasma membrane • integral component of plasma membrane • focal adhesion • integrin complex • external side of plasma membrane • cell surface • membrane • lamellipodium membrane • filopodium membrane • microvillus membrane • ruffle membrane • integrin alphav-beta3 complex • integrin alphav-beta5 complex • integrin alphav-beta8 complex • alphav-beta3 integrin-IGF-1-IGF1R complex • phagocytic vesicle • extracellular exosome Biological process • angiogenesis • antigen processing and presentation of peptide antigen via MHC class I • antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent • cell adhesion • cell-matrix adhesion • integrin-mediated signaling pathway • axon guidance • blood coagulation • positive regulation of cell proliferation • negative regulation of macrophage derived foam cell differentiation • negative regulation of lipid storage • cell growth • cell migration • extracellular matrix organization • positive regulation of cell migration • cell-substrate adhesion • negative regulation of lipid transport • positive regulation of osteoblast proliferation • heterotypic cell-cell adhesion • substrate adhesion-dependent cell spreading • endodermal cell differentiation • apolipoprotein A-I-mediated signaling pathway • antigen processing and presentation of exogenous peptide antigen via MHC class I • apoptotic cell clearance • negative regulation of low-density lipoprotein particle receptor biosynthetic process • positive regulation of cell adhesion • viral entry into host cell • vascular endothelial growth factor receptor signaling pathway • negative regulation of lipoprotein metabolic process • regulation of phagocytosis • leukocyte migration • negative chemotaxis • entry of symbiont into host cell by promotion of host phagocytosis • ERK1 and ERK2 cascade • calcium ion transmembrane transport • extrinsic apoptotic signaling pathway in absence of ligand • regulation of apoptotic cell clearance • negative regulation of entry of bacterium into host cell • negative regulation of extrinsic apoptotic signaling pathway Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	3685	16410
Ensembl	ENSG00000138448	ENSMUSG00000027087
UniProt	P06756	P43406
RefSeq (mRNA)	NM_001144999	NM_008402
RefSeq (protein)	NP_001138471	NP_032428
Location (UCSC)	Chr 2: 186.59 – 186.68 Mb	Chr 2: 83.72 – 83.81 Mb
PubMed search

Integrin alpha-V is a protein that in humans is encoded by the ITGAV gene.^[1]

ITAGV encodes integrin alpha chain V. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. Alpha V undergoes post-translational cleavage to yield disulfide-linked heavy and light chains, that combine with multiple integrin beta chains to form different integrins. Among the known associating beta chains (beta chains 1,3,5,6, and 8; 'ITGB1', 'ITGB3', 'ITGB5', 'ITGB6', and 'ITGB8'), each can interact with extracellular matrix ligands; the alpha V beta 3 integrin, perhaps the most studied of these, is referred to as the Vitronectin receptor (VNR). In addition to adhesion, many integrins are known to facilitate signal transduction.^[2]

Alpha V class integrins

In mammals the integrins that include alpha-V are :

Name	Synonyms	Distribution	Ligands
αVβ1		ocular melanoma; neurological tumors	vitronectin; fibrinogen
αVβ3	vitronectin receptor[3]	activated endothelial cells, melanoma, glioblastoma	vitronectin,[3] fibronectin, fibrinogen, osteopontin, Cyr61
αVβ5		widespread, esp. fibroblasts, epithelial cells	vitronectin and adenovirus
αVβ6		proliferating epithelia, esp. lung and mammary gland	fibronectin; TGFβ1+3
αVβ8		neural tissue; peripheral nerve	fibronectin; TGFβ1+3

As a drug target

The mAbs intetumumab, and abituzumab target this protein which is found on some tumour cells.

See also

• Cluster of differentiation

References

1. Sosnoski DM, Emanuel BS, Hawkins AL, van Tuinen P, Ledbetter DH, Nussbaum RL, Kaos FT, Schwartz E, Phillips D, Bennett JS; et al. (Aug 1988). "Chromosomal localization of the genes for the vitronectin and fibronectin receptors alpha subunits and for platelet glycoproteins IIb and IIIa". J Clin Invest 81 (6): 1993–8. doi:10.1172/JCI113548. PMC 442653. PMID 2454952.
2. "Entrez Gene: ITGAV integrin, alpha V (vitronectin receptor, alpha polypeptide, antigen CD51)".
3. Hermann P, Armant M, Brown E, Rubio M, Ishihara H, Ulrich D, Caspary RG, Lindberg FP, Armitage R, Maliszewski C, Delespesse G, Sarfati M (February 1999). "The vitronectin receptor and its associated CD47 molecule mediates proinflammatory cytokine synthesis in human monocytes by interaction with soluble CD23". J. Cell Biol. 144 (4): 767–75. doi:10.1083/jcb.144.4.767. PMC 2132927. PMID 10037797.

Further reading

• Horton MA (1997). "The alpha v beta 3 integrin "vitronectin receptor".". Int. J. Biochem. Cell Biol. 29 (5): 721–5. doi:10.1016/S1357-2725(96)00155-0. PMID 9251239.
• Porter JC, Hogg N (1999). "Integrins take partners: cross-talk between integrins and other membrane receptors.". Trends Cell Biol. 8 (10): 390–6. doi:10.1016/S0962-8924(98)01344-0. PMID 9789327.
• Sajid M, Stouffer GA (2002). "The role of alpha(v)beta3 integrins in vascular healing.". Thromb. Haemost. 87 (2): 187–93. PMID 11858476.
• Cooper CR, Chay CH, Pienta KJ (2002). "The role of alpha(v)beta(3) in prostate cancer progression.". Neoplasia 4 (3): 191–4. doi:10.1038/sj/neo/7900224. PMC 1531692. PMID 11988838.
• Cacciari B, Spalluto G (2005). "Non peptidic alphavbeta3 antagonists: recent developments.". Curr. Med. Chem. 12 (1): 51–70. doi:10.2174/0929867053363522. PMID 15638730.
• University of Edinburgh. (2013, November 10). Hope for transplant patients as study finds key to organ scarring. ScienceDaily. Retrieved December 2, 2014 from www.sciencedaily.com/releases/2013/11/131110184408.htm

External links

• CD51 Antigen at the US National Library of Medicine Medical Subject Headings (MeSH)
• ITGAV Info with links in the Cell Migration Gateway