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PTP4A1  -  protein tyrosine phosphatase type IVA,...

Homo sapiens

Synonyms: HH72, PRL-1, PRL1, PTP(CAAX1), PTP(CAAXI), ...
 
 
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Disease relevance of PTP4A1

 

High impact information on PTP4A1

 

Biological context of PTP4A1

  • Widespread expression of PRL-1 and -2 in multiple organ systems suggests an important functional role for these enzymes in normal tissue homeostasis [6].
  • Cellular Localization of PRL-1 and PRL-2 Gene Expression in Normal Adult Human Tissues [6].
  • PRL-1 is one of three closely related protein-tyrosine phosphatases, which are characterized by C-terminal farnesylation [7].
  • The intron enhancer contributed significantly to PRL-1 promoter activity in HepG2 cells which contain PIEC but not to NIH 3T3 cells which do not [8].
  • Here, we analyzed the structure of the human PRL-1 gene and localized it to chromosome 6 within band q12 [8].
 

Anatomical context of PTP4A1

 

Associations of PTP4A1 with chemical compounds

  • In the PRL-1 structure, a sulfate ion is bound to the active-site, providing stabilizing interactions to maintain the canonically found active conformation of PTPs, whereas the NMR structure exhibits an open conformation of the active-site [10].
  • Neither the OV-1 nor the PRL-1 protein shares strong homology with any previously characterised phosphotyrosine phosphatase, suggesting that they probably belong to a new phosphatase family [11].
  • When cells are treated with FTI-277, a selective farnesyltransferase inhibitor, PRL-1, -2, and -3 shifted into the nucleus [12].
  • When cells were treated with brefeldin A, PRL-1 and -3 accumulated in a collapsed compact structure around the microtubule-organizing center [12].
 

Other interactions of PTP4A1

  • PRL-2 was expressed heavily in almost every tissue and cell type examined, whereas PRL-1 expression levels varied considerably both between tissue types and between individuals [6].
  • Cells stably transfected with PRL-1 or PRL-2 exhibited 2.7-3.3-fold increases over control cells in the rate of DNA synthesis and the proportion of cells in S-phase, and they progressed more rapidly from G1 into S [9].
  • A 100-kb physical and transcriptional map around the EDH17B2 gene: identification of three novel genes and a pseudogene of a human homologue of the rat PRL-1 tyrosine phosphatase [11].
  • The detailed structural information on the active enzyme conformation and regulation of PRL-1 provides the structural basis for the development of potential inhibitors of PRL enzymes [10].
 

Analytical, diagnostic and therapeutic context of PTP4A1

  • Therefore, we investigated expression patterns for PRL-1 and -2 genes in multiple normal, adult human tissues using in situ hybridization [6].
  • Using immunofluorescence we studied the subcellular localization of endogenous PRL-1, and our results demonstrate that PRL-1 exhibits cell cycle-dependent localization; in non-mitotic HeLa cells, PRL-1 is localized to the endoplasmic reticulum in a farnesylation-dependent manner [7].
  • PRLF did not show any relation with neonatal morbidity, but PRL1 showed a significant direct relation with the Apgar score at 5 min [3].
  • To prepare specific monoclonal antibody (MAb) against PRL-3, cDNAs of PRL-1, -2, and -3 were cloned by RT-PCR and inserted into prokaryotic expression vector pGEX-4T1, respectively [13].

References

  1. 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]
  2. 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]
  3. Maternal and fetal prolactin in pregnancy-induced hypertension. Marlettini, M.G., Cassani, A., Morselli-Labate, A.M., Crippa, S., Contarini, A., Miniero, R., Platè, L., Orlandi, C. Arch. Gynecol. Obstet. (1990) [Pubmed]
  4. PRL-1 tyrosine phosphatase regulates c-Src levels, adherence, and invasion in human lung cancer cells. Achiwa, H., Lazo, J.S. Cancer Res. (2007) [Pubmed]
  5. PRL-3 and PRL-1 promote cell migration, invasion, and metastasis. Zeng, Q., Dong, J.M., Guo, K., Li, J., Tan, H.X., Koh, V., Pallen, C.J., Manser, E., Hong, W. Cancer Res. (2003) [Pubmed]
  6. Cellular Localization of PRL-1 and PRL-2 Gene Expression in Normal Adult Human Tissues. Dumaual, C.M., Sandusky, G.E., Crowell, P.L., Randall, S.K. J. Histochem. Cytochem. (2006) [Pubmed]
  7. The tyrosine phosphatase PRL-1 localizes to the endoplasmic reticulum and the mitotic spindle and is required for normal mitosis. Wang, J., Kirby, C.E., Herbst, R. J. Biol. Chem. (2002) [Pubmed]
  8. The gene encoding human nuclear protein tyrosine phosphatase, PRL-1. Cloning, chromosomal localization, and identification of an intron enhancer. Peng, Y., Genin, A., Spinner, N.B., Diamond, R.H., Taub, R. J. Biol. Chem. (1998) [Pubmed]
  9. Enhanced cell cycle progression and down regulation of p21(Cip1/Waf1) by PRL tyrosine phosphatases. Werner, S.R., Lee, P.A., DeCamp, M.W., Crowell, D.N., Randall, S.K., Crowell, P.L. Cancer Lett. (2003) [Pubmed]
  10. 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]
  11. A 100-kb physical and transcriptional map around the EDH17B2 gene: identification of three novel genes and a pseudogene of a human homologue of the rat PRL-1 tyrosine phosphatase. Montagna, M., Serova, O., Sylla, B.S., Feunteun, J., Lenoir, G.M. Hum. Genet. (1995) [Pubmed]
  12. Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosome. Zeng, Q., Si, X., Horstmann, H., Xu, Y., Hong, W., Pallen, C.J. J. Biol. Chem. (2000) [Pubmed]
  13. Preparation and characterization of monoclonal antibody against protein tyrosine phosphatase PRL-3. Peng, L., Li, Y., Meng, L., Shou, C. Hybrid. Hybridomics (2004) [Pubmed]
 
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