Integrin beta 1

'''Integrin beta-1''' ('''ITGB1'''), also known as '''CD29''', is a [[cell surface receptor]] that in humans is encoded by the ''ITGB1'' [[gene]].<ref name="pmid2524991">{{cite journal | vauthors = Goodfellow PJ, Nevanlinna HA, Gorman P, Sheer D, Lam G, Goodfellow PN | title = Assignment of the gene encoding the beta-subunit of the human fibronectin receptor (beta-FNR) to chromosome 10p11.2 | journal = Annals of Human Genetics | volume = 53 | issue = Pt 1 | pages = 15–22 | date = Jan 1989 | pmid = 2524991 | doi = 10.1111/j.1469-1809.1989.tb01118.x | s2cid = 36485270 }}</ref> This [[integrin]] associates with [[integrin alpha 1]] and [[integrin alpha 2]] to form integrin complexes which function as [[collagen receptor]]s. It also forms dimers with [[CD49c|integrin alpha 3]] to form integrin receptors for [[NTN1|netrin 1]] and [[reelin]]. These and other integrin beta 1 complexes have been historically known as very late activation (VLA) antigens.

Integrin beta 1 is expressed as at least four different [[isoforms]]. In [[cardiac muscle]] and [[skeletal muscle]], the integrin beta-1D isoform is specifically expressed, and localizes to [[costamere]]s, where it aids in the lateral force transmission from the [[sarcomere|Z-discs]] to the [[extracellular matrix]]. Abnormal levels of integrin beta-1D have been found in [[limb girdle muscular dystrophy]] and [[polyneuropathy]].

== Structure ==

Integrin beta-1 can exist as different [[isoform]]s via [[alternative splicing]]. Six [[alternative splicing|alternatively spliced]] variants have been found for this gene which encode five proteins with alternate [[C-terminus|C-termini]].<ref>{{cite web | title = Entrez Gene: ITGB1 integrin, beta 1 (fibronectin receptor, beta polypeptide, antigen CD29 includes MDF2, MSK12)| url = https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=3688}}</ref> Integrin receptors exist as heterodimers, and greater than 20 different integrin heterodimeric receptors have been described. All integrins, alpha and beta forms, have large extracellular and short intracellular domains.<ref name = "Hynes_1992">{{cite journal | vauthors = Hynes RO | title = Integrins: versatility, modulation, and signaling in cell adhesion | journal = Cell | volume = 69 | issue = 1 | pages = 11–25 | date = Apr 1992 | pmid = 1555235 | doi=10.1016/0092-8674(92)90115-s| s2cid = 32774108 }}</ref> The cytoplasmic domain of integrin beta-1 binds to the [[actin]] [[cytoskeleton]].<ref name = "Sastry_1993">{{cite journal | vauthors = Sastry SK, Horwitz AF | title = Integrin cytoplasmic domains: mediators of cytoskeletal linkages and extra- and intracellular initiated transmembrane signaling | journal = Current Opinion in Cell Biology | volume = 5 | issue = 5 | pages = 819–31 | date = Oct 1993 | pmid = 8240826 | doi=10.1016/0955-0674(93)90031-k}}</ref> Integrin beta-1 is the most abundant beta-integrin expressed and associates with at least 10 different integrin-alpha subunits.<ref name = "Hynes_1992"/>

