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Regulation and Functions of Integrin α2 in Cell Adhesion and Disease

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Journal Genes Dis
Date 2019 Mar 26
PMID 30906828
Citations 64
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Abstract

Integrins are cell adhesion molecules that are composed of an alpha (α) subunit and a beta (β) subunit with affinity for different extracellular membrane components. The integrin family includes 24 known members that actively regulate cellular growth, differentiation, and apoptosis. Each integrin heterodimer has a particular function in defined contexts as well as some partially overlapping features with other members in the family. As many reviews have covered the general integrin family in molecular and cellular studies in life science, this review will focus on the specific regulation, function, and signaling of integrin α2 subunit (CD49b, VLA-2; encoded by the gene ) in partnership with β1 (CD29) subunit in normal and cancer cells. Its roles in cell adhesion, cell motility, angiogenesis, stemness, and immune/blood cell regulations are discussed. The pivotal role of integrin α2 in many diseases such as cancer suggests its potential to be used as a novel therapeutic target.

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References
1.
Emsley J, Knight C, Farndale R, Barnes M, Liddington R . Structural basis of collagen recognition by integrin alpha2beta1. Cell. 2000; 101(1):47-56. DOI: 10.1016/S0092-8674(00)80622-4. View

2.
Liu A . Differential expression of cell surface molecules in prostate cancer cells. Cancer Res. 2000; 60(13):3429-34. View

3.
Bouvard D, Brakebusch C, Gustafsson E, Aszodi A, Bengtsson T, Berna A . Functional consequences of integrin gene mutations in mice. Circ Res. 2001; 89(3):211-23. DOI: 10.1161/hh1501.094874. View

4.
Gout S, Jacquier-Sarlin M, Rousselle P, Block M . RhoA-dependent switch between alpha2beta1 and alpha3beta1 integrins is induced by laminin-5 during early stage of HT-29 cell differentiation. Mol Biol Cell. 2001; 12(10):3268-81. PMC: 60172. DOI: 10.1091/mbc.12.10.3268. View

5.
Holtkotter O, Nieswandt B, Smyth N, Muller W, Hafner M, Schulte V . Integrin alpha 2-deficient mice develop normally, are fertile, but display partially defective platelet interaction with collagen. J Biol Chem. 2002; 277(13):10789-94. DOI: 10.1074/jbc.M112307200. View