Down-regulation of topoisomerase IIα is caused by up-regulation of GRP78

Biochemical and Biophysical Research Communications

Volumn 300, Issue 2, 2003, Pages 327-332

  Gosky, David ^a   Chatterjee, Satadal ^a  

^a CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

2 Deoxyglucose; 6 Aminonicotinamide; GRP78; PARP1; Topo II ; VP 16 resistance

Indexed keywords

6 AMINONICOTINAMIDE; DEOXYGLUCOSE; DNA TOPOISOMERASE (ATP HYDROLYSING); GLUCOSE REGULATED PROTEIN 78; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; ANTINEOPLASTIC AGENT; CARRIER PROTEIN; CHAPERONE; DNA; DNA BINDING PROTEIN; DNA TOPOISOMERASE II ALPHA; ETOPOSIDE; HEAT SHOCK PROTEIN; MOLECULAR CHAPERONE GRP78; PROTEIN; TUMOR ANTIGEN;

ANIMAL CELL; ARTICLE; CHINESE HAMSTER; CONTROLLED STUDY; DOWN REGULATION; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME KINETICS; ENZYME METABOLISM; ENZYME REGULATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN INDUCTION; UPREGULATION; ANIMAL; BIOSYNTHESIS; CELL LINE; DRUG RESISTANCE; HAMSTER; METABOLISM;

CRICETINAE; CRICETULUS GRISEUS;

6-AMINONICOTINAMIDE; ANIMALS; ANTIGENS, NEOPLASM; ANTINEOPLASTIC AGENTS, PHYTOGENIC; CARRIER PROTEINS; CELL LINE; CRICETINAE; DEOXYGLUCOSE; DNA; DNA TOPOISOMERASES, TYPE II, EUKARYOTIC; DNA-BINDING PROTEINS; DOWN-REGULATION; DRUG RESISTANCE; ETOPOSIDE; HEAT-SHOCK PROTEINS; MOLECULAR CHAPERONES; PROTEINS; UP-REGULATION;

EID: 0037427527     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(02)02857-7     Document Type: Article

References (46)

