Molecular cloning and characterization of a protein tyrosine phosphatase enriched in testis, a putative murine homologue of human PTPMEG

Kye Won Park, Eun Jin Lee, Soo Hyun Lee, Jong Eun Lee, Eun Young Choi, Byung Jin Kim, Ranjoo Hwang, Kyung Ah Park, Ja Hyun Baik

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

Protein tyrosine phosphorylation is regulated by protein tyrosine kinase and protein tyrosine phosphatase activities. These two counteracting proteins are implicated in cell growth and transformation. Using polymerase chain reaction with degenerate primers, we have identified a novel mouse protein tyrosine phosphatase (PTP). This cDNA contains a single open reading frame of the predicted 926 amino acids. Those predicted amino acids showed significant identity with human megakaryocyte protein-tyrosine phosphatase by 91% in nucleotide sequences and 94% in amino acid sequences. We have identified that expression of this PTP is highly enriched in the testis in mouse and human and has been termed here as a 'testis-enriched phosphatase' (TEP). Northern analysis detected two mRNA species of 3.7 and 3.2kb for this PTP in mouse testis and the expression of TEP is regulated during development. The recombinant phosphatase domain possesses protein tyrosine phosphatase activity when expressed in Escherichia coli. Immunohistochemical analysis of the cellular localization of TEP on mouse testis sections showed that this PTP is specifically expressed in spermatocytes and spermatids within seminiferous tubules, suggesting an important role in spermatogenesis. Copyright (C) 2000 Elsevier Science B.V.

Original languageEnglish
Pages (from-to)45-55
Number of pages11
JournalGene
Volume257
Issue number1
DOIs
Publication statusPublished - 2000 Oct 17
Externally publishedYes

Keywords

  • Cytoskeletal protein
  • Protein tyrosine phosphatase
  • Spermatogenesis
  • Testis

ASJC Scopus subject areas

  • Genetics

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