메뉴 건너뛰기




Volumn 90, Issue 2, 2012, Pages 224-231

HSPA2 overexpression protects V79 fibroblasts against bortezomib-induced apoptosis

Author keywords

Apoptosis; Cytoprotection; HSP70 family proteins; Proteasome inhibitors

Indexed keywords

CELL LINES; CHINESE HAMSTERS; CULTURE CONDITIONS; CYTOPROTECTION; CYTOTOXIC; HEAT-SHOCK; HEAT-SHOCK PROTEIN; OVER-EXPRESSION; PROTEASOME INHIBITORS; PROTEOTOXIC STRESS; SOMATIC CELLS; SOMATIC TISSUES; TOXIC EFFECT; V79-CELLS;

EID: 84862750260     PISSN: 08298211     EISSN: 12086002     Source Type: Journal    
DOI: 10.1139/o11-083     Document Type: Article
Times cited : (16)

References (33)
  • 1
    • 77953861120 scopus 로고    scopus 로고
    • Differential expression patterns of Puma and Hsp70 following proteasomal stress in the hippocampus are key determinants of neuronal vulnerability
    • 10.1111/j.1471-4159.2010.06790.x 20477911
    • Bonner H.P. Concannon C.G. Bonner C. Woods I. Ward M.W. Prehn J.H. 2010. Differential expression patterns of Puma and Hsp70 following proteasomal stress in the hippocampus are key determinants of neuronal vulnerability. J. Neurochem. 114 (2): 606-616. 10.1111/j.1471-4159.2010.06790.x 20477911
    • (2010) J. Neurochem. , vol.114 , Issue.2 , pp. 606-616
    • Bonner, H.P.1    Concannon, C.G.2    Bonner, C.3    Woods, I.4    Ward, M.W.5    Prehn, J.H.6
  • 2
    • 0027965687 scopus 로고
    • Cloning, sequencing, and mapping of the human chromosome 14 heat shock protein gene (HSPA2)
    • 10.1006/geno.1994.1462 7829106
    • Bonnycastle L.L. Yu C.E. Hunt C.R. Trask B.J. Clancy K.P. Weber J.L. et al. 1994. Cloning, sequencing, and mapping of the human chromosome 14 heat shock protein gene (HSPA2). Genomics, 23 (1): 85-93. 10.1006/geno.1994.1462 7829106
    • (1994) Genomics , vol.23 , Issue.1 , pp. 85-93
    • Bonnycastle, L.L.1    Yu, C.E.2    Hunt, C.R.3    Trask, B.J.4    Clancy, K.P.5    Weber, J.L.6
  • 3
    • 38649094249 scopus 로고    scopus 로고
    • Heat shock proteins: Stress proteins with Janus-like properties in cancer
    • 10.1080/02656730701858305 18214767
    • Calderwood S.K. Ciocca D.R. 2008. Heat shock proteins: stress proteins with Janus-like properties in cancer. Int. J. Hyperthermia, 24 (1): 31-39. 10.1080/02656730701858305 18214767
    • (2008) Int. J. Hyperthermia , vol.24 , Issue.1 , pp. 31-39
    • Calderwood, S.K.1    Ciocca, D.R.2
  • 4
    • 33644835965 scopus 로고    scopus 로고
    • Heat shock proteins in cancer: Chaperones of tumorigenesis
    • 10.1016/j.tibs.2006.01.006 16483782
    • Calderwood S.K. Khaleque M.A. Sawyer D.B. Ciocca D.R. 2006. Heat shock proteins in cancer: chaperones of tumorigenesis. Trends Biochem. Sci. 31 (3): 164-172. 10.1016/j.tibs.2006.01.006 16483782
    • (2006) Trends Biochem. Sci. , vol.31 , Issue.3 , pp. 164-172
    • Calderwood, S.K.1    Khaleque, M.A.2    Sawyer, D.B.3    Ciocca, D.R.4
  • 5
    • 34548533382 scopus 로고    scopus 로고
    • Hsp72 controls bortezomib-induced HepG2 cell death via interaction with pro-apoptotic factors
    • 17611669
