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Volumn 2, Issue 1, 2011, Pages

Beyond reduction of atherosclerosis: PON2 provides apoptosis resistance and stabilizes tumor cells

Author keywords

Apoptosis; CHOP; Endoplasmic reticulum stress; Mitochondria; Oxidative stress; Paraoxonase

Indexed keywords

ARYLDIALKYLPHOSPHATASE 2; CARDIOLIPIN; CASPASE; CYTOCHROME C; DACTINOMYCIN; DOXORUBICIN; IMATINIB; STAUROSPORINE; STRESS ACTIVATED PROTEIN KINASE; SUPEROXIDE; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND; ARYLDIALKYLPHOSPHATASE; PON2 PROTEIN, HUMAN;

EID: 79251528324     PISSN: None     EISSN: 20414889     Source Type: Journal    
DOI: 10.1038/cddis.2010.91     Document Type: Article
Times cited : (77)

References (40)
  • 1
    • 33644858343 scopus 로고    scopus 로고
    • The unfolded protein response: A stress signaling pathway critical for health and disease
    • PII 0000611420060124100018
    • Zhang K, Kaufman RJ. The unfolded protein response: a stress signaling pathway critical for health and disease. Neurology 2006; 66 (2 Suppl 1): S102-S109. (Pubitemid 43739994)
    • (2006) Neurology , vol.66 , Issue.2 SUPPL. 1
    • Zhang, K.1    Kaufman, R.J.2
  • 2
    • 10344222124 scopus 로고    scopus 로고
    • The role of the unfolded protein response in tumour development: Friend or foe?
    • DOI 10.1038/nrc1505
    • Ma Y, Hendershot LM. The role of the unfolded protein response in tumour development: friend or foe? Nat Rev Cancer 2004; 4: 966-977. (Pubitemid 39626220)
    • (2004) Nature Reviews Cancer , vol.4 , Issue.12 , pp. 966-977
    • Ma, Y.1    Hendershot, L.M.2
  • 3
    • 1842843855 scopus 로고    scopus 로고
    • Roles of CHOP/GADD153 in endoplasmic reticulum stress
    • DOI 10.1038/sj.cdd.4401373
    • Oyadomari S, Mori M. Roles of CHOP/GADD153 in endoplasmic reticulum stress. Cell Death Differ 2004; 11: 381-389. (Pubitemid 38489416)
    • (2004) Cell Death and Differentiation , vol.11 , Issue.4 , pp. 381-389
    • Oyadomari, S.1    Mori, M.2
  • 4
    • 55849096988 scopus 로고    scopus 로고
    • Chop deletion reduces oxidative stress, improves beta cell function, and promotes cell survival in multiple mouse models of diabetes
    • Song B, Scheuner D, Ron D, Pennathur S, Kaufman RJ. Chop deletion reduces oxidative stress, improves beta cell function, and promotes cell survival in multiple mouse models of diabetes. J Clin Invest 2008; 118: 3378-3389.
    • (2008) J Clin Invest , vol.118 , pp. 3378-3389
    • Song, B.1    Scheuner, D.2    Ron, D.3    Pennathur, S.4    Kaufman, R.J.5
  • 5
    • 34247490186 scopus 로고    scopus 로고
    • Mitochondria, oxidative stress and cell death
    • DOI 10.1007/s10495-007-0756-2, Special Issue on Mitochondria in Apoptosis
    • Ott M, Gogvadze V, Orrenius S, Zhivotovsky B. Mitochondria, oxidative stress and cell death. Apoptosis 2007; 12: 913-922. (Pubitemid 46653300)
    • (2007) Apoptosis , vol.12 , Issue.5 , pp. 913-922
    • Ott, M.1    Gogvadze, V.2    Orrenius, S.3    Zhivotovsky, B.4
  • 6
    • 34247213490 scopus 로고    scopus 로고
    • Paraoxonase-2 reduces oxidative stress in vascular cells and decreases endoplasmic reticulum stress-induced caspase activation
    • DOI 10.1161/CIRCULATIONAHA.106.681700