1. Lee A.S. Coordinated regulation of a set of genes by glucose and calcium ionophores in mammalian cells. Trends Biochem. Sci. 12:1987;20-23.
2. Schlesinger M.J. Heat shock proteins. J. Biol. Chem. 265:1990;12111- 12114.
3. Gething M.J., Sambrook J. Protein folding in the cell. Nature (London). 355:1992;33-45.
4. Kozutsumi Y., Segal M., Normington K., Gething M., Sambrook J. The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature (London). 332:1988;462-464.
5. Sutherland R. Cell and environment interactions in tumor microregions: the multicell spheroid mode. Science. 240:1988;177-184.
6. Cai J., Henderson B., Shen J., Subjeck J. Induction of glucose regulated proteins during growth of a murine tumor. J. Cell. Physiol. 154:1993;229-237.
7. Shen J., Hughes C., Chao C., Cai J., Bartels C., Gressner T., Subjeck J. Coinduction of glucose-regulated proteins and doxorubicin resistance in Chinese hamster cells. Proc. Natl. Acad. Sci. (USA). 84:1987;3278-3282.
8. Morris J., Dorner A., Edwards C., Hendershot L., Kaufman R. Immunoglobulin binding protein (BiP) function is required to protect cells from endoplasmic reticulum stress but is not required for the secretion of selective proteins. J. Biol. Chem. 272:1997;4327-4334.
9. Chatterjee S., Cheng M., Berger S.J., Berger N.A. Induction of. M(r) 78, 000 glucose-regulated stress protein in poly(adenosine diphosphate-ribose) polymerase- and nicotinamide adenine dinucleotide-deficient V79 cell lines and its relation to resistance to the topoisomerase II inhibitor etoposide Cancer Res. 54:1994;4405-4411.
10. Chatterjee S., Berger N.A. Poly(ADP-ribose) polymerase in response to DNA damage. Nicoloff J.A., Hoekstra M. DNA Damage and Repair: Vol. 2, DNA Repair in Higher Eucaryotes, Chapter 22. 1998;487-515 Humana Press, Clifton, UK.
11. Chatterjee S., Cheng M., Berger R., Berger S.J., Berger N.A. Effect of inhibitors of poly(ADP-ribose) polymerase on the induction of GRP78 and subsequent development of resistance to etoposide. Cancer Res. 55:1995;868-873.
12. Chatterjee S., Hirota H., Belfi C., Berger S.J., Berger N.A. Hypersensitivity to DNA cross-linking agents associated with up-regulation of glucose-regulated stress protein GRP78. Cancer Res. 57:1997;5112-5116.
13. Belfi C., Chatterjee S., Gosky D., Berger S.J., Berger N.A. Increased sensitivity of human colon cancer cells to DNA cross-linking agents after GRP78 up-regulation. Biochem. Biophys. Res. Commun. 257:1999;361-368.
14. Dietrich L.S., Friedland I.M., Kaplan L.A. Pyridine nucleotide metabolism: mechanism of action of the niacin antagonist, 6-aminonicotinamide. J. Biol. Chem. 233:1958;964-968.
15. Dietrich L.S., Kaplan L.A., Friedland I.M., Martin D.S. Quantitative biochemical differences between tumor and host tissue, 6-aminonicotinamide antagonism of DPN-dependent enzymatic systems. Cancer Res. 18:1958;1272-1280.
16. Gellert M. DNA topoisomerases. Annu. Rev. Biochem. 50:1981;879-910.
17. Wang J.C. DNA topoisomerases. Annu. Rev. Biochem. 54:1985;665-697.
18. Ross W. DNA topoisomerases as targets for cancer therapy. Biochem. Pharmacol. 34:1985;4191-4195.
19. Spiridonidis C.A., Chatterjee S., Petzold S.J., Berger N.A. Topoisomerase II-dependent and -independent mechanisms of etoposide resistance in Chinese hamster cell lines. Cancer Res. 49:1989;644-650.
20. Liu L. DNA topoisomerase poisons as antitumor drugs. Annu. Rev. Biochem. 58:1989;351-375.
21. Berger N.A., Chatterjee S., Schmotzer J.A., Helms S.R. Etoposide(VP-16-213)-induced gene alterations: potential contribution to cell death. Proc. Natl. Acad. Sci. (USA). 88:1991;8740-8743.
22. Sperry A.O., Blasquez V.C., Garrard W.T. Dysfunction of chromosomal loop attachment sites: illegitimate recombination linked to matrix association regions and topoisomerase II. Proc. Natl. Acad. Sci. (USA). 86:1989;5497-5501.
23. O'Dwyer P.J., Leyland-Jones B., Alonso M.T., Marsoni S., Wittes R.E. Etoposide(VP-16-213). Current status of an active anticancer drug. N. Eng. J. Med. 312:1985;692-700.