    • Calvaruso G. Giuliano M. Portanova P. Pellerito O. Vento R. Tesoriere G. 2007. Hsp72 controls bortezomib-induced HepG2 cell death via interaction with pro-apoptotic factors. Oncol. Rep. 18 (2): 447-450. 17611669
    • (2007) Oncol. Rep. , vol.18 , Issue.2 , pp. 447-450
    • Calvaruso, G.1    Giuliano, M.2    Portanova, P.3    Pellerito, O.4    Vento, R.5    Tesoriere, G.6
  • 6
    • 33746020449 scopus 로고    scopus 로고
    • Oligozoospermia and heat-shock protein expression in ejaculated spermatozoa
    • 10.1093/humrep/del055 16517558
    • Cedenho A.P. Lima S.B. Cenedeze M.A. Spaine D.M. Ortiz V. Oehninger S. 2006. Oligozoospermia and heat-shock protein expression in ejaculated spermatozoa. Hum. Reprod. 21 (7): 1791-1794. 10.1093/humrep/del055 16517558
    • (2006) Hum. Reprod. , vol.21 , Issue.7 , pp. 1791-1794
    • Cedenho, A.P.1    Lima, S.B.2    Cenedeze, M.A.3    Spaine, D.M.4    Ortiz, V.5    Oehninger, S.6
  • 7
    • 0141953292 scopus 로고    scopus 로고
    • Blockade of Hsp27 overcomes Bortezomib/proteasome inhibitor PS-341 resistance in lymphoma cells
    • 14559800
    • Chauhan D. Li G. Shringarpure R. Podar K. Ohtake Y. Hideshima T. Anderson K.C. 2003. Blockade of Hsp27 overcomes Bortezomib/proteasome inhibitor PS-341 resistance in lymphoma cells. Cancer Res. 63 (19): 6174-6177. 14559800
    • (2003) Cancer Res. , vol.63 , Issue.19 , pp. 6174-6177
    • Chauhan, D.1    Li, G.2    Shringarpure, R.3    Podar, K.4    Ohtake, Y.5    Hideshima, T.6    Anderson, K.C.7
  • 8
    • 0030751965 scopus 로고    scopus 로고
    • The p53 status of Chinese hamster V79 cells frequently used for studies on DNA damage and DNA repair
    • 10.1093/nar/25.5.992 9023109
    • Chaung W. Mi L.J. Boorstein R.J. 1997. The p53 status of Chinese hamster V79 cells frequently used for studies on DNA damage and DNA repair. Nucleic Acids Res. 25 (5): 992-994. 10.1093/nar/25.5.992 9023109
    • (1997) Nucleic Acids Res. , vol.25 , Issue.5 , pp. 992-994
    • Chaung, W.1    Mi, L.J.2    Boorstein, R.J.3
  • 9
    • 79951702955 scopus 로고    scopus 로고
    • Bortezomib as the first proteasome inhibitor anticancer drug: Current status and future perspectives
    • 10.2174/156800911794519752 21247388
    • Chen D. Frezza M. Schmitt S. Kanwar J. P Dou Q. 2011. Bortezomib as the first proteasome inhibitor anticancer drug: current status and future perspectives. Curr. Cancer Drug Targets, 11 (3): 239-253. 10.2174/ 156800911794519752 21247388
    • (2011) Curr. Cancer Drug Targets , vol.11 , Issue.3 , pp. 239-253
    • Chen, D.1    Frezza, M.2    Schmitt, S.3    Kanwar, J.4    Dou Q, P.5
  • 10
    • 47349102144 scopus 로고    scopus 로고
    • Effect of bortezomib on human neuroblastoma: Analysis of molecular mechanisms involved in cytotoxicity
    • 10.1186/1476-4598-7-50 18534018
    • Combaret V. Boyault S. Iacono I. Brejon S. Rousseau R. Puisieux A. 2008. Effect of bortezomib on human neuroblastoma: analysis of molecular mechanisms involved in cytotoxicity. Mol. Cancer, 7 (1): 50. 10.1186/1476-4598-7-50 18534018
    • (2008) Mol. Cancer , vol.7 , Issue.1 , pp. 50
