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2011 | 58 | 4 |

Tytuł artykułu

Tyrosine phosphatases as a superfamily of tumor suppressors in colorectal cancer

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
 Phosphorylation and dephosphorylation processes catalyzed by numerous kinases and phosphorylases are essential for cell homeostasis and may lead to disturbances in a variety of vital cellular pathways, such as cell proliferation and differentiation, and thus to complex diseases including cancer. As over 80 % of all oncogenes encode protein tyrosine kinases (PTKs), protein tyrosine phosphatases (PTPs), which can reverse the effects of tyrosine kinases, are very important tumor suppressors. Alterations in tyrosine kinase and phosphatase genes including point mutations, changes in epigenetic regulation, as well as chromosomal aberrations involving regions critical to these genes, are frequently observed in a variety of cancers. Colorectal cancer (CRC) is one of the most common cancers in humans. CRCs occur in a familial (about 15 % of all cases), hereditary (about 5%) and sporadic (almost 75-80 %) form. As genetic-environmental interrelations play an important role in the susceptibility to sporadic forms of CRCs, many studies are focused on genetic alterations in such tumors. Mutational analysis of the tyrosine phosphatome in CRCs has identified somatic mutations in PTPRG, PTPRT, PTPN3, PTPN13 and PTPN14. The majority of these mutations result in a loss of protein function. Also, alterations in the expression of these genes, such as decreased expression of PTPRR, PTPRO, PTPRG and PTPRD, mediated by epigenetic mechanisms have been observed in a variety of tumors. Since cancer is a social and global problem, there will be a growing number of studies on alterations in the candidate cancer genes, including protein kinases and phosphatases, to determine the origin, biology and potential pathways for targeted anticancer therapy.

Wydawca

-

Rocznik

Tom

58

Numer

4

Opis fizyczny

p.467-470,ref.