24. Zwelling L.A. DNA topoisomerase II as a target of antineoplastic drug therapy. Cancer Metastasis Rev. 4:1985;263-276.
25. Ross W., Rowe T., Glisson B., Yalowich J., Liu L. Role of topoisomerase II in mediating epipodophyllotoxin-induced DNA cleavage. Cancer Res. 44:1984;5857-5860.
26. Wang J.C. Recent studies of DNA topoisomerases. Biochem. Biophys. Acta. 909:1987;1-9.
27. r 170, 000 isozyme of DNA topoisomerase II in human tumor cells Cancer Res. 53:1993;1373-1379.
28. Pommier Y., Kerigan D., Schwartz R.E., Swack J.A., McCurdy A. Altered topoisomerase II activity in Chinese hamster cells resistant to topoisomerase II inhibitors. Cancer Res. 46:1986;3075-3081.
29. Hirota H., Gosky D., Berger N.A., Chatterjee S. Interference with topoisomerase II. α potentiates melphalan cytotoxicity Int. J. Oncol. 20:2002;311-318.
30. Ferguson P.J., Fisher M.H., Stephenson J., Li D.H., Zhou B.S., Cheng Y.C. Combined modalities of resistance in etoposide-resistant human KB cell lines. Cancer Res. 48:1988;5956-5964.
31. Danks M.K., Yalowich J.C., Beck W.T. Atypical multiple drug resistance in a human leukemic cell line selected for resistance to teniposide (VM -26). Cancer Res. 47:1987;1297-1301.
32. Shen J., Hughes C., Chao C., Cai J., Bartels C., Gessner T., Subjeck J. Coinduction of glucose-regulated proteins and doxorubicin resistance in Chinese hamster cells. Proc. Natl. Acad. Sci. (USA). 84:1987;3278-3282.
33. Hughes C.S., Shen J.W., Subjeck J.R. Resistance to etoposide(VP-16) induced by three glucose-regulated stresses in Chinese hamster ovary cells. Cancer Res. 49:1989;4452-4454.
34. Chatterjee S., Petzold S.J., Berger S.J., Berger N.A. Strategy for selection of cell variants deficient in poly(ADP-ribose) polymerase. Exp. Cell Res. 172:1987;245-257.
35. Chatterjee S., Hirschler N.V., Petzold S.J., Berger S.J., Berger N.A. Mutant cells defective in poly(ADP-ribose) synthesis due to stable alterations in enzyme activity or substrate availability. Exp. Cell Res. 184:1989;1-15.
36. ′ flanking region of the DNA-binding domain of topoisomerase II α associated with acquired resistance to topoisomerase II active agents Oncol. Res. 7:1995;21-29.
37. Hashimoto S., Chatterjee S., Ranjit G.B., Bao C., Ford J., Ganapathi R., Berger S.J., Berger N.A. Drastic reduction of topoisomerase II. α associated with major acquired resistance to topoisomerase II active agents but minor perturbations of cell growth Oncol. Res. 7:1995;407-416.
38. Hashimoto H., Chatterjee S., Berger N.A. Inhibition of etoposide(VP-16)-induced DNA recombination and mutant frequency by Bcl-2 protein overexpression. Cancer Res. 55:1995;4029-4035.
39. Duguet M., Lavenot C., Harper F., Mirambeau F., DeRecondo A.-M. DNA topoisomerases from rat liver: physiological variations. Nucleic Acids Res. 11:1983;1059-1075.
40. Muller M.T. Nucleosomes contain DNA binding proteins that resist dissociation by sodium dodecyl sulphate. Biochem. Biophys. Res. Commun. 114:1983;99-106.
41. Zwelling L.A., Hinds M., Chan D., Mayes J., Sie K.L., Parker E., Silberman L., Radcliffe A., Beran M., Blick M. Characterization of an amsacrine-resistant line of human leukemia cells. Evidence for a drug-resistant form of topoisomerase II. J. Biol. Chem. 264:1989;16411-16420.
42. Chatterjee S., Trivedi D., Petzold S.J., Berger N.A. Mechanism of epipodophyllotoxin-induced cell death in poly(adenosine diphosphate-ribose) synthesis-deficient V79 Chinese hamster cell lines. Cancer Res. 50:1990;2713-2718.
43. Hass I.G. BiP(GRP78), an essential hsp70 resident protein in the endoplasmic reticulum. Experientia. 50:1994;1012-1020.
44. Cai B., Tomida A., Mikami K., Nagata K., Tsuruo T. Down-regulation of epidermal growth factor receptor-signaling pathway by binding of GRP78/BiP to the receptor under glucose-starved stress conditions. J. Cell. Physiol. 177:1988;282-288.
45. Thorson A.H. Studies of carcinoid disease. Acta Med. Scand. 161(Suppl. 334):1958;81-98.
46. Davis Z., Moertel C.G., Mcllrath D.C. The malignant carcinoid syndrome. Sur. Gynecol. Obstet. 137:1973;637-644.