    • Combaret, V.1    Boyault, S.2    Iacono, I.3    Brejon, S.4    Rousseau, R.5    Puisieux, A.6
  • 11
    • 79956366646 scopus 로고    scopus 로고
    • Proteasome inhibitors in cancer therapy
    • 10.1007/s12079-011-0121-7 21484190
    • Crawford L.J. Walker B. Irvine A.E. 2011. Proteasome inhibitors in cancer therapy. J. Cell Commun. Signal. 5 (2): 101-110. 10.1007/s12079-011-0121-7 21484190
    • (2011) J. Cell Commun. Signal. , vol.5 , Issue.2 , pp. 101-110
    • Crawford, L.J.1    Walker, B.2    Irvine, A.E.3
  • 12
    • 34447528828 scopus 로고    scopus 로고
    • Daugaard M. Rohde M. Jttelä M. The heat shock protein 70 family: Highly homologous proteins with overlapping and distinct functions. (19): 3702 - 3710. 10.1016/j.febslet.2007.05.039 17544402
    • Daugaard M. Rohde M. Jttelä M. 2007. The heat shock protein 70 family: Highly homologous proteins with overlapping and distinct functions. FEBS Lett. 581 (19): 3702 - 3710. 10.1016/j.febslet.2007.05.039 17544402
    • (2007) FEBS Lett. , vol.581
  • 13
    • 0030721027 scopus 로고    scopus 로고
    • HSP70-2 is required for desynapsis of synaptonemal complexes during meiotic prophase in juvenile and adult mouse spermatocytes
    • 9409676
    • Dix D.J. Allen J.W. Collins B.W. Poorman-Allen P. Mori C. Blizard D.R. et al. 1997. HSP70-2 is required for desynapsis of synaptonemal complexes during meiotic prophase in juvenile and adult mouse spermatocytes. Development, 124 (22): 4595-4603. 9409676
    • (1997) Development , vol.124 , Issue.22 , pp. 4595-4603
    • Dix, D.J.1    Allen, J.W.2    Collins, B.W.3    Poorman-Allen, P.4    Mori, C.5    Blizard, D.R.6
  • 14
    • 71049173726 scopus 로고    scopus 로고
    • Heat-shock protein 70-2 (HSP70-2) expression in bladder urothelial carcinoma is associated with tumour progression and promotes migration and invasion
    • 10.1016/j.ejca.2009.10.020 19914824
    • Garg M. Kanojia D. Seth A. Kumar R. Gupta A. Surolia A. Suri A. 2010. Heat-shock protein 70-2 (HSP70-2) expression in bladder urothelial carcinoma is associated with tumour progression and promotes migration and invasion. Eur. J. Cancer, 46 (1): 207-215. 10.1016/j.ejca.2009.10.020 19914824
    • (2010) Eur. J. Cancer , vol.46 , Issue.1 , pp. 207-215
    • Garg, M.1    Kanojia, D.2    Seth, A.3    Kumar, R.4    Gupta, A.5    Surolia, A.6    Suri, A.7
  • 15
    • 0037168972 scopus 로고    scopus 로고
    • HSP70 overexpression increases resistance of V79 cells to cytotoxicity of airborne pollutants, but does not protect the mitotic spindle against damage caused by airborne toxins
    • 10.1016/S0300-483X(01)00556-X 11788158
    • Glowala M. Mazurek A. Piddubnyak V. Fiszer-Kierzkowska A. Michalska J. Krawczyk Z. 2002. HSP70 overexpression increases resistance of V79 cells to cytotoxicity of airborne pollutants, but does not protect the mitotic spindle against damage caused by airborne toxins. Toxicology, 170 (3): 211-219. 10.1016/S0300-483X(01)00556-X 11788158
    • (2002) Toxicology , vol.170 , Issue.3 , pp. 211-219
    • Glowala, M.1    Mazurek, A.2    Piddubnyak, V.3    Fiszer-Kierzkowska, A.4    Michalska, J.5    Krawczyk, Z.6
