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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Integrin alpha-V''' is a [[protein]] that in humans is encoded by the ''ITGAV'' [[gene]].<ref name="pmid2454952">{{cite journal | vauthors = Sosnoski DM, Emanuel BS, Hawkins AL, van Tuinen P, Ledbetter DH, Nussbaum RL, Kaos FT, Schwartz E, Phillips D, Bennett JS | title = Chromosomal localization of the genes for the vitronectin and fibronectin receptors alpha subunits and for platelet glycoproteins IIb and IIIa | journal = The Journal of Clinical Investigation | volume = 81 | issue = 6 | pages = 1993–8 | date = June 1988 | pmid = 2454952 | pmc = 442653 | doi = 10.1172/JCI113548 }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1jv2}}, {{PDB2|1l5g}}, {{PDB2|1m1x}}, {{PDB2|1u8c}}
| Name = Integrin, alpha V (vitronectin receptor, alpha polypeptide, antigen CD51)
| HGNCid = 6150
| Symbol = ITGAV
| AltSymbols =; CD51; MSK8; VNRA
| OMIM = 193210
| ECnumber = 
| Homologene = 20510
| MGIid = 96608
| GeneAtlas_image1 = PBB_GE_ITGAV_202351_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0008305 |text = integrin complex}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007160 |text = cell-matrix adhesion}} {{GNF_GO|id=GO:0007229 |text = integrin-mediated signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3685
    | Hs_Ensembl = ENSG00000138448
    | Hs_RefseqProtein = NP_002201
    | Hs_RefseqmRNA = NM_002210
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 187163045
    | Hs_GenLoc_end = 187253872
    | Hs_Uniprot = P06756
    | Mm_EntrezGene = 16410
    | Mm_Ensembl = ENSMUSG00000027087
    | Mm_RefseqmRNA = NM_008402
    | Mm_RefseqProtein = NP_032428
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 83525354
    | Mm_GenLoc_end = 83604646
    | Mm_Uniprot = Q3U4C8
  }}
}}
'''Integrin, alpha V (vitronectin receptor, alpha polypeptide, antigen CD51)''', also known as '''ITGAV''', is a human [[gene]].


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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.<ref>{{cite web | title = Entrez Gene: ITGAV integrin, alpha V (vitronectin receptor, alpha polypeptide, antigen CD51)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3685| accessdate = }}</ref>
{{PBB_Summary
| section_title =
| summary_text = ITAGV encodes integrin alpha chain V. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. The I-domain containing integrin 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.<ref>{{cite web | title = Entrez Gene: ITGAV integrin, alpha V (vitronectin receptor, alpha polypeptide, antigen CD51)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3685| accessdate = }}</ref>
}}


==References==
==Alpha V class integrins==
{{reflist|2}}
In mammals the [[integrin]]s that include alpha-V are :
==Further reading==
<!-- excerpt from [[Integrin#vertebrate integrins]] -->
{| class="wikitable"
| '''Name''' || '''Synonyms''' || '''Distribution''' || '''Ligands'''
|-
| '''alpha-v beta-1|α<sub>V</sub>β<sub>1</sub>'''  ||  || ocular melanoma; neurological tumors  ||  [[vitronectin]]; fibrinogen
|-
| '''[[alpha-v beta-3|α<sub>V</sub>β<sub>3</sub>]]'''  || vitronectin receptor<ref name="pmid10037797">{{cite journal | vauthors = Hermann P, Armant M, Brown E, Rubio M, Ishihara H, Ulrich D, Caspary RG, Lindberg FP, Armitage R, Maliszewski C, Delespesse G, Sarfati M | title = The vitronectin receptor and its associated CD47 molecule mediates proinflammatory cytokine synthesis in human monocytes by interaction with soluble CD23 | journal = The Journal of Cell Biology | volume = 144 | issue = 4 | pages = 767–75 | date = February 1999 | pmid = 10037797 | pmc = 2132927 | doi = 10.1083/jcb.144.4.767 | url = http://www.jcb.org/cgi/pmidlookup?view=long&pmid=10037797 }}</ref> || activated endothelial cells, melanoma, glioblastoma||  [[vitronectin]],<ref name="pmid10037797"/> fibronectin, fibrinogen, [[osteopontin]], [[CYR61|Cyr61]]
|-
| '''[[alpha-v beta-5|α<sub>V</sub>β<sub>5</sub>]]'''  ||  || widespread, esp. fibroblasts, epithelial cells  ||  [[vitronectin]] and adenovirus
|-
| '''alpha-v beta-6|α<sub>V</sub>β<sub>6</sub>'''  ||  || proliferating epithelia, esp. lung and mammary gland  ||  [[fibronectin]]; [[TGFβ]]1+3
|-
| '''alpha-v beta-8|α<sub>V</sub>β<sub>8</sub>'''  ||  || neural tissue; peripheral nerve  ||  [[fibronectin]]; [[TGFβ]]1+3
|}
 
==Clinical significance==
Overexpression of the ITGAV gene is associated with progression and spread of [[colorectal cancer]],<ref name=Waisberg2014>[https://www.ncbi.nlm.nih.gov/pubmed/25275062 ''Overexpression of the ITGAV gene is associated with progression and spread of colorectal cancer.'' Waisberg et al. 2014]</ref> and prostate cancer.<ref name=Cooper2002>{{cite journal | vauthors = Cooper CR, Chay CH, Pienta KJ | title = The role of alpha(v)beta(3) in prostate cancer progression | journal = Neoplasia | volume = 4 | issue = 3 | pages = 191–4 | year = 2002 | pmid = 11988838 | pmc = 1531692 | doi = 10.1038/sj/neo/7900224 }}</ref>
 
