Overexpression of the glucose-regulated stress gene GRP78 in malignant but not benign human breast lesions

Breast Cancer Research and Treatment

Volumn 59, Issue 1, 2000, Pages 15-26

  Fernandez, Patricia M ^a   Tabbara, Sana O ^a   Jacobs, Lisa K ^a   Manning, Frank C R ^a,b   Tsangaris, Theodore N ^a,c   Schwartz, Arnold M ^a   Kennedy, Katherine A ^a   Patierno, Steven R ^a  

^a GEORGE WASHINGTON UNIVERSITY MEDICAL CENTER   (United States)

^b LIVERPOOL JOHN MOORES UNIVERSITY   (United Kingdom)

^c GEORGETOWN UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Chemoresistance; Endoplasmic reticulum; GRP78; Human breast cancer

Indexed keywords

ESTROGEN RECEPTOR; GLUCOSE REGULATED PROTEIN; HEAT SHOCK PROTEIN; MESSENGER RNA;

ADOLESCENT; ADULT; ANIMAL CELL; APOPTOSIS; ARTICLE; BREAST CANCER; BREAST DISEASE; CANCER CHEMOTHERAPY; CLINICAL ARTICLE; CONTROLLED STUDY; GENE OVEREXPRESSION; HUMAN; HUMAN TISSUE; IMMUNOHISTOCHEMISTRY; NONHUMAN; NORTHERN BLOTTING; PRIORITY JOURNAL; PROTEIN EXPRESSION; WESTERN BLOTTING;

ADULT; AGED; APOPTOSIS; BREAST DISEASES; BREAST NEOPLASMS; CARRIER PROTEINS; FEMALE; GENE EXPRESSION REGULATION, NEOPLASTIC; HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; HUMANS; IMMUNOHISTOCHEMISTRY; MIDDLE AGED; MOLECULAR CHAPERONES; NEOPLASM PROTEINS;

EID: 0034021399     PISSN: 01676806     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1006332011207     Document Type: Article

References (63)

