Background: Low molecular weight protein tyrosine phosphatase (LMW-PTP) is a polymorphic protein with two major isoforms whose role in tumorigenesis is currently controversial.
Materials and methods: We characterized LMW-PTP genotype, isoform expression and activity in six different human breast cancer epithelial cell lines (ZR75, MDA-MB-231, MDA-MB-231BO, MCF7, MDA-MB-231BO2, MDA-MB-435) and compared them with MCF10A, a normal breast epithelial cell line.
Results: mRNA expression of the slow isoform was increased in almost all breast cancer cell lines and that of the fast isoform was reduced (p<0.05) in all breast cancer cell lines. Regarding enzymatic activity, only MCF7 had significantly lower (p<0.05) LMW-PTP activity compared to MCF10A.
Conclusion: Since these are novel and previously unreported findings, we propose that the differential expression of LMW-PTP fast and slow isoforms suggests their opposite roles in the tumorigenic process, with the fast isoform being anti-oncogenic and the slow isoform being oncogenic.
Keywords: LMW-PTP isoforms; Protein tyrosine phosphorylation; enzymatic activity; genotype; mRNA expression.