| Literature DB >> 9824304 |
F Magherini1, E Giannoni, G Raugei, P Cirri, P Paoli, A Modesti, G Camici, G Ramponi.
Abstract
The low molecular weight phosphotyrosine protein phosphatase (LMW-PTP) is a 18 kDa cytosolic enzyme, involved in the negative regulation of cell proliferation. In different mammalian species LMW-PTPs are expressed in two molecular forms produced from a single primary transcript through an alternative splicing mechanism. In this paper we report the cloning, expression and characterization of mouse isoforms of LMW-PTPs (called m-IF1 and m-IF2), very similar to the corresponding rat and human isoenzymes. Moreover we have identified a third cDNA encoding a protein (m-IF2P) that presents three substitutions compared to m-IF2. This new isoform is still active on pNPP, although to a lower extent: this reduction is mainly due to the leucine to proline substitution in position 13, within the catalytic loop. The mRNA expression level of this isoform is comparable to those of m-IF1 and m-IF2. It is likely that a gene duplication process followed by mutations has generated this new gene.Entities:
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Year: 1998 PMID: 9824304 DOI: 10.1016/s0014-5793(98)01241-1
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124