ICAM-1 and AMPK regulate cell detachment and apoptosis by N-methyl-N'-nitro-N-nitrosoguanidine, a widely spread environmental chemical, in human hormone-refractory prostate cancers

Toxicology and Applied Pharmacology

Volumn 257, Issue 3, 2011, Pages 412-419

  Chen, Yi Cheng ^a   Lu, Pin Hsuan ^a   Hsu, Jui Ling ^a   Yu, Chia Chun ^a   Guh, Jih Hwa ^a  

^a NATIONAL TAIWAN UNIVERSITY   (Taiwan)

Author keywords

AMP activated protein kinase; Intracellular cell adhesion molicule 1; MNNG; Nuclear factor b; Poly(ADP ribose) polymerase

Indexed keywords

GLYCOPROTEIN; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; I KAPPA B ALPHA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MESSENGER RNA; METHYLNITRONITROSOGUANIDINE; MITOGEN ACTIVATED PROTEIN KINASE P38; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 1; PROTEIN INTRACELLULAR ADHESION MOLECULE 1; PYRROLIDINE DITHIOCARBAMATE; STRESS ACTIVATED PROTEIN KINASE; UNCLASSIFIED DRUG; INTERCELLULAR ADHESION MOLECULE 1; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PARP1 PROTEIN, HUMAN;

APOPTOSIS; ARTICLE; CANCER CELL CULTURE; CELL ADHESION; CELL DEATH; CELL SURFACE; CELL SURVIVAL; CONTROLLED STUDY; HUMAN; HUMAN CELL; HUMAN TISSUE; MALE; PROSTATE CANCER; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; PROTEIN TRANSPORT; SIGNAL TRANSDUCTION; UPREGULATION; DNA DAMAGE; DOSE RESPONSE; DRUG EFFECT; GENETICS; METABOLISM; PATHOLOGY; PHOSPHORYLATION; PROSTATE TUMOR; TIME; TUMOR CELL LINE;

AMP-ACTIVATED PROTEIN KINASES; APOPTOSIS; CELL LINE, TUMOR; CELL SURVIVAL; DNA DAMAGE; DOSE-RESPONSE RELATIONSHIP, DRUG; HUMANS; INTERCELLULAR ADHESION MOLECULE-1; MALE; METHYLNITRONITROSOGUANIDINE; NF-KAPPA B; P38 MITOGEN-ACTIVATED PROTEIN KINASES; PHOSPHORYLATION; POLY(ADP-RIBOSE) POLYMERASES; PROSTATIC NEOPLASMS; RNA, MESSENGER; SIGNAL TRANSDUCTION; TIME FACTORS; UP-REGULATION;

EID: 84855720812     PISSN: 0041008X     EISSN: 10960333     Source Type: Journal    
DOI: 10.1016/j.taap.2011.09.025     Document Type: Article

References (46)

