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Volumn 42, Issue 1, 2013, Pages 188-196

The secreted protein acidic and rich in cysteine (SPARC) induces endoplasmic reticulum stress leading to autophagy-mediated apoptosis in neuroblastoma

Author keywords

Apoptosis; Autophagy; Endoplasmic reticulum stress; Neuroblastoma; Secreted protein acidic and rich in cysteine

Indexed keywords

CASPASE 3; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 153; OSTEONECTIN; PLASMID VECTOR; PROTEIN KINASE R; STRESS ACTIVATED PROTEIN KINASE;

EID: 84873658356     PISSN: 10196439     EISSN: 17912423     Source Type: Journal    
DOI: 10.3892/ijo.2012.1678     Document Type: Article
Times cited : (32)

References (34)
  • 2
    • 77956408842 scopus 로고    scopus 로고
    • Outcomes for children and adolescents with cancer: Challenges for the twenty-first century
    • Smith MA, Seibel NL, Altekruse SF, et al: Outcomes for children and adolescents with cancer: challenges for the twenty-first century. J Clin Oncol 28: 2625-2634, 2010.
    • (2010) J Clin Oncol , vol.28 , pp. 2625-2634
    • Smith, M.A.1    Seibel, N.L.2    Altekruse, S.F.3
  • 4
    • 0038444707 scopus 로고    scopus 로고
    • Apoptosis pathways in neuroblastoma therapy
    • DOI 10.1016/S0304-3835(03)00091-0
    • Fulda S and Debatin KM: Apoptosis pathways in neuroblastoma therapy. Cancer Lett 197: 131-135, 2003. (Pubitemid 36860002)
    • (2003) Cancer Letters , vol.197 , Issue.1-2 , pp. 131-135
    • Fulda, S.1    Debatin, K.-M.2
  • 5
    • 72449187453 scopus 로고    scopus 로고
    • SPARC: A matricellular regulator of tumorigenesis
    • Arnold SA and Brekken RA: SPARC: a matricellular regulator of tumorigenesis. J Cell Commun Signal 3: 255-273, 2009.
    • (2009) J Cell Commun Signal , vol.3 , pp. 255-273
    • Arnold, S.A.1    Brekken, R.A.2
  • 6
    • 0029992948 scopus 로고    scopus 로고
    • SPARC, an extracellular matrix protein with tumor-suppressing activity in human ovarian epithelial cells
    • Mok SC, Chan WY, Wong KK, Muto MG and Berkowitz RS: SPARC, an extracellular matrix protein with tumor-suppressing activity in human ovarian epithelial cells. Oncogene 12: 1895-1901, 1996. (Pubitemid 26154661)
    • (1996) Oncogene , vol.12 , Issue.9 , pp. 1895-1901
    • Mok, S.C.1    Chan, W.Y.2    Wong, K.K.3    Muto, M.G.4    Berkowitz, R.S.5
  • 7
    • 0042284883 scopus 로고    scopus 로고
    • SPARC/osteonectin is a frequent target for aberrant methylation in pancreatic adenocarcinoma and a mediator of tumor-stromal interactions
    • DOI 10.1038/sj.onc.1206807
    • Sato N, Fukushima N, Maehara N, et al: SPARC/osteonectin is a frequent target for aberrant methylation in pancreatic adenocarcinoma and a mediator of tumor-stromal interactions. Oncogene 22: 5021-5030, 2003. (Pubitemid 37026400)
    • (2003) Oncogene , vol.22 , Issue.32 , pp. 5021-5030
    • Sato, N.1    Fukushima, N.2    Maehara, N.3    Matsubayashi, H.4    Koopmann, J.5    Su, G.H.6    Hruban, R.H.7    Goggins, M.8
  • 8
    • 33645461015 scopus 로고    scopus 로고
    • Discovery of novel methylation biomarkers in cervical carcinoma by global demethylation and microarray analysis
    • Sova P, Feng Q, Geiss G, et al: Discovery of novel methylation biomarkers in cervical carcinoma by global demethylation and microarray analysis. Cancer Epidemiol Biomarkers Prev 15: 114-123, 2006.
    • (2006) Cancer Epidemiol Biomarkers Prev , vol.15 , pp. 114-123
    • Sova, P.1    Feng, Q.2    Geiss, G.3
  • 9
    • 68549109512 scopus 로고    scopus 로고
    • Effects of tetrandrine plus radiation on neuroblastoma cells
    • Chen Y, Chen JC and Tseng SH: Effects of tetrandrine plus radiation on neuroblastoma cells. Anticancer Res 29: 3163-3171, 2009.
    • (2009) Anticancer Res , vol.29 , pp. 3163-3171
    • Chen, Y.1    Chen, J.C.2    Tseng, S.H.3
  • 10
