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The Roles of Integrin α5β1 in Human Cancer

Overview
Publisher Dove Medical Press
Specialty Oncology
Date 2021 Jan 7
PMID 33408483
Citations 50
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Abstract

Cell adhesion to the extracellular matrix has important roles in tissue integrity and human health. Integrins are heterodimeric cell surface receptors that are composed by two non-covalently linked alpha and beta subunits that mainly participate in the interaction of cell-cell adhesion and cell-extracellular matrix and regulate cell motility, adhesion, differentiation, migration, proliferation, etc. In mammals, there have been eighteen α subunits and 8 β subunits and so far 24 distinct types of αβ integrin heterodimers have been identified in humans. Integrin α5β1, also known as the fibronectin receptor, is a heterodimer with α5 and β1 subunits and has emerged as an essential mediator in many human carcinomas. Integrin α5β1 alteration is closely linked to the progression of several types of human cancers, including cell proliferation, angiogenesis, tumor metastasis, and cancerogenesis. In this review, we will introduce the functions of integrin α5β1 in cancer progression and also explore its regulatory mechanisms. Additionally, the potential clinical applications as a target for cancer imaging and therapy are discussed. Collectively, the information reviewed here may increase the understanding of integrin α5β1 as a potential therapeutic target for cancer.

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References
1.
Naci D, Vuori K, Aoudjit F . Alpha2beta1 integrin in cancer development and chemoresistance. Semin Cancer Biol. 2015; 35:145-53. DOI: 10.1016/j.semcancer.2015.08.004. View

2.
Meng X, Jin Y, Yu Y, Bai J, Liu G, Zhu J . Characterisation of fibronectin-mediated FAK signalling pathways in lung cancer cell migration and invasion. Br J Cancer. 2009; 101(2):327-34. PMC: 2720209. DOI: 10.1038/sj.bjc.6605154. View

3.
Guo M, Sahni S, Sahni A, Francis C . Fibrinogen regulates the expression of inflammatory chemokines through NF-kappaB activation of endothelial cells. Thromb Haemost. 2004; 92(4):858-66. DOI: 10.1160/TH04-04-0261. View

4.
Roberts M, Woods A, Dale T, van der Sluijs P, Norman J . Protein kinase B/Akt acts via glycogen synthase kinase 3 to regulate recycling of alpha v beta 3 and alpha 5 beta 1 integrins. Mol Cell Biol. 2004; 24(4):1505-15. PMC: 344170. DOI: 10.1128/MCB.24.4.1505-1515.2004. View

5.
Subbaram S, DiPersio C . Integrin α3β1 as a breast cancer target. Expert Opin Ther Targets. 2011; 15(10):1197-210. PMC: 3212412. DOI: 10.1517/14728222.2011.609557. View