β1 Integrins as Therapeutic Targets to Disrupt Hallmarks of Cancer

Integrins belong to a large family of αβ heterodimeric transmembrane proteins first recognized as adhesion molecules that bind to dedicated elements of the extracellular matrix and also to other surrounding cells. As important sensors of the cell microenvironment, they regulate numerous signaling pa...

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Published inFrontiers in pharmacology Vol. 6; p. 279
Main Authors Blandin, Anne-Florence, Renner, Guillaume, Lehmann, Maxime, Lelong-Rebel, Isabelle, Martin, Sophie, Dontenwill, Monique
Format Journal Article
LanguageEnglish
Published Switzerland Frontiers 24.11.2015
Frontiers Media S.A
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Summary:Integrins belong to a large family of αβ heterodimeric transmembrane proteins first recognized as adhesion molecules that bind to dedicated elements of the extracellular matrix and also to other surrounding cells. As important sensors of the cell microenvironment, they regulate numerous signaling pathways in response to structural variations of the extracellular matrix. Biochemical and biomechanical cues provided by this matrix and transmitted to cells via integrins are critically modified in tumoral settings. Integrins repertoire are subjected to expression level modifications, in tumor cells, and in surrounding cancer-associated cells, implicated in tumor initiation and progression as well. As critical players in numerous cancer hallmarks, defined by Hanahan and Weinberg (2011), integrins represent pertinent therapeutic targets. We will briefly summarize here our current knowledge about integrin implications in those different hallmarks focusing primarily on β1 integrins.
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This article was submitted to Pharmacology of Anti-Cancer Drugs, a section of the journal Frontiers in Pharmacology
Edited by: Hervé Emonard, Université de Reims Champagne-Ardenne, France
Reviewed by: Stéphane Dedieu, Université de Reims Champagne-Ardenne, France; Anthony Lemarie, Institut National de la Santé et de la Recherche Médicale, France
ISSN:1663-9812
1663-9812
DOI:10.3389/fphar.2015.00279