== Function ==

Integrin family members are membrane receptors involved in cell adhesion and recognition in a variety of processes including embryogenesis, [[hemostasis]], tissue repair, [[immune response]] and [[Collective–amoeboid transition|metastatic diffusion of tumor cells]].<ref name = "Hynes_1992"/> Integrins link the [[actin]] [[cytoskeleton]] with the [[extracellular matrix]] and they transmit signals bidirectionally between the [[extracellular matrix]] and [[cytoplasm]]ic domains.<ref>{{cite journal | vauthors = Burridge K, Chrzanowska-Wodnicka M | title = Focal adhesions, contractility, and signaling | journal = Annual Review of Cell and Developmental Biology | volume = 12 | pages = 463–518 | date = 1996 | pmid = 8970735 | doi = 10.1146/annurev.cellbio.12.1.463 | s2cid = 28558568 | url = https://cdr.lib.unc.edu/record/uuid:96bc6692-90a2-4deb-9a12-825223b5501c }}</ref><ref>{{cite journal | vauthors = Schwartz MA, Schaller MD, Ginsberg MH | title = Integrins: emerging paradigms of signal transduction | journal = Annual Review of Cell and Developmental Biology | volume = 11 | pages = 549–99 | date = 1995 | pmid = 8689569 | doi = 10.1146/annurev.cb.11.110195.003001 }}</ref> Beta-integrins are primarily responsible for targeting integrin dimers to the appropriate subcellular locations, which in adhesive cells is mainly [[focal adhesion]]s.<ref name = "Sastry_1993"/><ref>{{cite journal | vauthors = LaFlamme SE, Akiyama SK, Yamada KM | title = Regulation of fibronectin receptor distribution | journal = The Journal of Cell Biology | volume = 117 | issue = 2 | pages = 437–47 | date = Apr 1992 | pmid = 1373145 | doi=10.1083/jcb.117.2.437 | pmc=2289425}}</ref> Integrin beta-1 mutants lose the ability to target to sites of [[focal adhesion]]s.<ref>{{cite journal | vauthors = Akiyama SK, Yamada SS, Yamada KM, LaFlamme SE | title = Transmembrane signal transduction by integrin cytoplasmic domains expressed in single-subunit chimeras | journal = The Journal of Biological Chemistry | volume = 269 | issue = 23 | pages = 15961–4 | date = Jun 1994 | doi = 10.1016/S0021-9258(17)33955-8 | pmid = 7515874 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Reszka AA, Hayashi Y, Horwitz AF | title = Identification of amino acid sequences in the integrin beta 1 cytoplasmic domain implicated in cytoskeletal association | journal = The Journal of Cell Biology | volume = 117 | issue = 6 | pages = 1321–30 | date = Jun 1992 | pmid = 1376731 | doi=10.1083/jcb.117.6.1321 | pmc=2289496}}</ref>

Three novel isoforms of integrin beta-1 have been identified, termed beta-1B, beta-1C and beta-1D. Integrin beta-1B is transcribed when the proximal 26 [[amino acid]]s of the [[cytoplasm]]ic domain in exon 6 are retained and then succeeded by a 12 [[amino acid]] stretch from an adjacent [[intron]]ic region.<ref>{{cite journal | vauthors = Altruda F, Cervella P, Tarone G, Botta C, Balzac F, Stefanuto G, Silengo L | title = A human integrin beta 1 subunit with a unique cytoplasmic domain generated by alternative mRNA processing | journal = Gene | volume = 95 | issue = 2 | pages = 261–6 | date = Nov 1990 | pmid = 2249781 | doi=10.1016/0378-1119(90)90369-3}}</ref> The integrin beta-1B [[isoform]] appears to act as a dominant negative in that it inhibits cell adhesion.<ref>{{cite journal | vauthors = Balzac F, Retta SF, Albini A, Melchiorri A, Koteliansky VE, Geuna M, Silengo L, Tarone G | title = Expression of beta 1B integrin isoform in CHO cells results in a dominant negative effect on cell adhesion and motility | journal = The Journal of Cell Biology | volume = 127 | issue = 2 | pages = 557–65 | date = Oct 1994 | pmid = 7523423 | doi=10.1083/jcb.127.2.557 | pmc=2120206| hdl = 2318/39410 }}</ref> A second integrin beta-1 [[isoform]], termed beta-1C, was described to have an additional 48 [[amino acid]]s appended to the 26 [[amino acid]]s in the [[cytoplasm]]ic domain;<ref>{{cite journal | vauthors = Languino LR, Ruoslahti E | title = An alternative form of the integrin beta 1 subunit with a variant cytoplasmic domain | journal = The Journal of Biological Chemistry | volume = 267 | issue = 10 | pages = 7116–20 | date = Apr 1992 | doi = 10.1016/S0021-9258(19)50545-2 | pmid = 1551917 | doi-access = free }}</ref> the function of this isoform was an inhibitory one on [[DNA synthesis]] in the [[G1 phase]] of the [[cell cycle]].<ref>{{cite journal | vauthors = Meredith J, Takada Y, Fornaro M, Languino LR, Schwartz MA | title = Inhibition of cell cycle progression by the alternatively spliced integrin beta 1C | journal = Science | volume = 269 | issue = 5230 | pages = 1570–2 | date = Sep 1995 | pmid = 7545312 | doi=10.1126/science.7545312| bibcode = 1995Sci...269.1570M }}</ref> The third [[isoform]], termed beta-1D, is a [[striated muscle]]-specific isoform, which replaces the canonical beta-1A [[isoform]] in [[cardiac muscle|cardiac]] and [[skeletal muscle]] cells. This [[isoform]] is produced from splicing into a novel additional exon between exons 6 and 7. The [[cytoplasm]]ic domain of integrin beta-1D replaces the distal 21 [[amino acid]]s (present in integrin beta-1A) with an alternative stretch of 24 [[amino acid]]s (13 unique).<ref>{{cite journal | vauthors = Zhidkova NI, Belkin AM, Mayne R | title = Novel isoform of beta 1 integrin expressed in skeletal and cardiac muscle | journal = Biochemical and Biophysical Research Communications | volume = 214 | issue = 1 | pages = 279–85 | date = Sep 1995 | pmid = 7545396 | doi = 10.1006/bbrc.1995.2285 | bibcode = 1995BBRC..214..279Z }}</ref><ref name = "van_der_Flier_1995">{{cite journal | vauthors = van der Flier A, Kuikman I, Baudoin C, van der Neut R, Sonnenberg A | title = A novel beta 1 integrin isoform produced by alternative splicing: unique expression in cardiac and skeletal muscle | journal = FEBS Letters | volume = 369 | issue = 2–3 | pages = 340–4 | date = Aug 1995 | pmid = 7544298 | doi=10.1016/0014-5793(95)00814-p| bibcode = 1995FEBSL.369..340V | s2cid = 86638879 | doi-access = free }}</ref>

