Abstract

This chapter discusses the role of immunohistochemical detection of phosphatase of regenerating liver (PRL)-3 in human gastric carcinomas. Protein tyrosine phosphatases play a fundamental role in regulating diverse proteins that participate in every aspect of cellular physiologic and pathogenic processes. The proteins PRL-1, -2, and -3 represent a novel class of protein tyrosine phosphatise superfamily members, in that they possess a unique COOH-terminal prenylation motif, with a protein tyrosine phosphatase-active site, signature sequence CX5R. The PRLs are found to be associated with the early endosome and plasma membrane in their prenylated state, whereas nuclear localization of these phosphatases may occur in the absence of prenylation. PRLs share 75% amino-acid sequence similarity, the ScanProsite analysis reveals that the potential sites of phosphorylation, by several kinases, are quite different. Moreover, Northern blot analysis demonstrates that the preferential messenger ribonucleic acid (mRNA) expression pattern of these PRLs also differed among the organs, indicating that PRLs are quite divergent in their functions. The PRL family tyrosine phosphatases, PRL-3 enhance the growth of human embryonic kidney fibroblasts.

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