PRL phosphatases as potential molecular targets in cancer

Molecular Cancer Therapeutics

Volumn 4, Issue 11, 2005, Pages 1653-1661

  Stephens, Bret J ^a   Han, Haiyong ^c   Gokhale, Vijay ^b   Von Hoff, Daniel D ^c  

^a University of Arizona   (United States)

^b UNIVERSITY OF ARIZONA   (United States)

^c TRANSLATIONAL GENOMICS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MARKER; PHOSPHATASE; PROTEIN FARNESYLTRANSFERASE INHIBITOR; SMALL INTERFERING RNA;

CANCER CELL; CELL MIGRATION; CELL MOTILITY; CELL PROLIFERATION; COLORECTAL CANCER; COLORECTAL TUMOR; DISEASE MODEL; FREQUENCY ANALYSIS; GENE EXPRESSION REGULATION; GENE OVEREXPRESSION; GENE TARGETING; HUMAN; IMMUNOHISTOCHEMISTRY; IN SITU HYBRIDIZATION; MALIGNANT NEOPLASTIC DISEASE; METASTASIS POTENTIAL; NONHUMAN; NORTHERN BLOTTING; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN STRUCTURE; SHORT SURVEY; STRUCTURE ANALYSIS;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BLOTTING, NORTHERN; CELL CYCLE PROTEINS; CELL LINE, TUMOR; CELL PROLIFERATION; COLON; COLONIC NEOPLASMS; HELA CELLS; HUMANS; IMMEDIATE-EARLY PROTEINS; IMMUNOHISTOCHEMISTRY; MEMBRANE PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NEOPLASM METASTASIS; NEOPLASM PROTEINS; NEOPLASMS; PHOSPHORYLATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN-TYROSINE-PHOSPHATASE; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; TUMOR MARKERS, BIOLOGICAL;

EID: 28044448270     PISSN: 15357163     EISSN: None     Source Type: Journal    
DOI: 10.1158/1535-7163.MCT-05-0248     Document Type: Short Survey

References (60)

