Integrin alpha6 cleavage: a novel modification to modulate cell migration.

ABSTRACT: Integrins play a major role in cell adhesion and migration. Previous work reported that a cleaved form of integrin alpha6 (alpha6p) was detected in invasive human prostate cancer tissue, absent in normal prostate tissue and was produced by urokinase-type Plasminogen Activator (uPA) in a plasmin-independent manner. Using site-directed mutagenesis we identified amino acid residues R594 and R595, located in the "stalk" region of integrin alpha6, as essential for cleavage. The cleavage site is located on the extracellular region of the protein between the beta-barrel domain and the thigh domain. Prostate cancer cells (PC3N) were stably transfected to overexpress the cleavable, wild-type (PC3N-alpha6-WT) or the non-cleavable form of integrin alpha6 (PC3N-alpha6-RR). The number of cells invading

SUBMITTER: Pawar SC 

PROVIDER: S-EPMC1905853 | biostudies-literature | 2007 Apr

REPOSITORIES: biostudies-literature