    • Horke S, Witte I, Wilgenbus P, Kruger M, Strand D, Forstermann U. Paraoxonase-2 reduces oxidative stress in vascular cells and decreases endoplasmic reticulum stressinduced caspase activation. Circulation 2007; 115: 2055-2064. (Pubitemid 46625957)
    • (2007) Circulation , vol.115 , Issue.15 , pp. 2055-2064
    • Horke, S.1    Witte, I.2    Wilgenbus, P.3    Kruger, M.4    Strand, D.5    Forstermann, U.6
  • 7
    • 0035976903 scopus 로고    scopus 로고
    • Paraoxonase-2 is a ubiquitously expressed protein with antioxidant properties and is capable of preventing cell-mediated oxidative modification of low density lipoprotein
    • Ng CJ, Wadleigh DJ, Gangopadhyay A, Hama S, Grijalva VR, Navab M et al. Paraoxonase-2 is a ubiquitously expressed protein with antioxidant properties and is capable of preventing cell-mediated oxidative modification of low density lipoprotein. J Biol Chem 2001; 276: 44444-44449.
    • (2001) J Biol Chem , vol.276 , pp. 44444-44449
    • Ng, C.J.1    Wadleigh, D.J.2    Gangopadhyay, A.3    Hama, S.4    Grijalva, V.R.5    Navab, M.6
  • 8
    • 34547120231 scopus 로고    scopus 로고
    • Paraoxonases are associated with intestinal inflammatory diseases and intracellularly localized to the endoplasmic reticulum
    • DOI 10.1016/j.freeradbiomed.2007.05.003, PII S0891584907003176
    • Rothem L, Hartman C, Dahan A, Lachter J, Eliakim R, Shamir R. Paraoxonases are associated with intestinal inflammatory diseases and intracellularly localized to the endoplasmic reticulum. Free Radic Biol Med 2007; 43: 730-739. (Pubitemid 47102121)
    • (2007) Free Radical Biology and Medicine , vol.43 , Issue.5 , pp. 730-739
    • Rothem, L.1    Hartman, C.2    Dahan, A.3    Lachter, J.4    Eliakim, R.5    Shamir, R.6
  • 9
    • 21244491480 scopus 로고    scopus 로고
    • Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities
    • DOI 10.1194/jlr.M400511-JLR200
    • Draganov DI, Teiber JF, Speelman A, Osawa Y, Sunahara R, La Du BN. Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities. J Lipid Res 2005; 46: 1239-1247. (Pubitemid 43109838)
    • (2005) Journal of Lipid Research , vol.46 , Issue.6 , pp. 1239-1247
    • Draganov, D.I.1    Teiber, J.F.2    Speelman, A.3    Osawa, Y.4    Sunahara, R.5    La Du, B.N.6
  • 11
    • 61449118867 scopus 로고    scopus 로고
    • The paraoxonases: Role in human diseases and methodological difficulties in measurement
    • Camps J, Marsillach J, Joven J. The paraoxonases: role in human diseases and methodological difficulties in measurement. Crit Rev Clin Lab Sci 2009; 46: 83-106.
    • (2009) Crit Rev Clin Lab Sci , vol.46 , pp. 83-106
    • Camps, J.1    Marsillach, J.2    Joven, J.3
  • 13
    • 46249112510 scopus 로고    scopus 로고
    • Dominant role of paraoxonases in inactivation of the Pseudomonas aeruginosa quorum-sensing signal N-(3- oxododecanoyl)-L-homoserine lactone
    • Teiber JF, Horke S, Haines DC, Chowdhary PK, Xiao J, Kramer GL et al. Dominant role of paraoxonases in inactivation of the Pseudomonas aeruginosa quorum-sensing signal N-(3- oxododecanoyl)-L-homoserine lactone. Infect Immun 2008; 76: 2512-2519.
    • (2008) Infect Immun , vol.76 , pp. 2512-2519
    • Teiber, J.F.1    Horke, S.2    Haines, D.C.3    Chowdhary, P.K.4    Xiao, J.5    Kramer, G.L.6
  • 14
    • 76549114781 scopus 로고    scopus 로고
