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.

Cloning of murine low molecular weight phosphotyrosine protein phosphatase cDNA: identification of a new isoform / F. Magherini; E. Giannoni;G. Raugei; P. Cirri; P. Paoli; A. Modesti; G. Camici; G. Ramponi. - In: FEBS LETTERS. - ISSN 0014-5793. - STAMPA. - 437:(1998), pp. 263-266.

Cloning of murine low molecular weight phosphotyrosine protein phosphatase cDNA: identification of a new isoform

MAGHERINI, FRANCESCA;GIANNONI, ELISA;RAUGEI, GIOVANNI;CIRRI, PAOLO;PAOLI, PAOLO;MODESTI, ALESSANDRA;CAMICI, GUIDO;RAMPONI, GIAMPIETRO
1998

Abstract

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.
1998
437
263
266
F. Magherini; E. Giannoni;G. Raugei; P. Cirri; P. Paoli; A. Modesti; G. Camici; G. Ramponi
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/310242
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