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

doi:10.1016/S0378-1119(00)00351-6

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 journal › Article › peer-review

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 language	English
Pages (from-to)	45-55
Number of pages	11
Journal	Gene
Volume	257
Issue number	1
DOIs	https://doi.org/10.1016/S0378-1119(00)00351-6
Publication status	Published - 2000 Oct 17
Externally published	Yes

Bibliographical note

Funding Information:
We thank Dr K.S. Rhee (Seoul National University, Seoul, South Korea) for providing testis cDNA library and Dr E. Borrelli, Dr A. Saiardi, Dr Y.D. Choi and Dr W.J. Lee for their comments and helpful discussions, and K.S. Chung and S.K. Ahn for technical assistance. B.J. Kim is the recipient of the Brain Korea 21 program for medical science from the Korea Ministry of Education. This work was supported by a non-directed research grant from the Korea Research Foundation, 1997 (to J.-H.B.), and partly by the Yonsei University College of Medicine Faculty Grant, 1996 (to J.-H.B.).

Keywords

Cytoskeletal protein
Protein tyrosine phosphatase
Spermatogenesis
Testis

ASJC Scopus subject areas

Genetics

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10.1016/S0378-1119(00)00351-6

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

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.",

keywords = "Cytoskeletal protein, Protein tyrosine phosphatase, Spermatogenesis, Testis",

author = "Park, {Kye Won} and Lee, {Eun Jin} and Lee, {Soo Hyun} and Lee, {Jong Eun} and Choi, {Eun Young} and Kim, {Byung Jin} and Ranjoo Hwang and Park, {Kyung Ah} and Baik, {Ja Hyun}",

note = "Funding Information: We thank Dr K.S. Rhee (Seoul National University, Seoul, South Korea) for providing testis cDNA library and Dr E. Borrelli, Dr A. Saiardi, Dr Y.D. Choi and Dr W.J. Lee for their comments and helpful discussions, and K.S. Chung and S.K. Ahn for technical assistance. B.J. Kim is the recipient of the Brain Korea 21 program for medical science from the Korea Ministry of Education. This work was supported by a non-directed research grant from the Korea Research Foundation, 1997 (to J.-H.B.), and partly by the Yonsei University College of Medicine Faculty Grant, 1996 (to J.-H.B.).",

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T1 - Molecular cloning and characterization of a protein tyrosine phosphatase enriched in testis, a putative murine homologue of human PTPMEG

AU - Park, Kye Won

AU - Lee, Eun Jin

AU - Lee, Soo Hyun

AU - Lee, Jong Eun

AU - Choi, Eun Young

AU - Kim, Byung Jin

AU - Hwang, Ranjoo

AU - Park, Kyung Ah

AU - Baik, Ja Hyun

N1 - Funding Information: We thank Dr K.S. Rhee (Seoul National University, Seoul, South Korea) for providing testis cDNA library and Dr E. Borrelli, Dr A. Saiardi, Dr Y.D. Choi and Dr W.J. Lee for their comments and helpful discussions, and K.S. Chung and S.K. Ahn for technical assistance. B.J. Kim is the recipient of the Brain Korea 21 program for medical science from the Korea Ministry of Education. This work was supported by a non-directed research grant from the Korea Research Foundation, 1997 (to J.-H.B.), and partly by the Yonsei University College of Medicine Faculty Grant, 1996 (to J.-H.B.).

PY - 2000/10/17

Y1 - 2000/10/17

N2 - 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.

AB - 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.

KW - Cytoskeletal protein

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KW - Spermatogenesis

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DO - 10.1016/S0378-1119(00)00351-6

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AN - SCOPUS:0034680356

SN - 0378-1119

VL - 257

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JF - Gene

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ER -

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

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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