Integrin beta-1D appears to be developmentally regulated during myofibrilogenesis,<ref name = "van_der_Flier_1995"/> appearing immediately following the fusion of [[myoblast]]s in [[C2C12]] cell with rising levels throughout [[myofibril]]lar differentiation.<ref name = "Belkin_1996">{{cite journal | vauthors = Belkin AM, Zhidkova NI, Balzac F, Altruda F, Tomatis D, Maier A, Tarone G, Koteliansky VE, Burridge K | title = Beta 1D integrin displaces the beta 1A isoform in striated muscles: localization at junctional structures and signaling potential in nonmuscle cells | journal = The Journal of Cell Biology | volume = 132 | issue = 1–2 | pages = 211–26 | date = Jan 1996 | pmid = 8567725 | doi=10.1083/jcb.132.1.211 | pmc=2120711}}</ref> Integrin beta-1D is specifically localized to [[costamere]]s and [[intercalated disc]]s of [[cardiac muscle]] and [[costamere]]s, [[myotendinous junction]]s and [[neuromuscular junction]]s of [[skeletal muscle]], and it appears to function in general like other integrins, as the clustering of beta-1D integrins on the surface of [[Chinese hamster ovary cell|CHO cells]] resulted in [[tyrosine]] [[phosphorylation]] of [[PTK2|pp125FAK]] and induced [[mitogen-activated protein kinase]] activation.<ref name = "Belkin_1996"/>

==Clinical significance== In patients with [[limb girdle muscular dystrophy]], type 2C, beta-1D integrin has been shown to be severely reduced in [[skeletal muscle]] biopsies, coordinate with a reduction in [[ITGA7|alpha 7B-integrin]] and [[FLNC|filamin 2]].<ref>{{cite journal | vauthors = Anastasi G, Cutroneo G, Trimarchi F, Santoro G, Bruschetta D, Bramanti P, Pisani A, Favaloro A | title = Evaluation of sarcoglycans, vinculin-talin-integrin system and filamin2 in alpha- and gamma-sarcoglycanopathy: an immunohistochemical study | journal = International Journal of Molecular Medicine | volume = 14 | issue = 6 | pages = 989–99 | date = Dec 2004 | pmid = 15547664 | doi = 10.3892/ijmm.14.6.989 }}</ref>

In patients with sensitive-motor [[polyneuropathy]], levels of [[ITGA7|integrin alpha-7B]], integrin beta-1D and [[agrin]] were significantly reduced nearly to undetectable levels; and this corresponded with lower [[mRNA]] levels.<ref>{{cite journal | vauthors = Anastasi G, Cutroneo G, Santoro G, Arco A, Rizzo G, Bramanti P, Rinaldi C, Sidoti A, Amato A, Favaloro A | title = Costameric proteins in human skeletal muscle during muscular inactivity | journal = Journal of Anatomy | volume = 213 | issue = 3 | pages = 284–95 | date = Sep 2008 | pmid = 18537849 | doi = 10.1111/j.1469-7580.2008.00921.x | pmc=2732038}}</ref>

