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PTPRH  -  protein tyrosine phosphatase, receptor...

Homo sapiens

Synonyms: R-PTP-H, Receptor-type tyrosine-protein phosphatase H, SAP-1, SAP1, Stomach cancer-associated protein tyrosine phosphatase 1, ...
 
 
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Disease relevance of PTPRH

 

High impact information on PTPRH

  • The cytoplasmic region of SAP-1 has now been shown to bind directly the tyrosine kinase Lck [5].
  • Interaction of SAP-1, a transmembrane-type protein-tyrosine phosphatase, with the tyrosine kinase Lck. Roles in regulation of T cell function [5].
  • Stomach cancer-associated protein-tyrosine phosphatase-1 (SAP-1), a transmembrane-type protein-tyrosine phosphatase, is thought to inhibit integrin signaling by mediating the dephosphorylation of focal adhesion-associated proteins [6].
  • Adenovirus-mediated overexpression of wild-type SAP-1, but not that of a catalytically inactive mutant of this enzyme, has now been shown to induce apoptosis in NIH 3T3 fibroblasts [6].
  • Inhibition of cell growth and spreading by stomach cancer-associated protein-tyrosine phosphatase-1 (SAP-1) through dephosphorylation of p130cas [7].
 

Biological context of PTPRH

 

Anatomical context of PTPRH

  • SAP-1 was mainly expressed in brain and liver and at a lower level in heart and stomach as a 4.2-kilobase mRNA, but it was not detected in pancreas or colon [2].
  • These results thus suggest that the direct interaction of SAP-1 with Lck results in inhibition of the kinase activity of the latter and a consequent negative regulation of T cell function [5].
  • Expression of recombinant SAP-1 induced the dephosphorylation of p130(cas) as well as that of two other components of the integrin-signaling pathway (focal adhesion kinase and p62(dok)) in intact cells [7].
  • Overexpression of SAP-1 induced disruption of the actin-based cytoskeleton as well as inhibited various cellular responses promoted by integrin-mediated cell adhesion, including cell spreading on fibronectin, growth factor-induced activation of extracellular signal-regulated kinase 2, and colony formation [7].
 

Associations of PTPRH with chemical compounds

  • The bacterially expressed SAP-1 fusion protein had tyrosine-specific phosphatase activity [2].
 

Other interactions of PTPRH

  • The extracellular region of SAP-1 consisted of eight fibronectin type III-like structure repeats and contained multiple N-glycosylation sites [2].
 

Analytical, diagnostic and therapeutic context of PTPRH

References

  1. Gene for the human transmembrane-type protein tyrosine phosphatase H (PTPRH): genomic structure, fine-mapping and its exclusion as a candidate for Peutz-Jeghers syndrome. Marneros, A.G., Mehenni, H., Reichenberger, E., Antonarakis, S.E., Krieg, T., Olsen, B.R. Cytogenet. Cell Genet. (2001) [Pubmed]
  2. Molecular cloning of a human transmembrane-type protein tyrosine phosphatase and its expression in gastrointestinal cancers. Matozaki, T., Suzuki, T., Uchida, T., Inazawa, J., Ariyama, T., Matsuda, K., Horita, K., Noguchi, H., Mizuno, H., Sakamoto, C. J. Biol. Chem. (1994) [Pubmed]
  3. Downregulation of stomach cancer-associated protein tyrosine phosphatase-1 (SAP-1) in advanced human hepatocellular carcinoma. Nagano, H., Noguchi, T., Inagaki, K., Yoon, S., Matozaki, T., Itoh, H., Kasuga, M., Hayashi, Y. Oncogene (2003) [Pubmed]
  4. Sap-1/PTPRH activity is regulated by reversible dimerization. Wälchli, S., Espanel, X., van Huijsduijnen, R.H. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  5. Interaction of SAP-1, a transmembrane-type protein-tyrosine phosphatase, with the tyrosine kinase Lck. Roles in regulation of T cell function. Ito, T., Okazawa, H., Maruyama, K., Tomizawa, K., Motegi, S., Ohnishi, H., Kuwano, H., Kosugi, A., Matozaki, T. J. Biol. Chem. (2003) [Pubmed]
  6. Induction of apoptosis by stomach cancer-associated protein-tyrosine phosphatase-1. Takada, T., Noguchi, T., Inagaki, K., Hosooka, T., Fukunaga, K., Yamao, T., Ogawa, W., Matozaki, T., Kasuga, M. J. Biol. Chem. (2002) [Pubmed]
  7. Inhibition of cell growth and spreading by stomach cancer-associated protein-tyrosine phosphatase-1 (SAP-1) through dephosphorylation of p130cas. Noguchi, T., Tsuda, M., Takeda, H., Takada, T., Inagaki, K., Yamao, T., Fukunaga, K., Matozaki, T., Kasuga, M. J. Biol. Chem. (2001) [Pubmed]
 
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