==As a drug target==
The [[monoclonal antibody|mAbs]] [[intetumumab]], and [[abituzumab]] target this protein which is found on some tumour cells.<ref name="ÉlezKocáková2015">{{cite journal | vauthors = 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 | title = 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 | journal = Annals of Oncology | volume = 26 | issue = 1 | pages = 132–40 | date = January 2015 | pmid = 25319061 | doi = 10.1093/annonc/mdu474 }}</ref>
 
== See also ==
* [[Cluster of differentiation]]
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Horton MA | title = The alpha v beta 3 integrin "vitronectin receptor" | journal = The International Journal of Biochemistry & Cell Biology | volume = 29 | issue = 5 | pages = 721–5 | date = May 1997 | pmid = 9251239 | doi = 10.1016/S1357-2725(96)00155-0 }}
| citations =
* {{cite journal | vauthors = Porter JC, Hogg N | title = Integrins take partners: cross-talk between integrins and other membrane receptors | journal = Trends in Cell Biology | volume = 8 | issue = 10 | pages = 390–6 | date = October 1998 | pmid = 9789327 | doi = 10.1016/S0962-8924(98)01344-0 }}
*{{cite journal | author=Horton MA |title=The alpha v beta 3 integrin "vitronectin receptor". |journal=Int. J. Biochem. Cell Biol. |volume=29 |issue= 5 |pages= 721-5 |year= 1997 |pmid= 9251239 |doi= }}
* {{cite journal | vauthors = Sajid M, Stouffer GA | title = The role of alpha(v)beta3 integrins in vascular healing | journal = Thrombosis and Haemostasis | volume = 87 | issue = 2 | pages = 187–93 | date = February 2002 | pmid = 11858476 | doi =  }}
*{{cite journal | author=Porter JC, Hogg N |title=Integrins take partners: cross-talk between integrins and other membrane receptors. |journal=Trends Cell Biol. |volume=8 |issue= 10 |pages= 390-6 |year= 1999 |pmid= 9789327 |doi= }}
* {{cite journal | vauthors = Cooper CR, Chay CH, Pienta KJ | title = The role of alpha(v)beta(3) in prostate cancer progression | journal = Neoplasia | volume = 4 | issue = 3 | pages = 191–4 | year = 2002 | pmid = 11988838 | pmc = 1531692 | doi = 10.1038/sj/neo/7900224 }}
*{{cite journal | author=Sajid M, Stouffer GA |title=The role of alpha(v)beta3 integrins in vascular healing. |journal=Thromb. Haemost. |volume=87 |issue= 2 |pages= 187-93 |year= 2002 |pmid= 11858476 |doi=  }}
* {{cite journal | vauthors = Cacciari B, Spalluto G | title = Non peptidic alphavbeta3 antagonists: recent developments | journal = Current Medicinal Chemistry | volume = 12 | issue = 1 | pages = 51–70 | year = 2005 | pmid = 15638730 | doi = 10.2174/0929867053363522 }}
*{{cite journal | author=Cooper CR, Chay CH, Pienta KJ |title=The role of alpha(v)beta(3) in prostate cancer progression. |journal=Neoplasia |volume=4 |issue= 3 |pages= 191-4 |year= 2002 |pmid= 11988838 |doi= 10.1038/sj/neo/7900224 }}
* {{cite web |author=University of Edinburgh.  |title=Hope for transplant patients as study finds key to organ scarring. |journal=ScienceDaily. (2013, November 10). |year=2013 |access-date=December 2, 2014 |url=https://www.sciencedaily.com/releases/2013/11/131110184408.htm }}
*{{cite journal | author=Cacciari B, Spalluto G |title=Non peptidic alphavbeta3 antagonists: recent developments. |journal=Curr. Med. Chem. |volume=12 |issue= 1 |pages= 51-70 |year= 2005 |pmid= 15638730 |doi= }}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=3685}}
== External links ==
* {{MeshName|CD51+Antigen}}
*[http://cmkb.cellmigration.org/report.cgi?report=orth_overview&gene_id=3685 ITGAV] Info with links in the [http://www.cellmigration.org/index.shtml Cell Migration Gateway]
{{Clusters of differentiation}}
{{Integrins}}
[[Category:Clusters of differentiation]]
[[Category:Integrins]]


{{protein-stub}}
{{membrane-protein-stub}}
{{WikiDoc Sources}}

Latest revision as of 14:20, 2 December 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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

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.[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

Clinical significance

Overexpression of the ITGAV gene is associated with progression and spread of colorectal cancer,[4] and prostate cancer.[5]

As a drug target

The mAbs intetumumab, and abituzumab target this protein which is found on some tumour cells.[6]

See also

References

  1. 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.
  2. "Entrez Gene: ITGAV integrin, alpha V (vitronectin receptor, alpha polypeptide, antigen CD51)".
  3. 3.0 3.1 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.
  4. Overexpression of the ITGAV gene is associated with progression and spread of colorectal cancer. Waisberg et al. 2014
  5. 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.
  6. 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

External links