Alpha-v beta-3
αVβ3 is a type of integrin that is a receptor for vitronectin.[1] It consists of two components, integrin alpha V and integrin beta 3 (CD61), and is expressed by platelets. Furthermore, it is a receptor for phagocytosis on macrophages or dendritic cells.[2]
As a drug target
Integrin αVβ3 is a potential drug target because abnormal expression of v3 is linked to the development and progression of various diseases. Its role in angiogenesis, in cancer and other diseases, is linked to the blood supply for problematic overgrowths.[3]
Inhibitors like etaracizumab may be used as antiangiogenics.[4]
One novel protein (ProAgio) has been designed to bind at an unusual site, and then induces apoptosis by recruiting caspase 8.[3] It is designed by mutating domain 1 of CD2 (D1-CD2), which naturally binds weakly to the receptor.[5]
Fibronectin domain 10 contains the RGD motif that αVβ3 recognizes. A high-affinity, pure antagonist mutant has been discovered for this protein.[6]
See also
- Proteases in angiogenesis
- Vitaxin, a respective antibody
References
- ^ 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.
- ^ Yamaguchi H, Takagi J, Miyamae T, Yokota S, Fujimoto T, Nakamura S, Ohshima S, Naka T, Nagata S (May 2008). "Milk fat globule EGF factor 8 in the serum of human patients of systemic lupus erythematosus". Journal of Leukocyte Biology. 83 (5): 1300–7. doi:10.1189/jlb.1107730. PMID 18303131.
- ^ a b Novel Protein Agent Targets Cancer and Host of Other Diseases. June 2016
- ^ Santulli G, Basilicata MF, De Simone M, Del Giudice C, Anastasio A, Sorriento D, Saviano M, Del Gatto A, Trimarco B, Pedone C, Zaccaro L, Iaccarino G (January 2011). "Evaluation of the anti-angiogenic properties of the new selective αVβ3 integrin antagonist RGDechiHCit". Journal of Translational Medicine. 9 (1): 7. doi:10.1186/1479-5876-9-7. PMC 3027097. PMID 21232121.
- ^ Turaga, Ravi Chakra; Yin, Lu; Yang, Jenny J.; Lee, Hsiauwei; Ivanov, Ivaylo; Yan, Chunli; Yang, Hua; Grossniklaus, Hans E.; Wang, Siming; Ma, Cheng; Sun, Li; Liu, Zhi-Ren (31 May 2016). "Rational design of a protein that binds integrin αvβ3 outside the ligand binding site". Nature Communications. 7 (1): 11675. Bibcode:2016NatCo...711675T. doi:10.1038/ncomms11675. PMC 4895024. PMID 27241473.
- ^ Van Agthoven JF, Xiong JP, Alonso JL, Rui X, Adair BD, Goodman SL, Arnaout MA (April 2014). "Structural basis for pure antagonism of integrin αVβ3 by a high-affinity form of fibronectin". Nature Structural & Molecular Biology. 21 (4): 383–8. doi:10.1038/nsmb.2797. PMC 4012256. PMID 24658351.
External links
- integrin+alphaVbeta3 at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
 | This membrane protein–related article is a stub. You can help Wikipedia by expanding it. |