Characterization of rat receptor-like protein tyrosine phosphatase gamma isoforms.

We identified four isoforms of receptor-like protein tyrosine phosphatase gamma (RPTPgamma) from rat brain by cDNA cloning. We designated these molecules RPTPgamma-A, -B, -C, and -S. RPTPgamma-A was the longest form and had the same structure as human and mouse RPTPgamma. RPTPgamma-B lacked the intracellular juxtamembrane 29 amino acids of RPTPgamma-A. RPTPgamma-C had a single phosphatase domain. RPTPgamma-S is an extracellular variant of RPTPgamma. mRNAs of the four isoforms were expressed in the brain, kidney, lung, and heart. Transfection of RPTPgamma-A and -S expression plasmids into COS7 cells resulted in the expression of membrane-bound 190-kDa proteins and secreted 120-kDa proteins, respectively. These molecules were similar to PTPzeta/RPTPbeta with regard not only to structure but also to the presence of both secretory and transmembrane forms. However, RPTPgamma isoforms were not expressed as proteoglycans.