== Interactions ==

CD29 has been shown to [[Protein-protein interaction|interact]] with {{div col|colwidth=20em}} * [[ACTN1]];<ref>{{cite journal | vauthors = Otey CA, Pavalko FM, Burridge K | title = An interaction between alpha-actinin and the beta 1 integrin subunit in vitro | journal = The Journal of Cell Biology | volume = 111 | issue = 2 | pages = 721–9 | date = Aug 1990 | pmid = 2116421 | doi=10.1083/jcb.111.2.721 | pmc=2116186}}</ref><ref>{{cite journal | vauthors = Otey CA, Vasquez GB, Burridge K, Erickson BW | title = Mapping of the alpha-actinin binding site within the beta 1 integrin cytoplasmic domain | journal = The Journal of Biological Chemistry | volume = 268 | issue = 28 | pages = 21193–7 | date = Oct 1993 | doi = 10.1016/S0021-9258(19)36909-1 | pmid = 7691808 | doi-access = free }}</ref> * [[CD46]],<ref name=pmid10741407>{{cite journal | vauthors = Lozahic S, Christiansen D, Manié S, Gerlier D, Billard M, Boucheix C, Rubinstein E | title = CD46 (membrane cofactor protein) associates with multiple beta1 integrins and tetraspans | journal = European Journal of Immunology | volume = 30 | issue = 3 | pages = 900–7 | date = Mar 2000 | pmid = 10741407 | doi = 10.1002/1521-4141(200003)30:3<900::AID-IMMU900>3.0.CO;2-X | doi-access = free }}</ref> * [[CD9]],<ref name=pmid8630057>{{cite journal | vauthors = Radford KJ, Thorne RF, Hersey P | title = CD63 associates with transmembrane 4 superfamily members, CD9 and CD81, and with beta 1 integrins in human melanoma | journal = Biochemical and Biophysical Research Communications | volume = 222 | issue = 1 | pages = 13–8 | date = May 1996 | pmid = 8630057 | doi = 10.1006/bbrc.1996.0690 | bibcode = 1996BBRC..222...13R }}</ref><ref name=pmid12175627>{{cite journal | vauthors = Mazzocca A, Carloni V, Sciammetta S, Cordella C, Pantaleo P, Caldini A, Gentilini P, Pinzani M | title = Expression of transmembrane 4 superfamily (TM4SF) proteins and their role in hepatic stellate cell motility and wound healing migration | journal = Journal of Hepatology | volume = 37 | issue = 3 | pages = 322–30 | date = Sep 2002 | pmid = 12175627 | doi = 10.1016/S0168-8278(02)00175-7 }}</ref> * [[FHL2]],<ref name=pmid10906324>{{cite journal | vauthors = Wixler V, Geerts D, Laplantine E, Westhoff D, Smyth N, Aumailley M, Sonnenberg A, Paulsson M | title = The LIM-only protein DRAL/FHL2 binds to the cytoplasmic domain of several alpha and beta integrin chains and is recruited to adhesion complexes | journal = The Journal of Biological Chemistry | volume = 275 | issue = 43 | pages = 33669–78 | date = Oct 2000 | pmid = 10906324 | doi = 10.1074/jbc.M002519200 | doi-access = free }}</ref> * [[Filamin]],<ref name= "pmid11807098">{{cite journal | vauthors = van der Flier A, Kuikman I, Kramer D, Geerts D, Kreft M, Takafuta T, Shapiro SS, Sonnenberg A | title = Different splice variants of filamin-B affect myogenesis, subcellular distribution, and determine binding to integrin [beta] subunits | journal = The Journal of Cell Biology | volume = 156 | issue = 2 | pages = 361–76 | date = Jan 2002 | pmid = 11807098 | pmc = 2199218 | doi = 10.1083/jcb.200103037 }}</ref><ref name=pmid9722563>{{cite journal | vauthors = Loo DT, Kanner SB, Aruffo A | title = Filamin binds to the cytoplasmic domain of the beta1-integrin. Identification of amino acids responsible for this interaction | journal = The Journal of Biological Chemistry | volume = 273 | issue = 36 | pages = 23304–12 | date = Sep 1998 | pmid = 9722563 | doi = 10.1074/jbc.273.36.23304 | doi-access = free }}</ref> * [[FLNB]],<ref name = "pmid11807098"/> * [[CD81]],<ref name=pmid12175627/><ref name=pmid10229664>{{cite journal | vauthors = Serru V, Le Naour F, Billard M, Azorsa DO, Lanza F, Boucheix C, Rubinstein E | title = Selective tetraspan-integrin complexes (CD81/alpha4beta1, CD151/alpha3beta1, CD151/alpha6beta1) under conditions disrupting tetraspan interactions | journal = The Biochemical Journal | volume = 340 | issue = Pt 1 | pages = 103–11 | date = May 1999 | pmid = 10229664 | pmc = 1220227 | doi = 10.1042/0264-6021:3400103 }}</ref> * [[GNB2L1]],<ref name=pmid12435334/><ref name=pmid9442085>{{cite journal | vauthors = Liliental J, Chang DD | title = Rack1, a receptor for activated protein kinase C, interacts with integrin beta subunit | journal = The Journal of Biological Chemistry | volume = 273 | issue = 4 | pages = 2379–83 | date = Jan 1998 | pmid = 9442085 | doi = 10.1074/jbc.273.4.2379 | doi-access = free }}</ref> * [[ITGB1BP1]],<ref name=pmid9281591>{{cite journal | vauthors = Chang DD, Wong C, Smith H, Liu J | title = ICAP-1, a novel beta1 integrin