Integrin clipping: a novel adhesion switch?
During human prostate cancer progression, the majority of normally expressed integrins are suppressed with the exception of the alpha6, alpha3, and beta1 integrins. We have shown that in prostate cancer, the alpha6 integrin is found paired with the beta1 integrin and that a novel form of the alpha6 integrin that lacks a large portion of the extracellular domain (alpha6p) exists. The alpha6pbeta1 integrin is found in human prostate cancer tissue specimens as well as tissue culture cell lines and is formed on the cell surface. This review discusses the mechanism of alpha6pbeta1 production and the potential functions of this integrin variant. Our current working model predicts that the alpha6pbeta1 integrin maintains the intracellular cytoskeletal connections associated with the heterodimer while allowing for an alteration in cell adhesion. The mechanism provides a selective advantage for cancer cell metastasis.
Demetriou
Manolis C
MC
Department of Cell Biology and Anatomy, The Arizona Cancer Center, Tucson, Arizona 85724, USA.
Cress
Anne E
AE
D002448:Cell Adhesion; D006801:Humans; D039422:Integrin alpha3 / Q000378:metabolism*; D039503:Integrin alpha6 / Q000378:metabolism*; D019012:Integrin beta1 / Q000378:metabolism*; D008297:Male; D011471:Prostatic Neoplasms / Q000378:metabolism*; D020033:Protein Isoforms / Q000378:metabolism; D014568:Urokinase-Type Plasminogen Activator / Q000378:metabolism*
D039422:Integrin alpha3; D039503:Integrin alpha6; D019012:Integrin beta1; D020033:Protein Isoforms; D014568:Urokinase-Type Plasminogen Activator