Editing Integrin (section)

== Vertebrate integrins ==
The following are 16 of the ~24 integrins found in vertebrates:
{| class="wikitable"
! Name !! Synonyms !! Distribution !! Ligands
 |-
 | '''α<sub>1</sub>β<sub>1</sub>'''  ||VLA-1 ||  Many  || [[Collagen]]s, [[laminin]]s<ref name="lodish">{{cite book | vauthors = Krieger M, Scott MP, Matsudaira PT, Lodish HF, Darnell JE, Zipursky L, Kaiser C, Berk A | title = Molecular cell biology | edition = fifth | publisher = W.H. Freeman and CO | location = New York | year = 2004 | isbn = 978-0-7167-4366-8 | url = https://archive.org/details/molecularcellbio00harv | url-access = registration }}</ref>
 |-
 | '''α<sub>2</sub>β<sub>1</sub>'''  || VLA-2||  Many  || Collagens, laminins<ref name=lodish/>
 |-
 | '''α<sub>3</sub>β<sub>1</sub>'''  || VLA-3||  Many  || Laminin-5 
 |-
 | '''[[VLA-4|α<sub>4</sub>β<sub>1</sub>]]'''  || VLA-4<ref name=lodish/> ||  [[Hematopoietic]] cells  ||  [[Fibronectin]], [[VCAM-1]]<ref name=lodish/>
 |-
 | '''[[LPAM-1|α<sub>4</sub>β<sub>7</sub>]]'''|| LPAM-1|| T cells ||  MAD-CAM1<ref>{{Cite journal |last1=Wang |first1=Caihong |last2=McDonough |first2=Jacquelyn S. |last3=McDonald |first3=Keely G. |last4=Huang |first4=Conway |last5=Newberry |first5=Rodney D. |date=2008-09-15 |title=Alpha4beta7/MAdCAM-1 interactions play an essential role in transitioning cryptopatches into isolated lymphoid follicles and a nonessential role in cryptopatch formation |journal=Journal of Immunology |volume=181 |issue=6 |pages=4052–4061 |doi=10.4049/jimmunol.181.6.4052 |issn=1550-6606 |pmc=2778276 |pmid=18768861}}</ref><ref>{{Cite journal |last1=Wagner |first1=N. |last2=Löhler |first2=J. |last3=Kunkel |first3=E. J. |last4=Ley |first4=K. |last5=Leung |first5=E. |last6=Krissansen |first6=G. |last7=Rajewsky |first7=K. |last8=Müller |first8=W. |date=1996-07-25 |title=Critical role for beta7 integrins in formation of the gut-associated lymphoid tissue |url=https://pubmed.ncbi.nlm.nih.gov/8684468 |journal=Nature |volume=382 |issue=6589 |pages=366–370 |doi=10.1038/382366a0 |issn=0028-0836 |pmid=8684468}}</ref>
|-
 | '''[[alpha-5 beta-1|α<sub>5</sub>β<sub>1</sub>]]'''|| VLA-5; fibronectin receptor || widespread || fibronectin<ref name="lodish" /> and [[proteinase]]s
 |-
 | '''[[alpha-6 beta-1|α<sub>6</sub>β<sub>1</sub>]]'''|| VLA-6; laminin receptor|| widespread || laminins
 |-
 | '''[[alpha-7 beta-1|α<sub>7</sub>β<sub>1</sub>]]'''|| ||  muscle, glioma  || laminins
 |-
 | '''[[LFA-1|α<sub>L</sub>β<sub>2</sub>]]'''|| LFA-1<ref name="lodish" />||  [[T-lymphocyte]]s||  [[ICAM-1]], [[ICAM-2]]<ref name="lodish" />
 |-
 | '''[[Integrin alpha M|α<sub>M</sub>β<sub>2</sub>]]'''|| Mac-1, CR3<ref name="lodish" />|| [[Neutrophil]]s and [[monocyte]]s||  [[Blood plasma|Serum]] proteins, ICAM-1<ref name="lodish" />
 |-
 | '''[[Glycoprotein IIb/IIIa|α<sub>IIb</sub>β<sub>3</sub>]]'''||  Fibrinogen receptor; gpIIbIIIa<ref name="pmid9150551">{{cite journal |vauthors=Elangbam CS, Qualls CW, Dahlgren RR |date=January 1997 |title=Cell adhesion molecules--update |journal=Veterinary Pathology |volume=34 |issue=1 |pages=61–73 |doi=10.1177/030098589703400113 |pmid=9150551 |doi-access=}}</ref>|| [[Platelet]]s<ref name="lodish" />||  fibrinogen, fibronectin<ref name="lodish" />
 |-
 | '''[[alpha-v beta-1|α<sub>V</sub>β<sub>1</sub>]]'''|| || neurological tumors||  [[vitronectin]], [[osteopontin]],<ref name="PMID17910028">{{cite journal |last1=Kazanecki |first1=CC |last2=Uzwiak |first2=DJ |last3=Denhxxardt |first3=DT |date=1 November 2007 |title=Control of osteopontin signaling and function by post-translational phosphorylation and protein folding. |journal=Journal of Cellular Biochemistry |volume=102 |issue=4 |pages=912–24 |doi=10.1002/jcb.21558 |pmid=17910028 |s2cid=24240459}}</ref> 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 |date=February 1999 |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 |doi=10.1083/jcb.144.4.767 |pmc=2132927 |pmid=10037797}}</ref>|| activated endothelial cells, melanoma, glioblastoma  ||  [[vitronectin]],<ref name="pmid10037797" /> fibronectin, fibrinogen, [[osteopontin]],<ref name="PMID17910028" /> [[CYR61|Cyr61]], [[thyroxine]],<ref>{{cite journal |vauthors=Bergh JJ, Lin HY, Lansing L, Mohamed SN, Davis FB, Mousa S, Davis PJ |date=July 2005 |title=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 |journal=Endocrinology |volume=146 |issue=7 |pages=2864–71 |doi=10.1210/en.2005-0102 |pmid=15802494 |doi-access=free}}</ref> [[TETRAC]]
 |-
 | '''[[alpha-v beta-5|α<sub>V</sub>β<sub>5</sub>]]'''|| || widespread, esp. fibroblasts, epithelial cells  ||  [[vitronectin]], osteopontin,<ref name="PMID17910028" /> 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
|-
|'''α<sub>6</sub>β<sub>4</sub>'''
|
|[[Epithelial]] cells<ref name="lodish" />
|[[Laminin]]<ref name="lodish" />
|}

Beta-1 integrins interact with many alpha integrin chains. Gene knockouts of integrins in mice are not always lethal, which suggests that during embryonal development, one integrin may substitute its function for another in order to allow survival. Some integrins are on the cell surface in an inactive state, and can be rapidly primed, or put into a state capable of binding their ligands, by cytokines. Integrins can assume several different well-defined shapes or "conformational states". Once primed, the conformational state changes to stimulate ligand binding, which then activates the receptors — also by inducing a shape change — to trigger outside-in signal transduction.