1. Feige U, Polla BS: Heat shock proteins: the hsp70 family. Experientia 50: 979-986, 1994
2. Little E, Ramakrishnan M, Roy B, Gazit G, Lee AS: The glucose-regulated proteins (GRP78 and GRP94): functions, gene regulation, and applications. Crit Rev Eukaryot Gene Expr 4: 1-18, 1994
3. Haas IG: Bip (GRP78), an essential hsp70 resident protein in the endoplasmic reticulum. Experientia 50: 1012-1020, 1994
4. Munro S, Pelham HRB: An Hsp70-like protein in the ER: identity with the 78 kd glucose regulated protein and immunoglobulin heavy chain binding proteins. Cell 46: 291-300, 1986
5. Lee AS: Coordinated regulation of a set of genes by glucose and calcium ionophores in mammalian cells. Trends Biochem 12: 20-23, 1987
6. Domer AJ, Wasley LC, Kaufman RJ: Protein dissociation from GRP78 and secretion are blocked by depletion of cellular ATP levels. Proc Natl Acad Sci USA 87: 7429-7432, 1990
7. Rothman JE: Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells. Cell 59: 591-601, 1989
8. Haas IG: BiP - a heat shock protein involved in immunoglobulin heavy chain assembly. Curr Topics Microbiol Immun 167: 71-82, 1991
9. Gething M-J, Sambrook J: Protein folding in the cell. Nature 355: 33-45, 1992
10. Kuznetsov G, Chen LB, Nigam SK: Multiple molecular chaperones complex with misfolded large oligomeric glycoproteins in the endoplasmic reticulum. J Biol Chem 272: 3057-3063, 1997
11. Gething M-J, McCammon K, Sambrook J: Expression of wild-type and mutant forms of influenza hemagglutinin: The role of folding in intracellular transport. Cell 46: 939-950, 1986
12. Silva AMD, Balch WE, Helenius A: Quality control in the endoplasmic reticulum: folding of vesicular stomatitis virus G protein in cells in vitro. J Cell Biol 111: 857-866, 1990
13. Vogel JP, Misra LM, Rose MD: Loss of BiP/GRP78 function blocks translocation of secretory proteins in yeast. J Cell Biol 110: 1885-1895, 1990
14. Nicchitta CV, Blobel G: Luminal proteins of the mammalian endoplasmic reticulum are required to complete protein translocation. Cell 73: 989-998, 1993
15. Lyman SK, Schekman R: Binding of secretory precursor polypeptides to a translocon subcomplex is regulated by BiP. Cell 88: 85-96, 1997
16. Knittler MR, Dirks S, Haas IG: Molecular chaperones involved in protein degradation in the endoplasmic reticulum: quantitative interaction of the heat shock cognate protein BiP with partially folded immunoglobulin light chains that are degraded in the endoplasmic reticulum. Proc Natl Acad Sci USA 92: 1764-1768, 1995
17. Lee AS, Delegeane AM, Baker V, Chow PC: Transcriptional regulation of two genes specifically induced by glucose starvation in a hamster mutant fibroblast cell line. J Biol Chem 258: 597-603, 1983
18. Lee AS: Mammalian stress response: induction of the glucose regulated protein family. Curr Opin Cell Biol 4: 267-273, 1992
19. Resendez EJ, Attenello JW, Grafsky A, Chang CS, Lee AS: Calcium ionophore A23187 induces expression of glucose-regulated genes and their heterologous fusion genes. Mol Cell Biol 5: 1212-1219, 1985
20. Watowich SS, Morimoto RI: Complex regulation of heat shock and glucose-responsive genes in human cells. Mol Cell Biol 8: 393-405, 1988
21. Dorner AJ, Wasley LC, Raney P, Haugejorden S, Green M, Kaufman RJ: The stress response in Chinese hamster ovary cells. J Biol Chem 265: 22029-22033, 1990
22. Liu ES, Ou J-h, Lee AS: Brefeldin A as a regulator of grp78 gene expression in mammalian cells. J Biol Chem 267: 7128-7133, 1992
23. Price BD, Mannheim-Rodman LA, Calderwood SK: Brefeldin A, Thapsigargin, and AIF4-stimulate the accumulation of GRP78 mRNA in a cycloheximide dependent manner, whilst induction by hypoxia is independent of protein synthesis. J Cell Physiol 152: 545-552, 1992
24. 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: 3278-3282, 1987
25. Hughes CS, Shen JW, Subjeck JR: Resistance to etoposide induced by three glucose-regulated stresses in Chinese hamster ovary cells. Cancer Res 49: 4452-4454, 1989
26. Vichi PJ, Tritton TR: Protection from adriamycin cytotoxicity in L1210 cells by brefeldin A. Cancer Res 53: 5237-5243, 1993
27. Chatterjee S, Cheng M-F, Berger SJ, Berger NA: Induction of Mr 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: 4405-4411, 1994
28. Chatterjee S, Cheng M-F, Berger RB, Berger SJ, Berger NA: Effect of inhibitors of poly(ADP-ribose) polymerase on the induction of GRP78 and subsequent development of resistance to etopiside. Cancer Res 55: 868-873, 1995
29. Yun J, Tomida A, Nagata K, Tsuruo T: Glucose-regulated stresses confer resistance to VP-16 in human cancer cells through a decreased expression of DNA topoisomerase II. Oncology Res 7: 583-590, 1995
30. Sacchi CM, Schiaffonati L: The effect of etopiside (VP-16) on mouse L fibroblasts: modulation of stress response, growth and apoptosis genes. Anticancer Res 16: 3659-3664, 1996
31. Sugawara S, Takeda K, Lee A, Dennert G: Suppression of stress protein GRP78 induction in tumor B/C10ME eliminates resistance to cell mediated cytotoxicity. Cancer Res 53: 6001-6005, 1993
32. Li L-J, Li X, Ferrario A, Rucker N, Liu ES, Wong S, Gomer CJ, Lee AS: Establishment of a Chinese hamster ovary cell line that expresses GRP78 antisense transcripts and suppresses A23187 induction of both GRP78 and GRP94. J Cell Physiol 153: 575-582, 1992