  • 16
    • 79952833763 scopus 로고    scopus 로고
    • The diverse members of the mammalian HSP70 machine show distinct chaperone-like activities
    • 10.1042/BJ20101247 21231916
    • Hageman J. van Waarde M.A. Zylicz A. Walerych D. Kampinga H.H. 2011. The diverse members of the mammalian HSP70 machine show distinct chaperone-like activities. Biochem. J. 435 (1): 127-142. 10.1042/BJ20101247 21231916
    • (2011) Biochem. J. , vol.435 , Issue.1 , pp. 127-142
    • Hageman, J.1    Van Waarde, M.A.2    Zylicz, A.3    Walerych, D.4    Kampinga, H.H.5
  • 17
    • 0033837992 scopus 로고    scopus 로고
    • Putative creatine kinase M-isoform in human sperm is identified as the 70-kilodalton heat shock protein HspA2
    • 10.1095/biolreprod63.3.925 10952940
    • Huszar G. Stone K. Dix D. Vigue L. 2000. Putative creatine kinase M-isoform in human sperm is identified as the 70-kilodalton heat shock protein HspA2. Biol. Reprod. 63 (3): 925-932. 10.1095/biolreprod63.3.925 10952940
    • (2000) Biol. Reprod. , vol.63 , Issue.3 , pp. 925-932
    • Huszar, G.1    Stone, K.2    Dix, D.3    Vigue, L.4
  • 18
    • 23044444001 scopus 로고    scopus 로고
    • Hsp70 protects mitotic cells against heat-induced centrosome damage and division abnormalities
    • 10.1091/mbc.E05-01-0038 15930131
    • Hut H.M. Kampinga H.H. Sibon O.C. 2005. Hsp70 protects mitotic cells against heat-induced centrosome damage and division abnormalities. Mol. Biol. Cell, 16 (8): 3776-3785. 10.1091/mbc.E05-01-0038 15930131
    • (2005) Mol. Biol. Cell , vol.16 , Issue.8 , pp. 3776-3785
    • Hut, H.M.1    Kampinga, H.H.2    Sibon, O.C.3
  • 19
    • 0036071225 scopus 로고    scopus 로고
    • Stressful preconditioning and HSP70 overexpression attenuate proteotoxicity of cellular ATP depletion
    • 12107062
    • Kabakov A.E. Budagova K.R. Latchman D.S. Kampinga H.H. 2002. Stressful preconditioning and HSP70 overexpression attenuate proteotoxicity of cellular ATP depletion. Am. J. Physiol. Cell Physiol. 283 (2): C521-C534. 12107062
    • (2002) Am. J. Physiol. Cell Physiol. , vol.283 , Issue.2
    • Kabakov, A.E.1    Budagova, K.R.2    Latchman, D.S.3    Kampinga, H.H.4
  • 20
    • 64549097439 scopus 로고    scopus 로고
    • Guidelines for the nomenclature of the human heat shock proteins
    • 10.1007/s12192-008-0068-7 18663603
    • Kampinga H.H. Hageman J. Vos M.J. Kubota H. Tanguay R.M. Bruford E.A. et al. 2009. Guidelines for the nomenclature of the human heat shock proteins. Cell Stress Chaperones, 14 (1): 105-111. 10.1007/s12192-008-0068-7 18663603
    • (2009) Cell Stress Chaperones , vol.14 , Issue.1 , pp. 105-111
    • Kampinga, H.H.1    Hageman, J.2    Vos, M.J.3    Kubota, H.4    Tanguay, R.M.5    Bruford, E.A.6
  • 21
    • 0024270042 scopus 로고
    • A rat testis-specific hsp70 gene-related transcript is coded by a novel gene from the hsp70 multigene family
    • 3247810
    • Krawczyk Z. Wisniewski J. Biesiada E. 1988. A rat testis-specific hsp70 gene-related transcript is coded by a novel gene from the hsp70 multigene family. Acta Biochim. Pol. 35 (4): 377-385. 3247810
