Inhibition of cancer cell growth by GRP78 siRNA lipoplex via activation of unfolded protein response

Biological and Pharmaceutical Bulletin

Volumn 37, Issue 4, 2014, Pages 648-653

  Matsumura, Kazushi ^a   Sakai, Chika ^a   Kawakami, Shigeru ^a,c   Yamashita, Fumiyoshi ^a   Hashida, Mitsuru ^a,b  

^a KYOTO UNIVERSITY   (Japan)

^b KYOTO UNIVERSITY   (Japan)

^c NAGASAKI UNIVERSITY   (Japan)

Author keywords

Apoptosis; Cancer cell; Endoplasmic reticulum stress; Glucose regulated protein 78; Small interfering RNA; Unfolded protein response

Indexed keywords

BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; DEOXYGLUCOSE; GLUCOSE REGULATED PROTEIN 78; LIPOPLEX; MESSENGER RNA; PROTEASOME INHIBITOR; SMALL INTERFERING RNA; TUNICAMYCIN; BENZYLOXYCARBONYLLEUCYL-LEUCYL-LEUCINE ALDEHYDE; HEAT SHOCK PROTEIN; LEUPEPTIN; MOLECULAR CHAPERONE GRP78;

ANIMAL CELL; APOPTOSIS; ARTICLE; CANCER INHIBITION; CANCER THERAPY; CARCINOMA CELL; CELL VIABILITY; CONTROLLED STUDY; DOWNSTREAM PROCESSING; ENDOPLASMIC RETICULUM STRESS; GENE EXPRESSION; GENETIC TRANSFECTION; IN VITRO STUDY; KIDNEY CARCINOMA; MELANOMA B16; MOUSE; NONHUMAN; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN SYNTHESIS; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; UNFOLDED PROTEIN RESPONSE; WESTERN BLOTTING; ANIMAL; ANTAGONISTS AND INHIBITORS; CELL PROLIFERATION; CELL SURVIVAL; DRUG EFFECTS; DRUG POTENTIATION; GENE EXPRESSION REGULATION; GENE SILENCING; SIGNAL TRANSDUCTION; TUMOR CELL LINE;

ANIMALS; CELL LINE, TUMOR; CELL PROLIFERATION; CELL SURVIVAL; DEOXYGLUCOSE; DRUG SYNERGISM; ENDOPLASMIC RETICULUM STRESS; GENE EXPRESSION REGULATION, NEOPLASTIC; GENE KNOCKDOWN TECHNIQUES; HEAT-SHOCK PROTEINS; LEUPEPTINS; MICE; RNA, SMALL INTERFERING; SIGNAL TRANSDUCTION; TRANSFECTION; TUNICAMYCIN; UNFOLDED PROTEIN RESPONSE;

EID: 84898760658     PISSN: 09186158     EISSN: 13475215     Source Type: Journal    
DOI: 10.1248/bpb.b13-00930     Document Type: Article

References (28)