Twórcy

  • Genetics Department, Medical University, Wroclaw, Poland

Bibliografia

  • Alonso A, Sasin J, Bottini N, Friedberg I, Friedberg I, Osterman A, Godzik A, Hunter T, Dixon J, Mustelin T (2004) Protein tyrosine phosphatases in the human genome. Cell 117: 699-711. 
  • Arena S, Benvenuti S, Bardelli (2005) Genetic analysis of the kinome and phosphatome in cancer. Cell Mol Life Sci 62: 2092-2099. 
  • Balavenkatraman KK, Jandt E, Friedrich K, Kautenburger T, Pool-Zobel BL, Ostman A, Böhmer FD (2006) DEP-1 protein tyrosine phosphatase inhibits proliferation and migration of colon carcinoma cells and is upregulated by protective nutrients. Oncogene 25: 6319-6324.  
  • Cheah PY (2009) Recent advances in colorectal cancer genetics and diagnostics. Crit Rev Oncol Hematol 69: 45-55. 
  • van Doorn R, Zoutman WH, Dijkman R, de Menezes RX, Commandeur S, Mulder AA, van der Velden PA, Vermeer MH, Willemze R, Yan PS, Huang TH, Tensen CP (2005) Epigenetic profiling of cutaneous T-cell lymphoma: promoter hypermethylation of multiple tumor suppressor genes including BCL7a, PTPRG, and p73. J Clin Oncol 23: 3886-3896.  
  • Funato K, Yamazumi Y, Oda T, Akiyama T (2011) Tyrosine phosphatase PTPRD suppresses colon cancer cell migration in coordination with CD44. Exp Ther Med 2: 457-463.
  • Jacob ST, Motiwala T (2005) Epigenetic regulation of protein tyrosine phosphatases: potential molecular targets for cancer therapy. Cancer Gene Ther 12: 665-672. 
  • Julien SG, Dubé N, Hardy S, Tremblay ML (2011) Inside the human cancer tyrosine phosphatome. Nat Rev Cancer 11: 35-49.  
  • Kim YH, Lee HC, Kim SY, Yeom YI, Ryu KJ, Min BH, Kim DH, Son HJ, Rhee PL, Kim JJ, Rhee JC, Kim HC, Chun HK, Grady WM, Kim YS (2011) Epigenomic analysis of aberrantly methylated genes in colorectal cancer identifies genes commonly affected by epigenetic alterations. Ann Surg Oncol 18: 2338-2347.  
  • Korff S, Woerner SM, Yuan YP, Bork P, von Knebel Doeberitz M, Gebert J (2008) Frameshift mutations in coding repeats of protein tyrosine phosphatase genes in colorectal tumors with microsatellite instability. BMC Cancer 8: 329. 
  • Lurkin I, Stoehr R, Hurst CD, van Tilborg AA, Knowles MA, Hartmann A, Zwarthoff EC (2010) Two multiplex assays that simultaneously identify 22 possible mutation sites in the KRAS, BRAF, NRAS and PIK3CA genes. PLoS One 5: e8802. 
  • Menigatti M, Cattaneo E, Sabates-Bellver J, Ilinsky VV, Went P, Buffoli F, Marquez VE, Jiricny J, Marra G (2009) The protein tyrosine phosphatase receptor type R gene is an early and frequent target of silencing in human colorectal tumorigenesis. Mol Cancer 8: 124. 
  • Mokarram P, Kumar K, Brim H, Naghibalhossaini F, Saberi-Firoozi M, Nouraie M, Green R, Lee E, Smoot DT, Ashktorab H (2009) Distinct high-profile methylated genes in colorectal cancer. PLoS One 4: e7012. 
  • Motiwala T, Ghoshal K, Das A, Majumder S, Weichenhan D, Wu YZ, Holman K, James SJ, Jacob ST, Plass C (2003) Suppression of the protein tyrosine phosphatase receptor type O gene (PTPRO) by methylation in hepatocellular carcinomas. Oncogene 22: 6319-6331. 
  • van Puijenbroek M, Dierssen JW, Stanssens P, van Eijk R, Cleton-Jansen AM, van Wezel T, Morreau H (2005) Mass spectrometry-based loss of heterozygosity analysis of single-nucleotide polymorphism loci in paraffin embedded tumors using the MassEXTEND assay: single-nucleotide polymorphism loss of heterozygosity analysis of the protein tyrosine phosphatase receptor type J in familial colorectal cancer. J Mol Diagn 7: 623-630. 
  • van Roon EH, de Miranda NF, van Nieuwenhuizen MP, de Meijer EJ, van Puijenbroek M, Yan PS, Huang TH, van Wezel T, Morreau H, Boer JM (2011) Tumour-specific methylation of PTPRG intron 1 locus in sporadic and Lynch syndrome colorectal cancer. Eur J Hum Genet 19: 307-312.  
  • Ruivenkamp C, Hermsen M, Postma C, Klous A, Baak J, Meijer G, Demant P (2003) LOH of PTPRJ occurs early in colorectal cancer and is associated with chromosomal loss of 18q12-21. Oncogene 22: 3472-3474. 
  • Saiardi A, Bhandari R, Resnick AC, Snowman AM, Snyder SH (2004) Phosphorylation of proteins by inositol pyrophosphates. Science 306: 2101-2105. 
  • Samowitz WS (2008) Genetic and epigenetic changes in colon cancer. Exp Mol Pathol 85: 64-67.  
  • Song SY, Kang MR, Yoo NJ, Lee SH (2010) Mutational analysis of mononucleotide repeats in dual specificity tyrosine phosphatase genes in gastric and colon carcinomas with microsatellite instability. APMIS 118: 389-393. 
  • Tabernero L, Aricescu AR, Jones EY, Szedlacsek SE (2008) Protein tyrosine phosphatases: structure-function relationships. FEBS J 275: 867-882.  
  • Toland AE, Rozek LS, Presswala S, Rennert G, Gruber SB (2008) PTPRJ haplotypes and colorectal cancer risk. Cancer Epidemiol Biomarkers Prev 17: 2782-2785. 
  • Veeriah S, Brennan C, Meng S, Singh B, Fagin JA, Solit DB, Paty PB, Rohle D, Vivanco I, Chmielecki J, Pao W, Ladanyi M, Gerald WL, Liau L, Cloughesy TC, Mischel PS, Sander C, Taylor B, Schultz N, Major J, Heguy A, Fang F, Mellinghoff IK, Chan TA (2009) The tyrosine phosphatase PTPRD is a tumor suppressor that is frequently inactivated and mutated in glioblastoma and other human cancers. Proc Natl Acad Sci USA 106: 9435-9440.  
  • Wang Z, Shen D, Parsons DW, Bardelli A, Sager J, Szabo S, Ptak J, Silliman N, Peters BA, van der Heijden MS, Parmigiani G, Yan H, Wang TL, Riggins G, Powell SM, Willson JK, Markowitz S, Kinzler KW, Vogelstein B, Velculescu VE (2004) Mutational analysis of the tyrosine phosphatome in colorectal cancers. Science 304: 1164-1166. 
  • Wicki A, Herrmann R, Christofori G (2010) Kras in metastatic colorectal cancer. Swiss Med Wkly 140: 13112. 
  • Zhang X, Guo A, Yu J, Possemato A, Chen Y, Zheng W, Polakiewicz RD, Kinzler KW, Vogelstein B, Velculescu VE, Wang ZJ (2007) Identification of STAT3 as a substrate of receptor protein tyrosine phosphatase T. Proc Natl Acad Sci USA 104: 4060-4064.  
  • Zhao Y, Zhang X, Guda K, Lawrence E, Sun Q, Watanabe T, Iwakura Y, Asano M, Wei L, Yang Z, Zheng W, Dawson D, Willis J, Markowitz SD, Satake M, Wang Z (2010) Identification and functional characterization of paxillin as a target of protein tyrosine phosphatase receptor T. Proc Natl Acad Sci USA 107: 2592-2597. 

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

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