Protein tyrosine phosphatases are enzymes that play a crucial role in the cell signal transduction process through dephosphorylation of the substrate. This communication and signaling within a cell can affect many cellular processes such as growth, migration, cell proliferation, gene transcription, and immune response. Low molecular weight protein tyrosine phosphatases (LMW-PTPs) are a group of 18 kDa soluble proteins that belong to Class II of cysteine based proteins in the PTP family. Of critical importance is LMW-PTP’s link to increased cell invasivity, epithelial cell migration, and tumorigenesis. The protein is present in two active isoforms, Isoform A being anti-oncogenic and Isoform B being oncogenic. Overexpression of LMW-PTPs have been found in human breast, colon, bladder, and kidney tumor samples. This suggests selective inhibition of LMW-PTP’s Isoform B has the potential to serve as a novel therapeutic cancer treatment. Careful handling of the phosphatase protein is essential as each isoform is susceptible to oxidation, precipitation, and freeze/thaw effects. Analysis of the nature and kinetic activity of both LMW-PTP’s Isoform A and Isoform B through biological activity and inhibition kinetic assays can shed light on the potential for the successful selective inhibition of LMW-PTP for anti-cancer applications.

Expression, purification, and analysis of the biological activity of human low molecular weight protein tyrosine phosphatase

251st National Meeting (2016)

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