1. Adams J. The proteasome: a suitable antineoplastic target. Nat. Rev. Cancer, 4, 349-360 (2004).
2. Kaufman RJ. Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls. Genes Dev., 13, 1211-1233 (1999).
3. Richardson PG, Sonneveld P, Schuster MW, Irwin D, Stadtmauer EA, Facon T, Harousseau JL, Ben-Yehuda D, Lonial S, Goldschmidt H, Reece D, San-Miguel JF, Bladé J, Boccadoro M, Cavenagh J, Dalton WS, Boral AL, Esseltine DL, Porter JB, Schenkein D, Anderson KC; Assessment of Proteasome Inhibition for Extending Remissions (APEX) Investigators. Bortezomib or high-dose dexamethasone for relapsed multiple myeloma. N. Engl. J. Med., 352, 2487-2498 (2005).
4. O'Connor OA, Wright J, Moskowitz C, Muzzy J, MacGregor-Cortelli B, Stubblefield M, Straus D, Portlock C, Hamlin P, Choi E, Dumetrescu O, Esseltine D, Trehu E, Adams J, Schenkein D, Zelenetz AD. Phase II clinical experience with the novel proteasome inhibitor bortezomib in patients with indolent non-Hodgkin's lymphoma and mantle cell lymphoma. J. Clin. Oncol., 23, 676-684 (2005).
5. Lawasut P, Chauhan D, Laubach J, Hayes C, Fabre C, Maglio M, Mitsiades C, Hideshima T, Anderson KC, Richardson PG. New proteasome inhibitors in myeloma. Curr. Hematol. Malig. Rep., 7, 258-266 (2012).
6. Schröder M, Kaufman RJ. The mammalian unfolded protein response. Annu. Rev. Biochem., 74, 739-789 (2005).
7. Nakajima S, Hiramatsu N, Hayakawa K, Saito Y, Kato H, Huang T, Yao J, Paton AW, Paton JC, Kitamura M. Selective abrogation of BiP/GRP78 blunts activation of NF-κB through the ATF6 branch of the UPR: involvement of C/ EBPβ and mTOR-dependent dephosphorylation of Akt. Mol. Cell. Biol., 31, 1710-1718 (2011).
8. Bertolotti A, Zhang Y, Hendershot LM, Harding HP, Ron D. Dynamic interaction of BiP and ER stress transducers in the unfoldedprotein response. Nat. Cell Biol., 2, 326-332 (2000).
9. Lee AS. The glucose-regulated proteins: stress induction and clinical applications. Trends Biochem. Sci., 26, 504-510 (2001).
10. Reddy RK, Mao C, Baumeister P, Austin RC, Kaufman RJ, Lee AS. Endoplasmic reticulum chaperone protein GRP78 protects cells from apoptosis induced by topoisomerase inhibitors: role of ATP binding site in suppression of caspase-7 activation. J. Biol. Chem., 278, 20915-20924 (2003).
11. Martin S, Hill DS, Paton JC, Paton AW, Birch-Machin MA, Lovat PE, Redfern CP. Targeting GRP78 to enhance melanoma cell death. Pigment Cell Melanoma Res., 23, 675-682 (2010).
12. Pyrko P, Schönthal AH, Hofman FM, Chen TC, Lee AS. The unfolded protein response regulator GRP78/BiP as a novel target for increasing chemosensitivity in malignant gliomas. Cancer Res., 67, 9809-9816 (2007).
13. Suzuki T, Lu J, Zahed M, Kita K, Suzuki N. Reduction of GRP78 expression with siRNA activates unfolded protein response leading to apoptosis in HeLa cells. Arch. Biochem. Biophys., 468, 1-14 (2007).
14. Li J, Lee AS. Stress induction of GRP78/BiP and its role in cancer. Curr. Mol. Med., 6, 45-54 (2006).
15. Virrey JJ, Dong D, Stiles C, Patterson JB, Pen L, Ni M, Schönthal AH, Chen TC, Hofman FM, Lee AS. Stress chaperone GRP78/BiP confers chemoresistance to tumor-associated endothelial cells. Mol. Cancer Res., 6, 1268-1275 (2008).
16. Xing X, Li Y, Liu H, Wang L, Sun L. Glucose regulated protein 78 (GRP78) is overexpressed in colorectal carcinoma and regulates colorectal carcinoma cell growth and apoptosis. Acta Histochem., 113, 777-782 (2011).
17. Wang Q, He Z, Zhang J, Wang Y, Wang T, Tong S, Wang L, Wang S, Chen Y. Overexpression of endoplasmic reticulum molecular chaperone GRP94 and GRP78 in human lung cancer tissues and its significance. Cancer Detect. Prev., 29, 544-551 (2005).
18. Xing X, Lai M, Wang Y, Xu E, Huang Q. Overexpression of glucose-regulated protein 78 in colon cancer. Clin. Chim. Acta, 364, 308-315 (2006).
19. Lee E, Nichols P, Spicer D, Groshen S, Yu MC, Lee AS. GRP78 as a novel predictor of responsiveness to chemotherapy in breast cancer. Cancer Res., 66, 7849-7853 (2006).
20. Sayers TJ, Brooks AD, Koh CY, Ma W, Seki N, Raziuddin A, Blazar BR, Zhang X, Elliott PJ, Murphy WJ. The proteasome inhibitor PS-341 sensitizes neoplastic cells to TRAIL-mediated apoptosis by reducing levels of c-FLIP. Blood, 102, 303-310 (2003).
21. Wolfson JJ, May KL, Thorpe CM, Jandhyala DM, Paton JC, Paton AW. Subtilase cytotoxin activates PERK, IRE1 and ATF6 endoplasmic reticulum stress-signalling pathways. Cell. Microbiol., 10, 1775-1786 (2008).
22. Olivari S, Cali T, Salo KE, Paganetti P, Ruddock LW, Molinari M. EDEM1 regulates ER-associated degradation by accelerating demannosylation of folding-defective polypeptides and by inhibiting their covalent aggregation. Biochem. Biophys. Res. Commun., 349, 1278-1284 (2006).
23. Shen Y, Meunier L, Hendershot LM. Identification and characterization of a novel endoplasmic reticulum (ER) DnaJ homologue, which stimulates ATPase activity of BiP in vitro and is induced by ER stress. J. Biol. Chem., 277, 15947-15956 (2002).
24. Li J, Lee AS. Stress induction of GRP78/BiP and its role in cancer. Curr. Mol. Med., 6, 45-54 (2006).
25. Jiang CC, Mao ZG, Avery-Kiejda KA, Wade M, Hersey P, Zhang XD. Glucose-regulated protein 78 antagonizes cisplatin and adriamycin in human melanoma cells. Carcinogenesis, 30, 197-204 (2008).
26. Lee E, Nichols P, Spicer D, Groshen S, Yu MC, Lee AS. GRP78 as a novel predictor of responsiveness to chemotherapy in breast cancer. Cancer Res., 66, 7849-7853 (2006).
27. Park HS, Jun do Y, Han CR, Woo HJ, Kim YH. Proteasome inhibitor MG132-induced apoptosis via ER stress-mediated apoptotic pathway and its potentiation by protein tyrosine kinase p56lck in human Jurkat T cells. Biochem. Pharmacol., 82, 1110-1125 (2011).
28. Xi H, Kurtoglu M, Liu H, Wangpaichitr M, You M, Liu X, Savaraj N, Lampidis TJ. 2-Deoxy- D -glucose activates autophagy via endoplasmic reticulum stress rather than ATP depletion. Cancer Chemother. Pharmacol., 67, 899-910 (2011).