Literature DB >> 9047348

Molecular cloning and chromosomal localization of a human gene homologous to the murine R-PTP-kappa, a receptor-type protein tyrosine phosphatase.

Y Yang1, M C Gil, E Y Choi, S H Park, K H Pyun, H Ha.   

Abstract

Tyrosine phosphorylation of proteins plays an important role in cellular signaling and many cellular activities. The levels of cellular phosphorylation are reversibly controlled by protein tyrosine kinases and protein tyrosine phosphatases. The murine R-PTP-kappa, a receptor-type protein tyrosine phosphatase, has recently been cloned (Jiang et al. (1993) Mol. Cell. Biol. 13, 2942-2951). In order to identify the protein tyrosine phosphatases critical to the cellular signal transduction in human keratinocytes, a polymerase chain reaction (PCR)-based strategy was employed, and we have cloned a human homologue of the murine R-PTP-kappa. Here, we report the isolation of a complementary DNA encoding a human R-PTP-kappa. Of the several overlapping cDNA clones, one clone, which we originally termed p55-7, was found to encode a transmembrane protein of 1440 amino acids and was highly conserved with murine R-PTP-kappa with 98% identity at the amino-acid levels. The human R-PTP-kappa gene was localized to chromosome 6 by southern hybridization of DNA from a rodent/human somatic cell mapping panel. Northern blot analysis of RNA from several human tissues revealed, like the murine R-PTP-kappa, the presence of a major mRNA of approx. 7.0 kb and a minor mRNA of approx. 5.3 kb. In contrast to the expression of murine R-PTP-kappa which was highly expressed in liver and kidney, the human R-PTP-kappa was predominantly expressed in spleen, prostate, and ovary. However, the transcripts were detectable at various levels in all examined tissues (thymus, testis, small intestine, and colon) except for PBL (peripheral blood leukocytes). In addition, human R-PTP-kappa displayed a restricted pattern of expression among a series of cell lines, and was apparently expressed in an epidermal cells and cell lines (human normal keratinocytes, HaCaT, and A431), but was not detectable in other cell lines tested after longer exposure.

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Year:  1997        PMID: 9047348     DOI: 10.1016/s0378-1119(96)00684-1

Source DB:  PubMed          Journal:  Gene        ISSN: 0378-1119            Impact factor:   3.688


  9 in total

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2.  The crystal structure of human receptor protein tyrosine phosphatase kappa phosphatase domain 1.

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Journal:  Protein Sci       Date:  2006-05-02       Impact factor: 6.725

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Journal:  Biochem J       Date:  2002-02-01       Impact factor: 3.857

4.  The lysyl oxidase propeptide interacts with the receptor-type protein tyrosine phosphatase kappa and inhibits β-catenin transcriptional activity in lung cancer cells.

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5.  Transforming growth factor {beta} (TGF-{beta})-Smad target gene protein tyrosine phosphatase receptor type kappa is required for TGF-{beta} function.

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Journal:  Mol Cell Biol       Date:  2005-06       Impact factor: 4.272

6.  A deletion mutation of the protein tyrosine phosphatase kappa (Ptprk) gene is responsible for T-helper immunodeficiency (thid) in the LEC rat.

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7.  Analysis of PTPRK polymorphisms in association with risk and age at onset of Alzheimer's disease, cancer risk, and cholesterol.

Authors:  Yang Chen; Chun Xu; Sam Harirforoosh; Xingguang Luo; Ke-Sheng Wang
Journal:  J Psychiatr Res       Date:  2017-09-27       Impact factor: 4.791

8.  Genomic organization and alternative splicing of the human and mouse RPTPrho genes.

Authors:  J A Besco; A Frostholm; M C Popesco; A H Burghes; A Rotter
Journal:  BMC Genomics       Date:  2001-06-08       Impact factor: 3.969

9.  Inactivation of the catalytic phosphatase domain of PTPRT/RPTPρ increases social interaction in mice.

Authors:  Keerthi Thirtamara Rajamani; Brian O'Neill; Dawn D Han; Adrienne Frostholm; Andrej Rotter; Howard H Gu
Journal:  Autism Res       Date:  2014-06-03       Impact factor: 5.216

  9 in total

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