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The ITGB3 protein product is the integrin beta chain beta 3. Integrins are integral cell-surface proteins composed of an alpha chain and a beta chain. A given chain may combine with multiple partners resulting in different integrins. Integrin beta 3 is found along with the alpha IIb chain in platelets. Integrins are known to participate in cell adhesion as well as cell-surface-mediated signaling.[3]
Role in endometriosis
Defectively expressed β3 integrin subunit has been correlated with presence of endometriosis, and has been suggested as a putative marker of this condition.[4]
↑Heemskerk, J. W. M.; Mattheij, N. J. A.; Cosemans, J. M. E. M. (2013). "Platelet-based coagulation: different populations, different functions". Journal of Thrombosis and Haemostasis. 11 (1): 2–16. doi:10.1111/jth.12045. ISSN1538-7933.
↑May, K. E.; Villar, J.; Kirtley, S.; Kennedy, S. H.; Becker, C. M. (2011). "Endometrial alterations in endometriosis: A systematic review of putative biomarkers". Human Reproduction Update. 17 (5): 637–653. doi:10.1093/humupd/dmr013. PMID21672902.
↑Chung, J; Gao A G; Frazier W A (June 1997). "Thrombspondin acts via integrin-associated protein to activate the platelet integrin alphaIIbbeta3". J. Biol. Chem. UNITED STATES. 272 (23): 14740–6. doi:10.1074/jbc.272.23.14740. ISSN0021-9258. PMID9169439.
↑Fujimoto, Tetsuro-Takahiro; Katsutani Shinya; Shimomura Takeshi; Fujimura Kingo (January 2002). "Novel alternatively spliced form of beta(3)-endonexin". Thromb. Res. United States. 105 (1): 63–70. doi:10.1016/S0049-3848(01)00405-4. ISSN0049-3848. PMID11864709.
↑Patil, S; Jedsadayanmata A; Wencel-Drake J D; Wang W; Knezevic I; Lam S C (October 1999). "Identification of a talin-binding site in the integrin beta(3) subunit distinct from the NPLY regulatory motif of post-ligand binding functions. The talin n-terminal head domain interacts with the membrane-proximal region of the beta(3) cytoplasmic tail". J. Biol. Chem. UNITED STATES. 274 (40): 28575–83. doi:10.1074/jbc.274.40.28575. ISSN0021-9258. PMID10497223.
↑Calderwood, David A; Yan Boxu; de Pereda Jose M; Alvarez Begoña García; Fujioka Yosuke; Liddington Robert C; Ginsberg Mark H (June 2002). "The phosphotyrosine binding-like domain of talin activates integrins". J. Biol. Chem. United States. 277 (24): 21749–58. doi:10.1074/jbc.M111996200. ISSN0021-9258. PMID11932255.
↑Naik, U P; Patel P M; Parise L V (February 1997). "Identification of a novel calcium-binding protein that interacts with the integrin alphaIIb cytoplasmic domain". J. Biol. Chem. UNITED STATES. 272 (8): 4651–4. doi:10.1074/jbc.272.8.4651. ISSN0021-9258. PMID9030514.
Further reading
Bray PF (1995). "Inherited diseases of platelet glycoproteins: considerations for rapid molecular characterization". Thromb. Haemost. 72 (4): 492–502. PMID7878622.
Charakida M, Tousoulis D, Stefanadis C, Toutouzas P (2003). "The impact of platelet glycoprotein IIIa and Ia polymorphisms in cardiovascular thrombotic disease". Italian Heart Journal. 4 (1): 17–22. PMID12690916.
Smith FB, Connor JM, Lee AJ, et al. (2004). "Relationship of the platelet glycoprotein PlA and fibrinogen T/G+1689 polymorphisms with peripheral arterial disease and ischaemic heart disease". Thromb. Res. 112 (4): 209–16. doi:10.1016/j.thromres.2003.11.010. PMID14987913.
Fullard JF (2004). "The role of the platelet glycoprotein IIb/IIIa in thrombosis and haemostasis". Curr. Pharm. Des. 10 (14): 1567–76. doi:10.2174/1381612043384682. PMID15134555.