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PTP4A3  -  protein tyrosine phosphatase type IVA,...

Homo sapiens

Synonyms: PRL-3, PRL-R, PRL3, Protein tyrosine phosphatase type IVA 3, Protein-tyrosine phosphatase 4a3, ...
 
 
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Disease relevance of PTP4A3

 

High impact information on PTP4A3

  • In 3 of 12 metastases examined, multiple copies of the PRL-3 gene were found within a small amplicon located at chromosome 8q24 [5].
  • Among the genes identified, the PRL-3 protein tyrosine phosphatase gene was of particular interest [5].
  • Because PRL-3 mRNA had been reported to be consistently elevated in metastatic samples derived from colorectal cancers, we attempted to investigate if PRL-3 might be involved in tumor angiogenesis and if PRL-3-expressing cells could cross-talk to human umbilical vascular endothelial cells (HUVEC) by using an in vitro coculture system [6].
  • PRL-3 Initiates Tumor Angiogenesis by Recruiting Endothelial Cells In vitro and In vivo [6].
  • We observed that both PRL-3-expressing Chinese hamster ovary (CHO) cells and PRL-3-expressing DLD-1 human colon cancer cells could redirect the migration of HUVECs toward them; in addition, PRL-3-expressing DLD-1 cells could enhance HUVEC vascular formation [6].
 

Chemical compound and disease context of PTP4A3

 

Biological context of PTP4A3

 

Anatomical context of PTP4A3

  • We screened over 1,400 hybridoma clones to generate mAbs specific to each PRL member.RESULTS: We obtained two hybridoma clones specifically against PRL-3 and another two clones specifically against PRL-1 [2].
  • Immunohistochemical analysis with anti-PRL-3 antibodies showed a cell membrane localization, consistent with the predicted isoprenylation of the protein [9].
  • In contrast, little or no PRL-3 expression was observed in normal colon, nonmetastatic primary cancers, or metastatic lesions derived from cancers other than those of the colon (pancreas, stomach, or esophagus) [9].
  • Moreover, we found a more frequent expression of PRL-3 in lymph node metastases as compared to the primary tumours (91.7 vs 66.7%; P = 0.033) [12].
  • We sought to associate a function with PRL-3 expression in both endothelial cells and malignant cells using in vitro models [13].
 

Associations of PTP4A3 with chemical compounds

  • When phosphate ions or sodium orthovanadate, which is a known inhibitor, are added to the apo PRL-3, the NMR signals from the residues in the active site appeared and could be assigned, indicating that the conformation of the residues has been stabilized [14].
  • Then we identified integrin alpha1 as a PRL-3-interacting protein for the first time, and verified this physical association with pull-down and co-immunoprecipitation assays [15].
  • PRL-3 activity was determined using the substrate 6,8-difluoro-4-methylumbelliferyl phosphate, and was inhibited by vanadate and analogs [16].
  • Role of PRL-3, a human muscle-specific tyrosine phosphatase, in angiotensin-II signaling [16].
  • E(2) stimulated transcriptional activity in MCF7A(2) cells transfected with PIII lacking an estrogen responsive element, and increased hPRLR mRNA and protein [8].
 

Physical interactions of PTP4A3

  • The abolition of the E(2) effect by mutation of Sp1 or C/EBP elements that bind Sp1/Sp3 and C/EBPbeta within PIII indicated the cooperation of these transfactors in E(2)-induced transcription of the hPRLR [8].
 

Regulatory relationships of PTP4A3

  • These findings demonstrate that an E(2)/ERalpha, Sp1, and C/EBPbeta complex with recruitment of coactivators and TFIIB and Pol II are required for E(2)-activated transcriptional expression of the hPRLR through PIII [8].
 

Other interactions of PTP4A3

 

