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Gene Review

Ptprj  -  protein tyrosine phosphatase, receptor...

Mus musculus

Synonyms: AI450271, BET, Byp, CD148, DEP-1, ...
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Disease relevance of Ptprj

  • Our recent experiments suggested that specific PTPases, PTP beta 2 and PTP epsilon, are involved in the early molecular events for in vitro differentiation of mouse erythroleukemia (MEL) as well as embryonic carcinoma (F9) cells [1].
  • Previously, we described in mouse strain CcS-19/Dem five susceptibility to colon cancer (Scc) loci, Scc1-Scc5 controlling tumor numbers [2].

High impact information on Ptprj


Biological context of Ptprj

  • The protein-tyrosine phosphatase DEP-1 modulates growth factor-stimulated cell migration and cell-matrix adhesion [6].
  • Using CcS-19, one of the highly susceptible RC strains, we mapped a novel colon tumor susceptibility gene, Scc-1, different from the oncogenes and tumor-suppressor genes known to be involved in colon tumorigenesis, in the vicinity of CD44 (Ly-24, Pgp-1) on chromosome 2 [7].
  • The putative Byp protein consists of 1238 amino acids, which possesses a single catalytic domain in the cytoplasmic region [8].
  • We have investigated the pattern of transcripts of PTPases during MEL cell differentiation and found that while the transcripts of most PTPases were unchanged or undetected in the cells, transcripts for two PTPases (PTP beta 2 and RIP) exhibited distinct patterns of induction at a very early stage of differentiation [9].
  • It has also been suggested that CD148 could be involved in mechanisms of differentiation and inhibition of cell growth [10].

Anatomical context of Ptprj


Associations of Ptprj with chemical compounds


Other interactions of Ptprj


Analytical, diagnostic and therapeutic context of Ptprj


  1. Chromosomal location of murine protein tyrosine phosphatase (Ptprj and Ptpre) genes. Watanabe, T., Mukouyama, Y., Rhodes, M., Thomas, M., Kume, T., Oishi, M. Genomics (1995) [Pubmed]
  2. Five new mouse susceptibility to colon cancer loci, Scc11-Scc15. Ruivenkamp, C.A., Csikós, T., Klous, A.M., van Wezel, T., Demant, P. Oncogene (2003) [Pubmed]
  3. Gene interaction and single gene effects in colon tumour susceptibility in mice. van Wezel, T., Stassen, A.P., Moen, C.J., Hart, A.A., van der Valk, M.A., Demant, P. Nat. Genet. (1996) [Pubmed]
  4. A mutant receptor tyrosine phosphatase, CD148, causes defects in vascular development. Takahashi, T., Takahashi, K., St John, P.L., Fleming, P.A., Tomemori, T., Watanabe, T., Abrahamson, D.R., Drake, C.J., Shirasawa, T., Daniel, T.O. Mol. Cell. Biol. (2003) [Pubmed]
  5. Regulated expression of the receptor-like tyrosine phosphatase CD148 on hemopoietic cells. Lin, J., Zhu, J.W., Baker, J.E., Weiss, A. J. Immunol. (2004) [Pubmed]
  6. The protein-tyrosine phosphatase DEP-1 modulates growth factor-stimulated cell migration and cell-matrix adhesion. Jandt, E., Denner, K., Kovalenko, M., Ostman, A., Böhmer, F.D. Oncogene (2003) [Pubmed]
  7. Scc-1, a novel colon cancer susceptibility gene in the mouse: linkage to CD44 (Ly-24, Pgp-1) on chromosome 2. Moen, C.J., Snoek, M., Hart, A.A., Demant, P. Oncogene (1992) [Pubmed]
  8. Molecular cloning and characterization of Byp, a murine receptor-type tyrosine phosphatase similar to human DEP-1. Kuramochi, S., Matsuda, S., Matsuda, Y., Saitoh, T., Ohsugi, M., Yamamoto, T. FEBS Lett. (1996) [Pubmed]
  9. Induction of specific protein tyrosine phosphatase transcripts during differentiation of mouse erythroleukemia cells. Kume, T., Tsuneizumi, K., Watanabe, T., Thomas, M.L., Oishi, M. J. Biol. Chem. (1994) [Pubmed]
  10. CD148, a new membrane tyrosine phosphatase involved in leukocyte function. Gayà, A., Pirotto, F., Palou, E., Autschbach, F., Del Pozo, V., Solé, J., Serra-Pages, C. Leuk. Lymphoma (1999) [Pubmed]
  11. Murine DEP-1, a receptor protein tyrosine phosphatase, is expressed in macrophages and is regulated by CSF-1 and LPS. Osborne, J.M., den Elzen, N., Lichanska, A.M., Costelloe, E.O., Yamada, T., Cassady, A.I., Hume, D.A. J. Leukoc. Biol. (1998) [Pubmed]
  12. From sentinel to messenger: an extended phenotypic analysis of the monocyte to dendritic cell transition. Woodhead, V.E., Binks, M.H., Chain, B.M., Katz, D.R. Immunology (1998) [Pubmed]
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