1. Allegra M., D'Acquisto F., Tesoriere L., Livrea M.A., Perretti M. Cross-talk between minimally primed HL-60 cells and resting HUVEC reveals a crucial role for adhesion over extracellularly released oxidants. Biochem. Pharmacol. 2011, 81:396-401.
2. Althaus F.R. Poly ADP-ribosylation: a histone shuttle mechanism in DNA excision repair. J. Cell Sci. 1992, 102:663-670.
3. Bai A., Ma A.G., Yong M., Weiss C.R., Ma Y., Guan Q., Bernstein C.N., Peng Z. AMPK agonist downregulates innate and adaptive immune responses in TNBS-induced murine acute and relapsing colitis. Biochem. Pharmacol. 2010, 80:1708-1717.
4. Carling D. The AMP-activated protein kinase cascade-a unifying system for energy control. Trends Biochem. Sci. 2004, 29:18-24.
5. Chen H.W., Chien M.L., Chaung Y.H., Lii C.K., Wang T.S. Extracts from cigarette smoke induce DNA damage and cell adhesion molecule expression through different pathways. Chem. Biol. Interact. 2004, 150:233-241.
6. Chiarugi A., Moskowitz M.A. Cell biology. PARP-1-a perpetrator of apoptotic cell death?. Science 2002, 297:200-201.
7. Cipriani G., Rapizzi E., Vannacci A., Rizzuto R., Moroni F., Chiarugi A. Nuclear poly(ADP-ribose) polymerase-1 rapidly triggers mitochondrial dysfunction. J. Biol. Chem. 2005, 280:17227-17234.
8. Conrad F., Zhu X., Zhang X., Chalkley R.J., Burlingame A.L., Marks J.D., Liu B. Human antibodies targeting cell surface antigens overexpressed by the hormone refractory metastatic prostate cancer cells: ICAM-1 is a tumor antigen that mediates prostate cancer cell invasion. J. Mol. Med. 2009, 87:507-514.
9. Cordes N. Integrin-mediated cell-matrix interactions for prosurvival and antiapoptotic signaling after genotoxic injury. Cancer Lett. 2006, 242:11-19.
10. Dal-Secco D., Freitas A., Abreu M.A., Garlet T.P., Rossi M.A., Ferreira S.H., Silva J.S., Alves-Filho J.C., Cunha F.Q. Reduction of ICAM-1 expression by carbon monoxide via soluble guanylate cyclase activation accounts for modulation of neutrophil migration. Naunyn Schmiedebergs Arch. Pharmacol. 2010, 381:483-493.
11. Dong Y., Bey E.A., Li L.S., Kabbani W., Yan J., Xie X.J., Hsieh J.T., Gao J., Boothman D.A. Prostate cancer radiosensitization through poly(ADP-Ribose) polymerase-1 hyperactivation. Cancer Res. 2010, 70:8088-8096.
12. Ewart M.A., Kohlhaas C.F., Salt I.P. Inhibition of tumor necrosis factor α-stimulated monocyte adhesion to human aortic endothelial cells by AMP-activated protein kinase. Arterioscler. Thromb. Vasc. Biol. 2008, 28:2255-2257.
13. Georgolios A., Batistatou A., Bonitsis N., Stagikas D., Manolopoulos L., Charalabopoulos K. The role of intercellular adhesion molecule-1 in head and neck cancer. Exp. Oncol. 2006, 28:270-274.
14. Giansanti V., Donà F., Tillhon M., Scovassi A.I. PARP inhibitors: new tools to protect from inflammation. Biochem. Pharmacol. 2010, 80:1869-1877.
15. Gottipati P., Vischioni B., Schultz N., Solomons J., Bryant H.E., Djureinovic T., Issaeva N., Sleeth K., Sharma R.A., Helleday T. Poly(ADP-ribose) polymerase is hyperactivated in homologous recombination-defective cells. Cancer Res. 2010, 70:5389-5398.
16. Gupta D., Podar K., Tai Y.T., Lin B., Hideshima T., Akiyama M., LeBlanc R., Catley L., Mitsiades N., Mitsiades C., Chauhan D., Munshi N.C., Anderson K.C. Beta-lapachone, a novel plant product, overcomes drug resistance in human multiple myeloma cells. Exp. Hematol. 2002, 30:711-720.
17. Ha H.C., Snyder S.H. Poly(ADP-ribose) polymerase-1 in the nervous system. Neurobiol. Dis. 2000, 7:225-239.
18. Hassa P.O., Hottiger M.O. The functional role of poly(ADP-ribose)polymerase 1 as novel coactivator of NF-kappaB in inflammatory disorders. Cell. Mol. Life Sci. 2002, 59:1534-1553.
19. Hawley S.A., Davison M., Woods A., Davies S.P., Beri R.K., Carling D., Hardie D.G. Characterization of the AMP-activated protein kinase kinase from rat liver and identification of threonine 172 as the major site at which it phosphorylates AMP-activated protein kinase. J. Biol. Chem. 1996, 271:27879-27887.
20. Hopkins A.M., Baird A.W., Nusrat A. ICAM-1: targeted docking for exogenous as well as endogenous ligands. Adv. Drug Deliv. Rev. 2004, 56:763-778.
21. Høyer-Hansen M., Jäättelä M. AMP-activated protein kinase: a universal regulator of autophagy?. Autophagy 2007, 3:381-383.
22. Johnson J.P. Cell adhesion molecules in the development and progression of malignant melanoma. Cancer Metastasis Rev. 1999, 18:345-357.
23. Jose C., Hébert-Chatelain E., Bellance N., Larendra A., Su M., Nouette-Gaulain K., Rossignol R. AICAR inhibits cancer cell growth and triggers cell-type distinct effects on OXPHOS biogenesis, oxidative stress and Akt activation. Biochim. Biophys. Acta 2011, 1807:707-718.