33. Koong AC, Chen EY, Lee AS, Brown JM, Giaccia AJ: Increased cytotoxicity of chronic hypoxic cells by molecular inhibition of GRP78 induction. Int J Radiat Oncol Biol Phys 28: 661-666, 1994
34. Chatterjee S, Hirota H, Belfi CA, Berger SJ, Berger NA: Hypersensitivity to DNA cross-linking agents associated with up-regulation of glucose-regulated stress protein GRP78. Cancer Res 57: 5112-5116, 1997
35. Kennedy KA: Hypoxic cells as specific drug targets for chemotherapy. Anti-Cancer Drug Design 2: 181-194, 1987
36. Vaupel P, Kallinowski F, Okunieff P: Blood flow, oxygen, and nutrient supply, and metabolic microenvironment of human tumors: A review. Cancer Res 49: 6449-6465, 1989
37. Pahl HL, Baeuerle PA: The ER-overload response: activation of NF-κB. Trends Biochem Sci 22: 63-67, 1997
38. Pahl HL, Baeuerle PA: Endoplasmic-reticulum-induced signal transduction and gene expression. Trends Cell Biol 7: 50-55, 1997
39. Kozutsumi Y, Segal M, Normington K, Gething M-J, Sambrook J: The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature 332: 462-464, 1988
40. Patierno SR, Tuscano JM, Kim KS, Landolph JR, Lee AS: Increased expression of the glucose-regulated gene encoding the Mr 78,000 glucose-regulated protein in chemically and radiation-transformed C3H 10T 1/2 mouse embryo cells. Cancer Res 47: 6220-6224, 1987
41. Cai JW, Henderson BW, Shen JW, Subjeck JR: Induction of glucose regulated proteins during growth of a murine tumor. J Cell Physiol 154: 229-237, 1993
42. Jamora C, Dennert G, Lee AS: Inhibition of tumor progression by suppression of stress protein GRP78/BiP induction in fibrosarcoma B/C10ME. Proc Natl Acad Sci USA 93: 7690-7694, 1996
43. Chomczynski P, Sacchi N: Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 162: 156-159, 1987
44. Manning FCR, Xu J, Patierno SR: Transcriptional inhibition by carcinogenic chromate: relationship to DNA damage. Mol Carcinogenesis 6: 156-159, 1992
45. Lee AS, Delegeane A, Scharff D: Highly conserved glucose-regulated protein in hamster and chicken cells: preliminary characterization of its cDNA clone. Proc Natl Acad Sci USA 78: 4922-4925, 1981
46. Feinberg AP, Vogelstcin B: A technique for radiolabelling DNA restriction endonuclease fragments to high specific activity. Anal Biochem 132: 6-13, 1983
47. Dive C, Hickman JA: Drug target interactions: only the first step in the commitment of a cell to a programmed cell death. Br J Cancer 64: 192-196, 1991
48. Dive C: Avoidance of apoptosis as a mechanism of drug resistance. J Int Med 242 (Suppl. 740): 139-145, 1997
49. McCormick TS, McColl KS, Distelhorst CW: Mouse lymphoma cells destined to undergo apoptosis in response to thapsigargin treatment fail to generate a calcium-mediated grp78/grp94 stress response. J Biol Chem 272: 6087-6092, 1997
50. Kaufmann S: Induction of endonucleolytic DNA cleavage in human acute myelogenous leukemic cells by etoposide, camptothecin, and other cytotoxic anticancer drugs: a cautionary note. Cancer Res 49: 5870-5878, 1989
51. Liu X, Kim CN, Yang J, Jemmerson R, Wang, X: Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell 86: 147-157, 1996
52. 2+ responses. Science 280: 1763-1766, 1998
53. Ciocca DR, Osterreich S, Chamness GC, McGuire WL, Fuqua S AW: Biological and clinical significance of heat shock protein 27,000 (Hsp27): a Review. J Natl Cancer Inst 85: 1558-1570, 1993
54. Edwards DP, Adams DJ, McGuire WL: Estradiol stimulates synthesis of a major intracellular protein in a human breast cancer cell line (MCF-7). Breast Cancer Res Treat 1: 209-223, 1981
55. Ramachandran C, Catelli MG, Schneider W, Shyamala G: Estrogenic regulation of uterine 90-kilodalton heat shock protein. Endocrinology 123: 956-961, 1988
56. Storm FK, Gilchrist KW, Warner TF, Mahvi DM: Distribution of Hsp-27 and HER-2/neu in in situ and invasive ductal breast carcinomas. Ann Surg Oncol 2: 43-48, 1995
57. Storm FK, Mahvi DM, Gilchrist KW: Lack of association between tumor necrosis and Hsp-27 expression in primary breast cancer. J Surg Oncol 61: 14-16, 1996
58. Fuqua SAW, Oesterreich S, Hilsenbeck SG, Von Hoff DD, Eckardt J, Osborne, CK: Heat shock proteins and drug resistance. Breast Cancer Res Treat, 32: 67-71, 1994
59. Oesterreich S, Weng C-N, Qiu M, Hilsenbeck SG, Osborne CK, Fuqua SAW: The small heat shock protein Hsp27 is correlated with growth and drug resistance in human breast cancer cell lines. Cancer Res 53: 4443-4448, 1993
60. Ciocca DR, Fuqua SAW, Lock-Lim S, Toft DO, Welch, WJ, McGuire WL: Response of human breast cancer cells to heat shock and chemotherapeutic drugs. Cancer Res 52: 3648-3654, 1992
61. Ciocca DR, Green S, Elledge RM, Clark GM, Pugh R, Ravdin P, Lew D, Martino S, Osborne CK: Heat shock proteins Hsp27 and Hsp70: Lack of correlation with response to tamoxifen and clinical course of disease in estrogen receptor-positive metastatic breast cancer (A Southwest Oncology Group Study). Clin Cancer Res 5: 1263-1266, 1998
62. Lin ZP, Boller YC, Amer SM, Russell RL, Pacelli KA, Patierno SR, Kennedy KA: Prevention of brefeldin A-induced resistance to teniposide by the proteasome inhibitor MG-132: involvement of NF-κB activation in drug resistance. Cancer Res 58: 3059-3065, 1998
63. Lin ZP, Patierno SR, Kennedy KA: Activation of NF-κ B is involved in hypoxia-induced drug resistance to topoisomerase 11-directed agents, (submitted), 1999