    • 0034100255 scopus 로고    scopus 로고
    • The role of p53 in gemcitabine-mediated cytotoxicity and radiosensitization
    • Chen M, Hough AM and Lawrence TS: The role of p53 in gemcitabine-mediated cytotoxicity and radiosensitization. Cancer Chemother Pharmacol 45: 369-374, 2000. (Pubitemid 30217160)
    • (2000) Cancer Chemotherapy and Pharmacology , vol.45 , Issue.5 , pp. 369-374
    • Chen, M.1    Hough, A.M.2    Lawrence, T.S.3
  • 12
    • 0026149822 scopus 로고
    • Endoscopic operations spare the patient. Rapid rehabilitation dispensing with large incisions removal of appendix gallbladder and esophagus
    • (In German)
    • Heck A: [Endoscopic operations spare the patient. Rapid rehabilitation, dispensing with large incisions, removal of appendix, gallbladder and esophagus]. Krankenpfl J 29: 148-149, 1991 (In German).
    • (1991) Krankenpfl J , vol.29 , pp. 148-149
    • Heck, A.1
  • 13
    • 80053241158 scopus 로고    scopus 로고
    • SPARC mediates Src-induced disruption of actin cytoskeleton via inactivation of small GTPases Rho-Rac-Cdc42
    • Bhoopathi P, Gondi CS, Gujrati M, Dinh DH and Lakka SS: SPARC mediates Src-induced disruption of actin cytoskeleton via inactivation of small GTPases Rho-Rac-Cdc42. Cell Signal 23: 1978-1987, 2011.
    • (2011) Cell Signal , vol.23 , pp. 1978-1987
    • Bhoopathi, P.1    Gondi, C.S.2    Gujrati, M.3    Dinh, D.H.4    Lakka, S.S.5
  • 14
    • 77956668302 scopus 로고    scopus 로고
    • Cathepsin B facilitates autophagy mediated apoptosis in SPARC overexpressed primitive neuroectodermal tumor cells
    • Bhoopathi P, Chetty C, Gujrati M, Dinh DH, Rao JS and Lakka SS: Cathepsin B facilitates autophagy mediated apoptosis in SPARC overexpressed primitive neuroectodermal tumor cells. Cell Death Differ 17: 1529-1539, 2010.
    • (2010) Cell Death Differ , vol.17 , pp. 1529-1539
    • Bhoopathi, P.1    Chetty, C.2    Gujrati, M.3    Dinh, D.H.4    Rao, J.S.5    Lakka, S.S.6
  • 15
    • 34548037901 scopus 로고    scopus 로고
    • Connecting endoplasmic reticulum stress to autophagy by unfolded protein response and calcium
    • DOI 10.1038/sj.cdd.4402200, PII 4402200
    • Hoyer-Hansen M and Jaattela M: Connecting endoplasmic reticulum stress to autophagy by unfolded protein response and calcium. Cell Death Differ 14: 1576-1582, 2007. (Pubitemid 47278843)
    • (2007) Cell Death and Differentiation , vol.14 , Issue.9 , pp. 1576-1582
    • Hoyer-Hansen, M.1    Jaattela, M.2
  • 17
    • 76349122661 scopus 로고    scopus 로고
    • The role of MMP-9 in the anti-angiogenic effect of secreted protein acidic and rich in cysteine
    • Bhoopathi P, Chetty C, Gujrati M, Dinh DH, Rao JS and Lakka SS: The role of MMP-9 in the anti-angiogenic effect of secreted protein acidic and rich in cysteine. Br J Cancer 102: 530-540, 2010.
    • (2010) Br J Cancer , vol.102 , pp. 530-540
    • Bhoopathi, P.1    Chetty, C.2    Gujrati, M.3    Dinh, D.H.4    Rao, J.S.5    Lakka, S.S.6
  • 19
    • 38349175935 scopus 로고    scopus 로고
    • Blockade of tumor growth due to matrix metalloproteinase-9 inhibition is mediated by sequential activation of beta1-integrin, ERK, and NF-kappaB
    • Bhoopathi P, Chetty C, Kunigal S, Vanamala SK, Rao JS and Lakka SS: Blockade of tumor growth due to matrix metalloproteinase-9 inhibition is mediated by sequential activation of beta1-integrin, ERK, and NF-kappaB. J Biol Chem 283: 1545-1552, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 1545-1552
    • Bhoopathi, P.1    Chetty, C.2    Kunigal, S.3    Vanamala, S.K.4    Rao, J.S.5    Lakka, S.S.6
  • 20
    • 49649093187 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase 3 suppresses tumor angiogenesis in matrix metalloproteinase 2-down-regulated lung cancer