1. Hunter T. Signaling - 2000 and beyond. Cell 2000;100:113-27.
2. Lyon MA, Ducruet AP, Wipf P, Lazo JS. Dual-specificity phosphatases as targets for antineoplastic agents. Nat Rev Drug Discov 2002;1:961-76.
3. van Huijsduijnen RH, Bombrun A, Swinnen D. Selecting protein tyrosine phosphatases as drug targets. Drug Discov Today 2002;7:1013-9.
4. Alonso A, Sasin J, Bottini N, et al. Protein tyrosine phosphatases in the human genome. Cell 2004;117:699-711.
5. Kim KA, Song JS, Jee J, et al. Structure of human PRL-3, the phosphatase associated with cancer metastasis. FEBS Lett 2004;565: 181-7.
6. 15N resonance assignments and secondary structure of the human protein tyrosine phosphatase, PRL-2. J Biomol NMR 2003;27:397-8.
7. Kozlov G, Chang J, Ziomek E, Banville D, Gehring K, Ekiel I. Structural insights into molecular function of the metastasis-associated phosphatase PRL-3. J Biol Chem 2004;279:11882-9.
8. Zeng Q, Si X, Horstmann H, Xu Y, Hong W, Pallen CJ. Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosome. J Biol Chem 2000;275:21444-52.
9. Wang J, Kirby CE, Herbst R. The tyrosine phosphatase PRL-1 localizes to the endoplasmic reticulum and the mitotic spindle and is required for normal mitosis. J Biol Chem 2002;277:46659-68.
10. Zeng Q, Hong W, Tan YH. Mouse PRL-2 and PRL-3, two potentially prenylated protein tyrosine phosphatases homologous to PRL-1. Biochem Biophys Res Commun 1998;244:421 -7.
11. Diamond RH, Cressman DE, Laz TM, Abrams CS, Taub R. PRL-1, a unique nuclear protein tyrosine phosphatase, affects cell growth. Mol Cell Biol 1994;14:3752-62.
12. Jeong DG, Kim SJ, Kim JH, et al. Trimeric structure of PRL-1 phosphatase reveals an active enzyme conformation and regulation mechanisms. J Mol Biol 2005;345:401-13.
13. den Hertog J, Groen A, van der Wijk T. Redox regulation of protein-tyrosine phosphatases. Arch Biochem Biophys 2005;434:11-5.
14. 13C resonance assignments of the human protein tyrosine phosphatase PRL-1. J Biomol NMR 2004;29:417-8.
15. Lee JO, Yang H, Georgescu MM, et al. Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association. Cell 1999;99:323-34.
16. Yuvaniyama J, Denu JM, Dixon JE, Sager MA. Crystal structure of the dual specificity protein phosphatase VHR. Science 1996;272:1328-31.
17. Mohn KL, Laz TM, Hsu JC, Melby AE, Bravo R, Taub R. The immediate-early growth response in regenerating liver and insulin-stimulated H-35 cells: comparison with serum-stimulated 3T3 cells and identification of 41 novel immediate-early genes. Mol Cell Biol 1991;11:381-90.
18. Matter WF, Estridge T, Zhang C, et al. Role of PRL-3, a human muscle-specific tyrosine phosphatase, in angiotensin-II signaling. Biochem Biophys Res Commun 2001;283:1061-8.
19. Kong W, Swain GP, Li S, Diamond RH. PRL-1 PTPase expression is developmentally regulated with tissue-specific patterns in epithelial tissues. Am J Physiol Gastrointest Liver Physiol 2000;279:G613-21.
20. Diamond RH, Peters C, Jung SP, et al. Expression of PRL-1 nuclear PTPase is associated with proliferation in liver but with differentiation in intestine. Am J Physiol 1996;271:G121-9.
21. Saha S, Bardelli A, Buckhaults P, et al. A phosphatase associated with metastasis of colorectal cancer. Science 2001;294:1343-6.
22. Bardelli A, Saha S, Sager JA, et al. PRL-3 expression in metastatic cancers. Clin Cancer Res 2003;9:5607-15.
23. Schwering I, Brauninger A, Distler V, et al. Profiling of Hodgkin's lymphoma cell line L1236 and germinal center B cells: identification of Hodgkin's lymphoma-specific genes. Mol Med 2003;9:85-95.
24. Wu X, Zeng H, Zhang X, et al. Phosphatase of regenerating liver-3 promotes motility and metastasis of mouse melanoma cells. Am J Pathol 2004;164:2039-54.
25. Parker BS, Argani P, Cook BP, et al. Alterations in vascular gene expression in invasive breast carcinoma. Cancer Res 2004;64:7857-66.
26. Han H, Bearss DJ, Browne LW, Calaluce R, Nagle RB, Von Hoff DD. Identification of differentially expressed genes in pancreatic cancer cells using cDNA microarray. Cancer Res 2002;62:2890-6.
27. Wang Q, Holmes DI, Powell SM, Lu QL, Waxman J. Analysis of stromal-epithelial interactions in prostate cancer identifies PTPCAAX2 as a potential oncogene. Cancer Lett 2002;175:63-9.
28. Daoud SS, Munson PJ, Reinhold W, et al. Impact of p53 knockout and topotecan treatment on gene expression profiles in human colon carcinoma cells: a pharmacogenomic study. Cancer Res 2003;63: 2782-93.
29. Fontemaggi G, Kela I, Amariglio N, et al. Identification of direct p73 target genes combining DNA microarray and chromatin immunoprecipitation analyses. J Biol Chem 2002;277:43359-68.
30. Peng Y, Genin A, Spinner NB, Diamond RH, Taub R. The gene encoding human nuclear protein tyrosine phosphatase, PRL-1. Cloning, chromosomal localization, and identification of an intron enhancer. J Biol Chem 1998;273:17286-95.
31. Peng Y, Du K, Ramirez S, Diamond RH, Taub R. Mitogenic upregulation of the PRL-1 protein-tyrosine phosphatase gene by Egr-1. Egr-1 activation is an early event in liver regeneration. J Biol Chem 1999;274: 4513-20.
