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Integrin alpha V

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(Redirected from ITGAV) Mammalian protein found in Homo sapiens

ITGAV
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1JV2, 1L5G, 1M1X, 1U8C, 3IJE, 4G1E, 4G1M, 4MMX, 4MMY, 4MMZ, 4O02, 4UM8, 4UM9

Identifiers
AliasesITGAV, CD51, MSK8, VNRA, VTNR, integrin subunit alpha V
External IDsOMIM: 193210; MGI: 96608; HomoloGene: 20510; GeneCards: ITGAV; OMA:ITGAV - orthologs
Gene location (Human)
Chromosome 2 (human)
Chr.Chromosome 2 (human)
Chromosome 2 (human)Genomic location for ITGAVGenomic location for ITGAV
Band2q32.1Start186,590,056 bp
End186,680,901 bp
Gene location (Mouse)
Chromosome 2 (mouse)
Chr.Chromosome 2 (mouse)
Chromosome 2 (mouse)Genomic location for ITGAVGenomic location for ITGAV
Band2 D|2 49.33 cMStart83,554,741 bp
End83,637,260 bp
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • retinal pigment epithelium

  • Epithelium of choroid plexus

  • germinal epithelium

  • tibia

  • right ventricle

  • skin of hip

  • visceral pleura

  • glomerulus

  • metanephric glomerulus

  • parietal pleura
Top expressed in
  • cumulus cell

  • retinal pigment epithelium

  • renal corpuscle

  • conjunctival fornix

  • decidua

  • calvaria

  • epithelium of lens

  • body of femur

  • gastrula

  • external carotid artery
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

3685

16410

Ensembl

ENSG00000138448

ENSMUSG00000027087

UniProt

P06756

P43406

RefSeq (mRNA)

NM_001144999
NM_001145000
NM_002210

NM_008402
NM_001398691

RefSeq (protein)

NP_001138471
NP_001138472
NP_002201

NP_032428
NP_001385620

Location (UCSC)Chr 2: 186.59 – 186.68 MbChr 2: 83.55 – 83.64 Mb
PubMed search
Wikidata
View/Edit HumanView/Edit Mouse

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

Function

ITGAV 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.

Alpha V class integrins

In mammals the integrins that include alpha-V are :

Name Synonyms Distribution Ligands
αVβ1 neurological tumors vitronectin; fibrinogen
αVβ3 vitronectin receptor activated endothelial cells, melanoma, glioblastoma vitronectin, fibronectin, fibrinogen, osteopontin, Cyr61, thyroxine
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

Clinical significance

Overexpression of the ITGAV gene is associated with progression and spread of colorectal cancer, and prostate cancer.

As a drug target

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

See also

References

  1. ^ GRCh38: Ensembl release 89: ENSG00000138448Ensembl, May 2017
  2. ^ GRCm38: Ensembl release 89: ENSMUSG00000027087Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Sosnoski DM, Emanuel BS, Hawkins AL, van Tuinen P, Ledbetter DH, Nussbaum RL, et al. (June 1988). "Chromosomal localization of the genes for the vitronectin and fibronectin receptors alpha subunits and for platelet glycoproteins IIb and IIIa". The Journal of Clinical Investigation. 81 (6): 1993–1998. doi:10.1172/JCI113548. PMC 442653. PMID 2454952.
  6. "Entrez Gene: ITGAV integrin, alpha V (vitronectin receptor, alpha polypeptide, antigen CD51)".
  7. ^ Hermann P, Armant M, Brown E, Rubio M, Ishihara H, Ulrich D, et al. (February 1999). "The vitronectin receptor and its associated CD47 molecule mediates proinflammatory cytokine synthesis in human monocytes by interaction with soluble CD23". The Journal of Cell Biology. 144 (4): 767–775. doi:10.1083/jcb.144.4.767. PMC 2132927. PMID 10037797.
  8. Bergh JJ, Lin HY, Lansing L, Mohamed SN, Davis FB, Mousa S, et al. (July 2005). "Integrin alphaVbeta3 contains a cell surface receptor site for thyroid hormone that is linked to activation of mitogen-activated protein kinase and induction of angiogenesis". Endocrinology. 146 (7): 2864–2871. doi:10.1210/en.2005-0102. PMID 15802494.
  9. Schmohl KA, Han Y, Tutter M, Schwenk N, Sarker RS, Steiger K, et al. (December 2020). "Integrin αvβ3-dependent thyroid hormone effects on tumour proliferation and vascularisation". Endocrine-Related Cancer. 27 (12): 685–697. doi:10.1530/ERC-20-0353. PMID 33112795.
  10. Waisberg J, De Souza Viana L, Affonso Junior RJ, Silva SR, Denadai MV, Margeotto FB, et al. (October 2014). "Overexpression of the ITGAV gene is associated with progression and spread of colorectal cancer". Anticancer Research. 34 (10): 5599–5607. PMID 25275062.
  11. Cooper CR, Chay CH, Pienta KJ (2002). "The role of alpha(v)beta(3) in prostate cancer progression". Neoplasia. 4 (3): 191–194. doi:10.1038/sj.neo.7900224. PMC 1531692. PMID 11988838.
  12. Élez E, Kocáková I, Höhler T, Martens UM, Bokemeyer C, Van Cutsem E, et al. (January 2015). "Abituzumab combined with cetuximab plus irinotecan versus cetuximab plus irinotecan alone for patients with KRAS wild-type metastatic colorectal cancer: the randomised phase I/II POSEIDON trial". Annals of Oncology. 26 (1): 132–140. doi:10.1093/annonc/mdu474. PMID 25319061.

Further reading

PDB gallery
  • 1jv2: CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN ALPHAVBETA3 1jv2: CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN ALPHAVBETA3
  • 1l5g: CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN AVB3 IN COMPLEX WITH AN ARG-GLY-ASP LIGAND 1l5g: CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN AVB3 IN COMPLEX WITH AN ARG-GLY-ASP LIGAND
  • 1m1x: CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN ALPHA VBETA3 BOUND TO MN2+ 1m1x: CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN ALPHA VBETA3 BOUND TO MN2+
  • 1u8c: A novel adaptation of the integrin PSI domain revealed from its crystal structure 1u8c: A novel adaptation of the integrin PSI domain revealed from its crystal structure

External links

Proteins: clusters of differentiation (see also list of human clusters of differentiation)
1–50
51–100
101–150
151–200
201–250
251–300
301–350
Integrins
Alpha
Beta
Dimers
Cytoadhesin receptor:
Fibrinogen receptor:
Fibronectin receptor:
Leukocyte-adhesion receptor:
Very late antigen receptor:
Vitronectin receptor:
see also cell surface receptor deficiencies
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