cytoplasmic domain-associated protein, binds to a conserved and functionally important NPXY sequence motif of beta1 integrin | journal = The Journal of Cell Biology | volume = 138 | issue = 5 | pages = 1149–57 | date = Sep 1997 | pmid = 9281591 | pmc = 2136751 | doi = 10.1083/jcb.138.5.1149 }}</ref><ref name=pmid11741908>{{cite journal | vauthors = Chang DD, Hoang BQ, Liu J, Springer TA | title = Molecular basis for interaction between Icap1 alpha PTB domain and beta 1 integrin | journal = The Journal of Biological Chemistry | volume = 277 | issue = 10 | pages = 8140–5 | date = Mar 2002 | pmid = 11741908 | doi = 10.1074/jbc.M109031200 | doi-access = free }}</ref> * [[LGALS8]],<ref name=pmid10852818>{{cite journal | vauthors = Hadari YR, Arbel-Goren R, Levy Y, Amsterdam A, Alon R, Zakut R, Zick Y | title = Galectin-8 binding to integrins inhibits cell adhesion and induces apoptosis | journal = Journal of Cell Science | volume = 113 | issue = 13| pages = 2385–97 | date = Jul 2000 | doi = 10.1242/jcs.113.13.2385 | pmid = 10852818 }}</ref> * [[MAP4K4]],<ref name=pmid11967148>{{cite journal | vauthors = Poinat P, De Arcangelis A, Sookhareea S, Zhu X, Hedgecock EM, Labouesse M, Georges-Labouesse E | title = A conserved interaction between beta1 integrin/PAT-3 and Nck-interacting kinase/MIG-15 that mediates commissural axon navigation in C. elegans | journal = Current Biology | volume = 12 | issue = 8 | pages = 622–31 | date = Apr 2002 | pmid = 11967148 | doi = 10.1016/S0960-9822(02)00764-9 | s2cid = 9977605 | doi-access = free | bibcode = 2002CBio...12..622P }}</ref> * [[NME1]],<ref name=pmid11919189>{{cite journal | vauthors = Fournier HN, Dupé-Manet S, Bouvard D, Lacombe ML, Marie C, Block MR, Albiges-Rizo C | title = Integrin cytoplasmic domain-associated protein 1alpha (ICAP-1alpha ) interacts directly with the metastasis suppressor nm23-H2, and both proteins are targeted to newly formed cell adhesion sites upon integrin engagement | journal = The Journal of Biological Chemistry | volume = 277 | issue = 23 | pages = 20895–902 | date = Jun 2002 | pmid = 11919189 | doi = 10.1074/jbc.M200200200 | doi-access = free}}</ref> * [[PKC alpha]],<ref name=pmid12435334>{{cite journal | vauthors = Lee HS, Millward-Sadler SJ, Wright MO, Nuki G, Al-Jamal R, Salter DM | title = Activation of Integrin-RACK1/PKCalpha signalling in human articular chondrocyte mechanotransduction | journal = Osteoarthritis and Cartilage | volume = 10 | issue = 11 | pages = 890–7 | date = Nov 2002 | pmid = 12435334 | doi = 10.1053/joca.2002.0842 | doi-access = free }}</ref><ref name=pmid12138200>{{cite journal | vauthors = Parsons M, Keppler MD, Kline A, Messent A, Humphries MJ, Gilchrist R, Hart IR, Quittau-Prevostel C, Hughes WE, Parker PJ, Ng T | title = Site-directed perturbation of protein kinase C- integrin interaction blocks carcinoma cell chemotaxis | journal = Molecular and Cellular Biology | volume = 22 | issue = 16 | pages = 5897–911 | date = Aug 2002 | pmid = 12138200 | pmc = 133968 | doi = 10.1128/MCB.22.16.5897-5911.2002 }}</ref> * [[TLN1]],<ref>{{cite journal | vauthors = Tapley P, Horwitz A, Buck C, Duggan K, Rohrschneider L | title = Integrins isolated from Rous sarcoma virus-transformed chicken embryo fibroblasts | journal = Oncogene | volume = 4 | issue = 3 | pages = 325–33 | date = Mar 1989 | pmid = 2468126 }}</ref><ref>{{cite journal | vauthors = Horwitz A, Duggan K, Buck C, Beckerle MC, Burridge K | title = Interaction of plasma membrane fibronectin receptor with talin--a transmembrane linkage | journal = Nature | volume = 320 | issue = 6062 | pages = 531–3 | date = 1986 | pmid = 2938015 | doi = 10.1038/320531a0 | bibcode = 1986Natur.320..531H | s2cid = 4356748 | url = https://cdr.lib.unc.edu/record/uuid:ccf789da-0198-42b3-99a9-8fe20c8109c7 }}</ref> * [[TSPAN4]],<ref name=pmid9360996>{{cite journal | vauthors = Tachibana I, Bodorova J, Berditchevski F, Zutter MM, Hemler ME | title = NAG-2, a novel transmembrane-4 superfamily (TM4SF) protein that complexes with integrins and other TM4SF proteins | journal = The Journal of Biological Chemistry | volume = 272 | issue = 46 | pages = 29181–9 | date = Nov 1997 | pmid = 9360996 | doi = 10.1074/jbc.272.46.29181 | doi-access = free }}</ref> and * [[YWHAB]].<ref name=pmid11313964>{{cite journal | vauthors = Han DC, Rodriguez LG, Guan JL | title = Identification of a novel interaction between integrin beta1 and 14-3-3beta | journal = Oncogene | volume = 20 | issue = 3 | pages = 346–57 | date = Jan 2001 | pmid = 11313964 | doi = 10.1038/sj.onc.1204068 | s2cid = 7405925 | doi-access = }}</ref> {{Div col end}} {{Clear}}