    • Paraoxonase 2 is down-regulated by the Pseudomonas aeruginosa quorumsensing signal N-(3- oxododecanoyl)-L-homoserine lactone and attenuates oxidative stress induced by pyocyanin
    • Horke S, Witte I, Altenhofer S, Wilgenbus P, Goldeck M, Forstermann U et al. Paraoxonase 2 is down-regulated by the Pseudomonas aeruginosa quorumsensing signal N-(3- oxododecanoyl)-L-homoserine lactone and attenuates oxidative stress induced by pyocyanin. Biochem J 2010; 426: 73-83.
    • (2010) Biochem J , vol.426 , pp. 73-83
    • Horke, S.1    Witte, I.2    Altenhofer, S.3    Wilgenbus, P.4    Goldeck, M.5    Forstermann, U.6
  • 15
    • 68449096849 scopus 로고    scopus 로고
    • The roles of PON1 and PON2 in cardiovascular disease and innate immunity
    • Shih DM, Lusis AJ. The roles of PON1 and PON2 in cardiovascular disease and innate immunity. Curr Opin Lipidol 2009; 20: 288-292.
    • (2009) Curr Opin Lipidol , vol.20 , pp. 288-292
    • Shih, D.M.1    Lusis, A.J.2
  • 19
    • 5344238178 scopus 로고    scopus 로고
    • Paraoxonases 1, 2, and 3, oxidative stress, and macrophage foam cell formation during atherosclerosis development
    • DOI 10.1016/j.freeradbiomed.2004.06.030, PII S0891584904005246
    • Aviram M, Rosenblat M. Paraoxonases 1,2, and 3, oxidative stress, and macrophage foam cell formation during atherosclerosis development. Free Radic Biol Med 2004; 37: 1304-1316. (Pubitemid 39349234)
    • (2004) Free Radical Biology and Medicine , vol.37 , Issue.9 , pp. 1304-1316
    • Aviram, M.1    Rosenblat, M.2
  • 21
    • 77950937747 scopus 로고    scopus 로고
    • Epigenetic inactivation of the placentally imprinted tumor suppressor gene TFPI2 in prostate carcinoma
    • Ribarska T, Ingenwerth M, Goering W, Engers R, Schulz WA. Epigenetic inactivation of the placentally imprinted tumor suppressor gene TFPI2 in prostate carcinoma. Cancer Genomics Proteomics 2010; 7: 51-60.
    • (2010) Cancer Genomics Proteomics , vol.7 , pp. 51-60
    • Ribarska, T.1    Ingenwerth, M.2    Goering, W.3    Engers, R.4    Schulz, W.A.5
  • 24
    • 77949879862 scopus 로고    scopus 로고
    • Gene expression classifiers for relapse-free survival and minimal residual disease improve risk classification and outcome prediction in pediatric B-precursor acute lymphoblastic leukemia
    • Kang H, Chen IM, Wilson CS, Bedrick EJ, Harvey RC, Atlas SR et al. Gene expression classifiers for relapse-free survival and minimal residual disease improve risk classification and outcome prediction in pediatric B-precursor acute lymphoblastic leukemia. Blood 2010; 115: 1394-1405.
    • (2010) Blood , vol.115 , pp. 1394-1405
    • Kang, H.1    Chen, I.M.2    Wilson, C.S.3    Bedrick, E.J.4    Harvey, R.C.5    Atlas, S.R.6
  • 26
    • 58949085858 scopus 로고    scopus 로고
    • Protective effect of paraoxonase-2 against endoplasmic reticulum stress-induced apoptosis is lost upon disturbance of calcium homoeostasis
    • Horke S, Witte I, Wilgenbus P, Altenhofer S, Kruger M, Li H et al. Protective effect of paraoxonase-2 against endoplasmic reticulum stress-induced apoptosis is lost upon disturbance of calcium homoeostasis. Biochem J 2008; 416: 395-405.
    • (2008) Biochem J , vol.416 , pp. 395-405
    • Horke, S.1    Witte, I.2    Wilgenbus, P.3    Altenhofer, S.4    Kruger, M.5    Li, H.6