Analytical, diagnostic and therapeutic context of PTP4A3

References

  1. Structural insights into molecular function of the metastasis-associated phosphatase PRL-3. Kozlov, G., Cheng, J., Ziomek, E., Banville, D., Gehring, K., Ekiel, I. J. Biol. Chem. (2004) [Pubmed]
  2. Generation of PRL-3- and PRL-1-specific monoclonal antibodies as potential diagnostic markers for cancer metastases. Li, J., Guo, K., Koh, V.W., Tang, J.P., Gan, B.Q., Shi, H., Li, H.X., Zeng, Q. Clin. Cancer Res. (2005) [Pubmed]
  3. PRL-3 phosphatase is implicated in ovarian cancer growth. Polato, F., Codegoni, A., Fruscio, R., Perego, P., Mangioni, C., Saha, S., Bardelli, A., Broggini, M. Clin. Cancer Res. (2005) [Pubmed]
  4. Translational control of C-terminal Src kinase (Csk) expression by PRL3 phosphatase. Liang, F., Luo, Y., Dong, Y., Walls, C.D., Liang, J., Jiang, H.Y., Sanford, J.R., Wek, R.C., Zhang, Z.Y. J. Biol. Chem. (2008) [Pubmed]
  5. A phosphatase associated with metastasis of colorectal cancer. Saha, S., Bardelli, A., Buckhaults, P., Velculescu, V.E., Rago, C., St Croix, B., Romans, K.E., Choti, M.A., Lengauer, C., Kinzler, K.W., Vogelstein, B. Science (2001) [Pubmed]
  6. PRL-3 Initiates Tumor Angiogenesis by Recruiting Endothelial Cells In vitro and In vivo. Guo, K., Li, J., Wang, H., Osato, M., Tang, J.P., Quah, S.Y., Gan, B.Q., Zeng, Q. Cancer Res. (2006) [Pubmed]
  7. DNA copy number changes at 8q11-24 in metastasized colorectal cancer. Buffart, T.E., Coffa, J., Hermsen, M.A., Carvalho, B., van der Sijp, J.R., Ylstra, B., Pals, G., Schouten, J.P., Meijer, G.A. Cellular oncology : the official journal of the International Society for Cellular Oncology. (2005) [Pubmed]
  8. A novel estradiol/estrogen receptor alpha-dependent transcriptional mechanism controls expression of the human prolactin receptor. Dong, J., Tsai-Morris, C.H., Dufau, M.L. J. Biol. Chem. (2006) [Pubmed]
  9. PRL-3 expression in metastatic cancers. Bardelli, A., Saha, S., Sager, J.A., Romans, K.E., Xin, B., Markowitz, S.D., Lengauer, C., Velculescu, V.E., Kinzler, K.W., Vogelstein, B. Clin. Cancer Res. (2003) [Pubmed]
  10. High expression of PRL-3 promotes cancer cell motility and liver metastasis in human colorectal cancer: a predictive molecular marker of metachronous liver and lung metastases. Kato, H., Semba, S., Miskad, U.A., Seo, Y., Kasuga, M., Yokozaki, H. Clin. Cancer Res. (2004) [Pubmed]
  11. Trimeric structure of PRL-1 phosphatase reveals an active enzyme conformation and regulation mechanisms. Jeong, D.G., Kim, S.J., Kim, J.H., Son, J.H., Park, M.R., Lim, S.M., Yoon, T.S., Ryu, S.E. J. Mol. Biol. (2005) [Pubmed]
  12. Expression and prognostic impact of the protein tyrosine phosphatases PRL-1, PRL-2, and PRL-3 in breast cancer. Radke, I., Götte, M., Kersting, C., Mattsson, B., Kiesel, L., Wülfing, P. Br. J. Cancer (2006) [Pubmed]
  13. Protein tyrosine phosphatase PRL-3 in malignant cells and endothelial cells: expression and function. Rouleau, C., Roy, A., St Martin, T., Dufault, M.R., Boutin, P., Liu, D., Zhang, M., Puorro-Radzwill, K., Rulli, L., Reczek, D., Bagley, R., Byrne, A., Weber, W., Roberts, B., Klinger, K., Brondyk, W., Nacht, M., Madden, S., Burrier, R., Shankara, S., Teicher, B.A. Mol. Cancer Ther. (2006) [Pubmed]
  14. Structure of human PRL-3, the phosphatase associated with cancer metastasis. Kim, K.A., Song, J.S., Jee, J., Sheen, M.R., Lee, C., Lee, T.G., Ro, S., Cho, J.M., Lee, W., Yamazaki, T., Jeon, Y.H., Cheong, C. FEBS Lett. (2004) [Pubmed]
  15. Identification of integrin alpha1 as an interacting protein of protein tyrosine phosphatase PRL-3. Peng, L., Jin, G., Wang, L., Guo, J., Meng, L., Shou, C. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  16. Role of PRL-3, a human muscle-specific tyrosine phosphatase, in angiotensin-II signaling. Matter, W.F., Estridge, T., Zhang, C., Belagaje, R., Stancato, L., Dixon, J., Johnson, B., Bloem, L., Pickard, T., Donaghue, M., Acton, S., Jeyaseelan, R., Kadambi, V., Vlahos, C.J. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
 
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