    • (1988) Acta Biochim. Pol. , vol.35 , Issue.4 , pp. 377-385
    • Krawczyk, Z.1    Wisniewski, J.2    Biesiada, E.3
  • 22
    • 61849152933 scopus 로고    scopus 로고
    • Many facets of bortezomib resistance/susceptibility
    • 10.1182/blood-2008-07-167767 18779399
    • Kumar S. Rajkumar S.V. 2008. Many facets of bortezomib resistance/susceptibility. Blood, 112 (6): 2177-2178. 10.1182/blood-2008-07- 167767 18779399
    • (2008) Blood , vol.112 , Issue.6 , pp. 2177-2178
    • Kumar, S.1    Rajkumar, S.V.2
  • 23
    • 29244470510 scopus 로고    scopus 로고
    • Bortezomib inhibits PKR-like endoplasmic reticulum (ER) kinase and induces apoptosis via ER stress in human pancreatic cancer cells
    • 10.1158/0008-5472.CAN-05-2394 16357160
    • Nawrocki S.T. Carew J.S. Dunner K. Jr Boise L.H. Chiao P.J. Huang P. et al. 2005. Bortezomib inhibits PKR-like endoplasmic reticulum (ER) kinase and induces apoptosis via ER stress in human pancreatic cancer cells. Cancer Res. 65 (24): 11510-11519. 10.1158/0008-5472.CAN-05-2394 16357160
    • (2005) Cancer Res. , vol.65 , Issue.24 , pp. 11510-11519
    • Nawrocki, S.T.1    Carew, J.S.2    Dunner Jr., K.3    Boise, L.H.4    Chiao, P.J.5    Huang, P.6
  • 24
    • 33646857461 scopus 로고    scopus 로고
    • Over-expression of 70-kDa heat shock protein confers protection against monochloramine-induced gastric mucosal cell injury
    • 10.1016/j.lfs.2006.01.013 16492383
    • Oyake J. Otaka M. Matsuhashi T. Jin M. Odashima M. Komatsu K. et al. 2006. Over-expression of 70-kDa heat shock protein confers protection against monochloramine-induced gastric mucosal cell injury. Life Sci. 79 (3): 300-305. 10.1016/j.lfs.2006.01.013 16492383
    • (2006) Life Sci. , vol.79 , Issue.3 , pp. 300-305
    • Oyake, J.1    Otaka, M.2    Matsuhashi, T.3    Jin, M.4    Odashima, M.5    Komatsu, K.6
  • 25
    • 0021767876 scopus 로고
    • Hsp70 accelerates the recovery of nucleolar morphology after heat shock
    • 6441707
    • Pelham H.R. 1984. Hsp70 accelerates the recovery of nucleolar morphology after heat shock. EMBO J. 3 (13): 3095-3100. 6441707
    • (1984) EMBO J , vol.3 , Issue.13 , pp. 3095-3100
    • Pelham, H.R.1
  • 26
    • 33947591338 scopus 로고    scopus 로고
    • The structural and functional analysis of the human HSPA2 gene promoter region
    • 17369882
    • Pigłowski W. Nowak R. Krawczyk Z. Scieglińska D. 2007. The structural and functional analysis of the human HSPA2 gene promoter region. Acta Biochim. Pol. 54 (1): 99-106. 17369882
    • (2007) Acta Biochim. Pol. , vol.54 , Issue.1 , pp. 99-106
    • Pigłowski, W.1    Nowak, R.2    Krawczyk, Z.3    Scieglińska, D.4
  • 27
    • 14644435819 scopus 로고    scopus 로고
    • Rohde M. Daugaard M. Jensen M.H. Helin K. Nylandsted J. Jttelä M. Members of the heat-shock protein 70 family promote cancer cell growth by distinct mechanisms. (5): 570 - 582. 10.1101/gad.305405 15741319
    • Rohde M. Daugaard M. Jensen M.H. Helin K. Nylandsted J. Jttelä M. 2005. Members of the heat-shock protein 70 family promote cancer cell growth by distinct mechanisms. Genes Dev. 19 (5): 570 - 582. 10.1101/gad.305405 15741319