== References == {{reflist|33em}}

== Further reading == {{refbegin|33em}} * {{cite journal | vauthors = Evans JP | title = Fertilin beta and other ADAMs as integrin ligands: insights into cell adhesion and fertilization | journal = BioEssays | volume = 23 | issue = 7 | pages = 628–39 | date = Jul 2001 | pmid = 11462216 | doi = 10.1002/bies.1088 | s2cid = 23712246 }} * {{cite journal | vauthors = Armulik A | title = Splice variants of human beta 1 integrins: origin, biosynthesis and functions | journal = Frontiers in Bioscience | volume = 7 | issue = 1–3| pages = d219-27 | date = Jan 2002 | pmid = 11779688 | doi = 10.2741/armulik | doi-access = free }} * {{cite journal | vauthors = Brakebusch C, Fässler R | title = beta 1 integrin function in vivo: adhesion, migration and more | journal = Cancer and Metastasis Reviews | volume = 24 | issue = 3 | pages = 403–11 | date = Sep 2005 | pmid = 16258728 | doi = 10.1007/s10555-005-5132-5 | s2cid = 24210890 }} {{refend}}

== External links == * {{MeshName|CD29+Antigen}} * {{UCSC gene info|ITGB1}}

[[Category:Integrins]] [[Category:Clusters of differentiation]]