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Ptprm  -  protein tyrosine phosphatase, receptor...

Mus musculus

Synonyms: Kiaa4044, Protein-tyrosine phosphatase mu, R-PTP-mu, RPTPmu, Receptor-type tyrosine-protein phosphatase mu, ...
 
 
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High impact information on Ptprm

  • Cell surface expression of receptor protein tyrosine phosphatase RPTP mu is regulated by cell-cell contact [1].
  • In this study, we have examined how RPTP mu may function as a cell contact receptor in mink lung epithelial cells, which express RPTPmu endogenously, as well as in transfected 3T3 cells [1].
  • RPTPmu surface expression increases significantly with increasing cell density [1].
  • This density-induced upregulation of RPTP mu is independent of its catalytic activity and is also observed when transcription is driven by a constitutive promoter, indicating that modulation of RPTPmu surface expression occurs posttranscriptionally [1].
  • The multimers are composed of disulfide-linked dimers attached noncovalently by interactions involving the meprin, A5 protein, receptor protein-tyrosine phosphatase mu (MAM) domain [2].
 

Biological context of Ptprm

 

Anatomical context of Ptprm

 

Associations of Ptprm with chemical compounds

  • The receptor-like protein tyrosine phosphatase mu (RPTPmu) belongs to the subfamily of meprin, A5, RPTPmu (MAM) domain-containing RPTPs, which are thought to play an important role in cell-cell adhesion mediated processes [4].
  • From its structure, POEM was suggested to be a novel adhesion molecule with five EGF-like domains, an Arg-Gly-Asp (RGD) cell binding motif, and a meprin, A5 protein, and receptor protein-tyrosine phosphatase mu (MAM) domain [7].
 

Analytical, diagnostic and therapeutic context of Ptprm

References

  1. Cell surface expression of receptor protein tyrosine phosphatase RPTP mu is regulated by cell-cell contact. Gebbink, M.F., Zondag, G.C., Koningstein, G.M., Feiken, E., Wubbolts, R.W., Moolenaar, W.H. J. Cell Biol. (1995) [Pubmed]
  2. Multimeric structure of the secreted meprin A metalloproteinase and characterization of the functional protomer. Ishmael, F.T., Norcum, M.T., Benkovic, S.J., Bond, J.S. J. Biol. Chem. (2001) [Pubmed]
  3. Genetic mapping of Ptprm on mouse chromosome 17. Mukouyama, Y., Watanabe, T., Kume, T., Oishi, M. Mamm. Genome (1995) [Pubmed]
  4. Receptor protein tyrosine phosphatase mu expression as a marker for endothelial cell heterogeneity; analysis of RPTPmu gene expression using LacZ knock-in mice. Koop, E.A., Lopes, S.M., Feiken, E., Bluyssen, H.A., van der Valk, M., Voest, E.E., Mummery, C.L., Moolenaar, W.H., Gebbink, M.F. Int. J. Dev. Biol. (2003) [Pubmed]
  5. Impaired flow-induced dilation in mesenteric resistance arteries from receptor protein tyrosine phosphatase-mu-deficient mice. Koop, E.A., Gebbink, M.F., Sweeney, T.E., Mathy, M.J., Heijnen, H.F., Spaan, J.A., Voest, E.E., VanBavel, E., Peters, S.L. Am. J. Physiol. Heart Circ. Physiol. (2005) [Pubmed]
  6. RPTP delta and the novel protein tyrosine phosphatase RPTP psi are expressed in restricted regions of the developing central nervous system. Sommer, L., Rao, M., Anderson, D.J. Dev. Dyn. (1997) [Pubmed]
  7. Molecular cloning of POEM: a novel adhesion molecule that interacts with alpha8beta1 integrin. Morimura, N., Tezuka, Y., Watanabe, N., Yasuda, M., Miyatani, S., Hozumi, N., Tezuka Ki, K. J. Biol. Chem. (2001) [Pubmed]
 
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