24. Kammerer S., Roth R.B., Reneland R., Marnellos G., Hoyal C.R., Markward N.J., Ebner F., Kiechle M., Schwarz-Boeger U., Griffiths L.R., Ulbrich C., Chrobok K., Forster G., Praetorius G.M., Meyer P., Rehbock J., Cantor C.R., Nelson M.R., Braun A. Large-scale association study identifies ICAM gene region as breast and prostate cancer susceptibility locus. Cancer Res. 2004, 64:8906-8910.
25. Kim E.K., Choi E.J. Pathological roles of MAPK signaling pathways in human diseases. Biochim. Biophys. Acta 2010, 1802:396-405.
26. Kim W.J., Beardsley D.I., Adamson A.W., Brown K.D. The monofunctional alkylating agent N-methyl-N'-nitro-N-nitrosoguanidine triggers apoptosis through p53-dependent and -independent pathways. Toxicol. Appl. Pharmacol. 2005, 202:84-98.
27. Kirkland J.B. Poly ADP-ribose polymerase-1 and health. Exp. Biol. Med. (Maywood) 2010, 235:561-568.
28. Koh H.J., Brandauer J., Goodyear L.J. LKB1 and AMPK and the regulation of skeletal muscle metabolism. Curr. Opin. Clin. Nutr. Metab. Care 2008, 11:227-232.
29. Labuzek K., Liber S., Gabryel B., Adamczyk J., Okopień B. Metformin increases phagocytosis and acidifies lysosomal/endosomal compartments in AMPK-dependent manner in rat primary microglia. Naunyn Schmiedebergs Arch. Pharmacol. 2010, 381:171-186.
30. Lim S.O., Gu J.M., Kim M.S., Kim H.S., Park Y.N., Park C.K., Cho J.W., Park Y.M., Jung G. Epigenetic changes induced by reactive oxygen species in hepatocellular carcinoma: methylation of the E-cadherin promoter. Gastroenterology 2008, 135:2128-2140.
31. Luo Z., Saha A.K., Xiang X., Ruderman N.B. AMPK, the metabolic syndrome and cancer. Trends Pharmacol. Sci. 2005, 26:69-76.
32. Manikandan P., Vidjaya Letchoumy P., Prathiba D., Nagini S. Proliferation, angiogenesis and apoptosis-associated proteins are molecular targets for chemoprevention of MNNG-induced gastric carcinogenesis by ethanolic Ocimum sanctum leaf extract. Singapore Med. J. 2007, 48:645-651.
33. Mégnin-Chanet F., Bollet M.A., Hall J. Targeting poly(ADP-ribose) polymerase activity for cancer therapy. Cell. Mol. Life Sci. 2010, 67:3649-3662.
34. Nakajima H., Nagaso H., Kakui N., Ishikawa M., Hiranuma T., Hoshiko S. Critical role of the automodification of poly(ADP-ribose) polymerase-1 in nuclear factor-kappaB-dependent gene expression in primary cultured mouse glial cells. J. Biol. Chem. 2004, 279:42774-42786.
35. Pan J.S., Hong M.Z., Ren J.L. Reactive oxygen species: a double-edged sword in oncogenesis. World J. Gastroenterol. 2009, 15:1702-1707.
36. Panwalkar A., Verstovsek S., Giles F. Nuclear factor-kappaB modulation as a therapeutic approach in hematologic malignancies. Cancer 2004, 100:1578-1589.
37. Piela-Smith T.H., Aune T., Aneiro L., Nuveen E., Korn J.H. Impairment of lymphocyte adhesion to cultured fibroblasts and endothelial cells by gamma-irradiation. J. Immunol. 1992, 148:41-46.
38. Ray R.M., Jin S., Bavaria M.N., Johnson L.R. Regulation of JNK activity in the apoptotic response of intestinal epithelial cells. Am. J. Physiol. Gastrointest. Liver Physiol. 2011, 300:G761-G770.
39. Sanli T., Rashid A., Liu C., Harding S., Bristow R.G., Cutz J.C., Singh G., Wright J., Tsakiridis T. Ionizing radiation activates AMP-activated kinase (AMPK): a target for radiosensitization of human cancer cells. Int. J. Radiat. Oncol. Biol. Phys. 2010, 78:221-229.
40. Schins R.P., Borm P.J. Mechanisms and mediators in coal dust induced toxicity: a review. Ann. Occup. Hyg. 1999, 43:7-33.
41. Sodhi R.K., Singh N., Jaggi A.S. Poly(ADP-ribose) polymerase-1 (PARP-1) and its therapeutic implications. Vascul. Pharmacol. 2010, 53:77-87.
42. Virág L., Szabó C. The therapeutic potential of poly(ADP-ribose) polymerase inhibitors. Pharmacol. Rev. 2002, 54:375-429.
43. Woods A., Vertommen D., Neumann D., Turk R., Bayliss J., Schlattner U., Wallimann T., Carling D., Rider M.H. Identification of phosphorylation sites in AMP-activated protein kinase (AMPK) for upstream AMPK kinases and study of their roles by site-directed mutagenesis. J. Biol. Chem. 2003, 278:28434-28442.
44. Wyatt M.D., Pittman D.L. Methylating agents and DNA repair responses: methylated bases and sources of strand breaks. Chem. Res. Toxicol. 2006, 19:1580-1594.
45. Xu Y., Huang S., Liu Z.G., Han J. Poly(ADP-ribose) polymerase-1 signaling to mitochondria in necrotic cell death requires RIP1/TRAF2-mediated JNK1 activation. J. Biol. Chem. 2006, 281:8788-8795.
46. Yodkeeree S., Ampasavate C., Sung B., Aggarwal B.B., Limtrakul P. Demethoxycurcumin suppresses migration and invasion of MDA-MB-231 human breast cancer cell line. Eur. J. Pharmacol. 2010, 627:8-15.