    • Chetty C, Lakka SS, Bhoopathi P, Kunigal S, Geiss R and Rao JS: Tissue inhibitor of metalloproteinase 3 suppresses tumor angiogenesis in matrix metalloproteinase 2-down-regulated lung cancer. Cancer Res 68: 4736-4745, 2008.
    • (2008) Cancer Res , vol.68 , pp. 4736-4745
    • Chetty, C.1    Lakka, S.S.2    Bhoopathi, P.3    Kunigal, S.4    Geiss, R.5    Rao, J.S.6
  • 23
    • 16844387124 scopus 로고    scopus 로고
    • Role of JNK activation in apoptosis: A double-edged sword
    • DOI 10.1038/sj.cr.7290262
    • Liu J and Lin A: Role of JNK activation in apoptosis: a double-edged sword. Cell Res 15: 36-42, 2005. (Pubitemid 41653963)
    • (2005) Cell Research , vol.15 , Issue.1 , pp. 36-42
    • Liu, J.1    Lin, A.2
  • 24
    • 84856111924 scopus 로고    scopus 로고
    • The unfolded protein response: Controlling cell fate decisions under ER stress and beyond
    • Hetz C: The unfolded protein response: controlling cell fate decisions under ER stress and beyond. Nat Rev Mol Cell Biol 13: 89-102, 2012.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 89-102
    • Hetz, C.1
  • 25
    • 45149106189 scopus 로고    scopus 로고
    • A prototypic matricellular protein in the tumor microenvironment - Where there's SPARC, there's fire
    • DOI 10.1002/jcb.21688
    • Clark CJ and Sage EH: A prototypic matricellular protein in the tumor microenvironment - where there's SPARC, there's fire. J Cell Biochem 104: 721-732, 2008. (Pubitemid 351830824)
    • (2008) Journal of Cellular Biochemistry , vol.104 , Issue.3 , pp. 721-732
    • Clark, C.J.1    Sage, E.H.2
  • 27
    • 84889271499 scopus 로고    scopus 로고
    • IFNγ sensitizes for apoptosis by upregulating caspase-8 expression through the Stat1 pathway
    • DOI 10.1038/sj/onc/1205255
    • Fulda S and Debatin KM: IFNgamma sensitizes for apoptosis by upregulating caspase-8 expression through the Stat1 pathway. Oncogene 21: 2295-2308, 2002. (Pubitemid 34407289)
    • (2002) Oncogene , vol.21 , Issue.15 , pp. 2295-2308
    • Fulda, S.1    Debatin, K.-M.2
  • 28
    • 38049155818 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress induces calcium-dependent permeability transition, mitochondrial outer membrane permeabilization and apoptosis
    • Deniaud A, Sharaf el Dein O, Maillier E, Poncet D, Kroemer G, Lemaire C and Brenner C: Endoplasmic reticulum stress induces calcium-dependent permeability transition, mitochondrial outer membrane permeabilization and apoptosis. Oncogene 27: 285-299, 2008.
    • (2008) Oncogene , vol.27 , pp. 285-299
    • Deniaud, A.1    Sharaf El Dein, O.2    Maillier, E.3    Poncet, D.4    Kroemer, G.5    Lemaire, C.6    Brenner, C.7
  • 30
    • 0034723235 scopus 로고    scopus 로고
    • Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1
    • DOI 10.1126/science.287.5453.664
    • Urano F, Wang X, Bertolotti A, Zhang Y, Chung P, Harding HP and Ron D: Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science 287: 664-666, 2000. (Pubitemid 30070916)
    • (2000) Science , vol.287 , Issue.5453 , pp. 664-666
    • Urano, F.1    Wang, X.2    Bertolotti, A.3    Zhang, Y.4    Chung, P.5    Harding, H.P.6    Ron, D.7
  • 31
    • 58449084895 scopus 로고    scopus 로고
    • Divergent effects of PERK and IRE1 signaling on cell viability
    • Lin JH, Li H, Zhang Y, Ron D and Walter P: Divergent effects of PERK and IRE1 signaling on cell viability. PLoS One 4: e4170, 2009.
    • (2009) PLoS One , vol.4
    • Lin, J.H.1    Li, H.2    Zhang, Y.3    Ron, D.4    Walter, P.5
  • 32
    • 0033782015 scopus 로고    scopus 로고
    • Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
    • Bertolotti A, Zhang Y, Hendershot LM, Harding HP and Ron D: Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Nat Cell Biol 2: 326-332, 2000.
    • (2000) Nat Cell Biol , vol.2 , pp. 326-332
    • Bertolotti, A.1    Zhang, Y.2    Hendershot, L.M.3    Harding, H.P.4    Ron, D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.