    • (2005) Genes Dev. , vol.19
  • 28
    • 57349152434 scopus 로고    scopus 로고
    • Bortezomib-induced survival signals and genes in human proximal tubular cells
    • 10.1124/jpet.108.142604 18776064
    • Sarközi R. Perco P. Hochegger K. Enrich J. Wiesinger M. Pirklbauer M. et al. 2008. Bortezomib-induced survival signals and genes in human proximal tubular cells. J. Pharmacol. Exp. Ther. 327 (3): 645-656. 10.1124/jpet.108. 142604 18776064
    • (2008) J. Pharmacol. Exp. Ther. , vol.327 , Issue.3 , pp. 645-656
    • Sarközi, R.1    Perco, P.2    Hochegger, K.3    Enrich, J.4    Wiesinger, M.5    Pirklbauer, M.6
  • 30
    • 79956219069 scopus 로고    scopus 로고
    • Differential expression of HSPA1 and HSPA2 proteins in human tissues; Tissue microarray-based immunohistochemical study
    • 10.1007/s00418-011-0791-5 21373891
    • Scieglinska D. Piglowski W. Czekan M. Mazurek A. Krawczyk Z. 2011. Differential expression of HSPA1 and HSPA2 proteins in human tissues; tissue microarray-based immunohistochemical study. Histochem. Cell Biol. 135 (4): 337-350. 10.1007/s00418-011-0791-5 21373891
    • (2011) Histochem. Cell Biol. , vol.135 , Issue.4 , pp. 337-350
    • Scieglinska, D.1    Piglowski, W.2    Czekan, M.3    Mazurek, A.4    Krawczyk, Z.5
  • 31
    • 33745169658 scopus 로고    scopus 로고
    • Gene expression analysis of B-lymphoma cells resistant and sensitive to bortezomib
    • 10.1111/j.1365-2141.2006.06132.x 16846475
    • Shringarpure R. Catley L. Bhole D. Burger R. Podar K. Tai Y.T. et al. 2006. Gene expression analysis of B-lymphoma cells resistant and sensitive to bortezomib. Br. J. Haematol. 134 (2): 145-156. 10.1111/j.1365-2141.2006.06132.x 16846475
    • (2006) Br. J. Haematol. , vol.134 , Issue.2 , pp. 145-156
    • Shringarpure, R.1    Catley, L.2    Bhole, D.3    Burger, R.4    Podar, K.5    Tai, Y.T.6
  • 32
    • 0023921692 scopus 로고
    • Identification and sequence analysis of a new member of the mouse HSP70 gene family and characterization of its unique cellular and developmental pattern of expression in the male germ line
    • 3405224
    • Zakeri Z.F. Wolgemuth D.J. Hunt C.R. 1988. Identification and sequence analysis of a new member of the mouse HSP70 gene family and characterization of its unique cellular and developmental pattern of expression in the male germ line. Mol. Cell. Biol. 8 (7): 2925-2932. 3405224
    • (1988) Mol. Cell. Biol. , vol.8 , Issue.7 , pp. 2925-2932
    • Zakeri, Z.F.1    Wolgemuth, D.J.2    Hunt, C.R.3
  • 33
    • 0030864750 scopus 로고    scopus 로고
    • HSP70-2 is required for CDC2 kinase activity in meiosis i of mouse spermatocytes
    • 9247342
    • Zhu D. Dix D.J. Eddy E.M. 1997. HSP70-2 is required for CDC2 kinase activity in meiosis I of mouse spermatocytes. Development, 124 (15): 3007-3014. 9247342
    • (1997) Development , vol.124 , Issue.15 , pp. 3007-3014
    • Zhu, D.1    Dix, D.J.2    Eddy, E.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.