Integrin alpha V

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)[1]
Chromosome 2 (human)
Genomic location for ITGAV
Genomic location for ITGAV
Band2q32.1Start186,590,056 bp[1]
End186,680,901 bp[1]
Gene location (Mouse)
Chromosome 2 (mouse)
Chr.Chromosome 2 (mouse)[2]
Chromosome 2 (mouse)
Genomic location for ITGAV
Genomic location for ITGAV
Band2 D|2 49.33 cMStart83,554,741 bp[2]
End83,637,260 bp[2]
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
  • transforming growth factor beta binding
  • metal ion binding
  • voltage-gated calcium channel activity
  • virus receptor activity
  • protein kinase C binding
  • protease binding
  • extracellular matrix protein binding
  • extracellular matrix binding
  • fibronectin binding
  • opsonin binding
  • insulin-like growth factor I binding
  • protein binding
  • fibroblast growth factor binding
  • neuregulin binding
  • coreceptor activity
  • C-X3-C chemokine binding
  • signaling receptor binding
  • peptide binding
  • integrin binding
Cellular component
  • lamellipodium membrane
  • integrin alphav-beta3 complex
  • extracellular exosome
  • alphav-beta3 integrin-IGF-1-IGF1R complex
  • integral component of membrane
  • integrin alphav-beta5 complex
  • membrane
  • integrin alphav-beta8 complex
  • ruffle membrane
  • integrin complex
  • microvillus membrane
  • filopodium membrane
  • external side of plasma membrane
  • phagocytic vesicle
  • plasma membrane
  • integral component of plasma membrane
  • cell surface
  • cytosol
  • focal adhesion
  • cell junction
  • specific granule membrane
  • integrin alphav-beta6 complex
  • alphav-beta3 integrin-PKCalpha complex
  • alphav-beta3 integrin-HMGB1 complex
Biological process
  • regulation of phagocytosis
  • apoptotic cell clearance
  • endodermal cell differentiation
  • apolipoprotein A-I-mediated signaling pathway
  • negative chemotaxis
  • negative regulation of lipid storage
  • extracellular matrix organization
  • heterotypic cell-cell adhesion
  • positive regulation of cell migration
  • regulation of apoptotic cell clearance
  • substrate adhesion-dependent cell spreading
  • vascular endothelial growth factor receptor signaling pathway
  • cell-matrix adhesion
  • viral process
  • antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent
  • blood vessel development
  • negative regulation of entry of bacterium into host cell
  • integrin-mediated signaling pathway
  • calcium ion transmembrane transport
  • negative regulation of macrophage derived foam cell differentiation
  • negative regulation of extrinsic apoptotic signaling pathway
  • leukocyte migration
  • cell-substrate adhesion
  • negative regulation of lipoprotein metabolic process
  • negative regulation of lipid transport
  • extrinsic apoptotic signaling pathway in absence of ligand
  • positive regulation of cell adhesion
  • ERK1 and ERK2 cascade
  • cell growth
  • positive regulation of osteoblast proliferation
  • cell adhesion
  • angiogenesis
  • vasculogenesis
  • cellular calcium ion homeostasis
  • positive regulation of cytosolic calcium ion concentration
  • positive regulation of cell population proliferation
  • cell migration
  • neutrophil degranulation
  • positive regulation of MAPK cascade
  • cell adhesion mediated by integrin
  • viral entry into host cell
  • regulation of transforming growth factor beta activation
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[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Integrin alpha-V is a protein that in humans is encoded by the ITGAV gene.[5]

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.[6]

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[7] activated endothelial cells, melanoma, glioblastoma vitronectin,[7] 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

Clinical significance

Overexpression of the ITGAV gene is associated with progression and spread of colorectal cancer,[8] and prostate cancer.[9]

As a drug target

The mAbs intetumumab, and abituzumab target this protein which is found on some tumour cells.[10]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000138448 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027087 – Ensembl, 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, Kaos FT, Schwartz E, Phillips D, Bennett JS (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): 1993–8. doi:10.1172/JCI113548. PMC 442653. PMID 2454952.
  6. ^ "Entrez Gene: ITGAV integrin, alpha V (vitronectin receptor, alpha polypeptide, antigen CD51)".
  7. ^ a b 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". The Journal of Cell Biology. 144 (4): 767–75. doi:10.1083/jcb.144.4.767. PMC 2132927. PMID 10037797.
  8. ^ Waisberg J, De Souza VL, Affonso Junior RJ, Silva SR, Denadai MV, Margeotto FB, De Souza CS, Matos D (2014). "Overexpression of the ITGAV gene is associated with progression and spread of colorectal cancer". Anticancer Res. 34 (10): 5599–607. PMID 25275062.
  9. ^ 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.
  10. ^ Élez E, Kocáková I, Höhler T, Martens UM, Bokemeyer C, Van Cutsem E, Melichar B, Smakal M, Csőszi T, Topuzov E, Orlova R, Tjulandin S, Rivera F, Straub J, Bruns R, Quaratino S, Tabernero J (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): 132–40. doi:10.1093/annonc/mdu474. PMID 25319061.

Further reading

  • Horton MA (May 1997). "The alpha v beta 3 integrin "vitronectin receptor"". The International Journal of Biochemistry & Cell Biology. 29 (5): 721–5. doi:10.1016/S1357-2725(96)00155-0. PMID 9251239.
  • Porter JC, Hogg N (October 1998). "Integrins take partners: cross-talk between integrins and other membrane receptors". Trends in Cell Biology. 8 (10): 390–6. doi:10.1016/S0962-8924(98)01344-0. PMID 9789327.
  • Sajid M, Stouffer GA (February 2002). "The role of alpha(v)beta3 integrins in vascular healing". Thrombosis and Haemostasis. 87 (2): 187–93. doi:10.1055/s-0037-1612971. PMID 11858476. S2CID 76995133.
  • 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". Current Medicinal Chemistry. 12 (1): 51–70. doi:10.2174/0929867053363522. PMID 15638730.
  • University of Edinburgh (2013). "Hope for transplant patients as study finds key to organ scarring". ScienceDaily. Retrieved December 2, 2014.
  • v
  • t
  • e
  • 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

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151–200
201–250
251–300
301–350
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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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