32. Calogero A, Arcella A, De Gregorio G, et al. The early growth response gene EGR-1 behaves as a suppressor gene that is down-regulated independent of ARF/Mdm2 but not p53 alterations in fresh human gliomas. Clin Cancer Res 2001;7:2788-96.
33. Kobayashi D, Yamada M, Kamagata C, et al. Overexpression of early growth response-1 as a metastasis-regulatory factor in gastric cancer. Anticancer Res 2002;22:3963-70.
34. Buffart TE, Coffa J, Hermsen MA, et al. DNA copy number changes at 8q11-24 in metastasized colorectal cancer. Cell Oncol 2005;27:57-65.
35. Cates CA, Michael RL, Stayrook KR, et al. Prenylation of oncogenic human PTP(CAAX) protein tyrosine phosphatases. Cancer Lett 1996;110: 49-55.
36. Werner SR, Lee PA, DeCamp MW, Crowell DN, Randall SK, Crowell PL. Enhanced cell cycle progression and down regulation of p21(Cip1/Waf1) by PRL tyrosine phosphatases. Cancer Lett 2003;202:201-11.
37. Kato H, Semba S, Miskad UA, Seo Y, Kasuga M, Yokozaki H. 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. Clin Cancer Res 2004;10:7318-28.
38. Zeng Q, Dong JM, Guo K, et al. PRL-3 and PRL-1 promote cell migration, invasion, and metastasis. Cancer Res 2003;63:2716-22.
39. Peters CS, Liang X, Li S, et al. ATF-7, a novel bZIP protein, interacts with the PRL-1 protein-tyrosine phosphatase. J Biol Chem 2001;276: 13718-26.
40. Persengiev SP, Devireddy LR, Green MR. Inhibition of apoptosis by ATFx: a novel role for a member of the ATF/CREB family of mammalian bZIP transcription factors. Genes Dev 2002;16:1806-14.
41. Angelastro JM, Ignatova TN, Kukekov VG, et al. Regulated expression of ATF5 is required for the progression of neural progenitor cells to neurons. J Neurosci 2003;23:4590-600.
42. Si X, Zeng Q, Ng CH, Hong W, Pallen CJ. Interaction of farnesylated PRL-2, a protein-tyrosine phosphatase, with the β-subunit of geranylgeranyltransferase II. J Biol Chem 2001; 276:32875-82.
43. Pathak MK, Dhawan D, Lindner DJ, Borden EC, Farver C, Yi T. Pentamidine is an inhibitor of PRL phosphatases with anticancer activity. Mol Cancer Ther 2002;1:1255-64.
44. Fox KR, Sansom CE, Stevens MF. Footprinting studies on the sequence-selective binding of pentamidine to DNA. FEBS Lett 1990; 266:150-4.
45. Cordes JS, Sun Z, Lloyd DB, et al. Pentamidine reduces hERG expression to prolong the QT interval. Br J Pharmacol 2005;145:15-23.
46. Kuryshev YA, Ficker E, Wang L, et al. Pentamidine-induced long QT syndrome and block of hERG trafficking. J Pharmacol Exp Ther 2005; 312:316-23.
47. Sebti SM, Der CJ. Opinion: searching for the elusive targets of farnesyltransferase inhibitors. Nat Rev Cancer 2003;3:945-51.
48. Takano S, Fukuyama H, Fukumoto M, et al. PRL-1, a protein tyrosine phosphatase, is expressed in neurons and oligodendrocytes in the brain and induced in the cerebral cortex following transient forebrain ischemia. Brain Res Mol Brain Res 1996;40:105-15.
49. Yarovinsky TO, Rickman DW, Diamond RH, Taub R, Hageman GS, Bowes Rickman C. Expression of the protein tyrosine phosphatase, phosphatase of regenerating liver 1, in the outer segments of primate cone photoreceptors. Brain Res Mol Brain Res 2000;77:95-103.
50. Peng L, Ning J, Meng L, Shou C. The association of the expression level of protein tyrosine phosphatase PRL-3 protein with liver metastasis and prognosis of patients with colorectal cancer. J Cancer Res Clin Oncol 2004;130:521-6.
51. Miskad UA, Semba S, Kato H, Yokozaki H. Expression of PRL-3 phosphatase in human gastric carcinomas: close correlation with invasion and metastasis. Pathobiology 2004;71:176-84.
52. + memory T cells. Proc Natl Acad Sci U S A 2002;99:6192-7.
53. Mayanil CS, George D, Freilich L, et al. Microarray analysis detects novel Pax3 downstream target genes. J Biol Chem 2001;276:49299-309.
54. Raghavendra Prasad HS, Qi Z, Srinivasan KN, Gopalakrishnakone P. Potential effects of tetrodotoxin exposure to human glial cells postulated using microarray approach. Toxicon 2004;44:597-608.
55. Kobayashi SD, Voyich JM, Braughton KR, DeLeo FR. Down-regulation of proinflammatory capacity during apoptosis in human polymorphonuclear leukocytes. J Immunol 2003;170:3357-68.
56. McLean DJ, Friel PJ, Pouchnik D, Griswold MD. Oligonucleotide microarray analysis of gene expression in follicle-stimulating hormone-treated rat Sertoli cells. Mol Endocrinol 2002;16:2780-92.
57. Gregory RC, Lord KA, Panek LB, Gaines P, Dillon SB, Wojchowski DM. Subtraction cloning and initial characterization of novel epo-immediate response genes. Cytokine 2000;12:845-57.
58. Richer JK, Jacobsen BM, Manning NG, Abel MG, Wolf DM, Horwitz KB. Differential gene regulation by the two progesterone receptor isoforms in human breast cancer cells. J Biol Chem 2002;277:5209-18.
59. Magnusson C, Svensson A, Christerson U, Tagerud S. Denervation-induced alterations in gene expression in mouse skeletal muscle. Eur J Neurosci 2005;21:577-80.
60. Kyng KJ, May A, Brosh RM, Jr., et al. The transcriptional response after oxidative stress is defective in Cockayne syndrome group B cells. Oncogene 2003;22:1135-49.