  • 27
    • 77955300136 scopus 로고    scopus 로고
    • One enzyme, two functions: PON2 prevents mitochondrial superoxide formation and apoptosis independent from its lactonase activity
    • Altenhofer S, Witte I, Teiber JF, Wilgenbus P, Pautz A, Li H et al. One enzyme, two functions: PON2 prevents mitochondrial superoxide formation and apoptosis independent from its lactonase activity. J Biol Chem 2010; 285: 24398-24403.
    • (2010) J Biol Chem , vol.285 , pp. 24398-24403
    • Altenhofer, S.1    Witte, I.2    Teiber, J.F.3    Wilgenbus, P.4    Pautz, A.5    Li, H.6
  • 28
    • 78650869947 scopus 로고    scopus 로고
    • Paraoxonase 2 deficiency alters mitochondrial function and exacerbates the development of atherosclerosis
    • doi:10.1089/ars.2010.3430
    • Devarajan A, Bourquard N, Hama S, Navab M, Grijalva V, Morvardi S et al. Paraoxonase 2 deficiency alters mitochondrial function and exacerbates the development of atherosclerosis. Antioxid Redox Signal 2010, doi:10.1089/ars. 2010.3430.
    • (2010) Antioxid Redox Signal
    • Devarajan, A.1    Bourquard, N.2    Hama, S.3    Navab, M.4    Grijalva, V.5    Morvardi, S.6
  • 29
    • 35848957485 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and oxidative stress: A vicious cycle or a double-edged sword?
    • DOI 10.1089/ars.2007.1782
    • Malhotra JD, Kaufman RJ. Endoplasmic reticulum stress and oxidative stress: a vicious cycle or a double-edged sword? Antioxid Redox Signal 2007; 9: 2277-2293. (Pubitemid 350059010)
    • (2007) Antioxidants and Redox Signaling , vol.9 , Issue.12 , pp. 2277-2293
    • Malhotra, J.D.1    Kaufman, R.J.2
  • 30
    • 33644862368 scopus 로고    scopus 로고
    • JNK signaling pathway is a key modulator in cell death mediated by reactive oxygen and nitrogen species
    • Shen HM, Liu ZG. JNK signaling pathway is a key modulator in cell death mediated by reactive oxygen and nitrogen species. Free Radic Biol Med 2006; 40: 928-939.
    • (2006) Free Radic Biol Med , vol.40 , pp. 928-939
    • Shen, H.M.1    Liu, Z.G.2
  • 32
    • 31444449462 scopus 로고    scopus 로고
    • Role of the unfolded protein response in cell death
    • DOI 10.1007/s10495-005-3088-0
    • Kim R, Emi M, Tanabe K, Murakami S. Role of the unfolded protein response in cell death. Apoptosis 2006; 11: 5-13. (Pubitemid 43151639)
    • (2006) Apoptosis , vol.11 , Issue.1 , pp. 5-13
    • Kim, R.1    Emi, M.2    Tanabe, K.3    Murakami, S.4
  • 33
    • 33751093349 scopus 로고    scopus 로고
    • Adenovirus mediated expression of human paraoxonase 2 protects against the development of atherosclerosis in apolipoprotein E-deficient mice
    • DOI 10.1016/j.ymgme.2006.07.004, PII S1096719206002526
    • Ng CJ, Hama SY, Bourquard N, Navab M, Reddy ST. Adenovirus mediated expression of human paraoxonase 2 protects against the development of atherosclerosis in apolipoprotein E-deficient mice. Mol Genet Metab 2006; 89: 368-373. (Pubitemid 44767734)
    • (2006) Molecular Genetics and Metabolism , vol.89 , Issue.4 , pp. 368-373
    • Ng, C.J.1    Hama, S.Y.2    Bourquard, N.3    Navab, M.4    Reddy, S.T.5
  • 34
    • 65349135431 scopus 로고    scopus 로고
    • Reduced apoptosis and plaque necrosis in advanced atherosclerotic lesions of Apoe-/- and Ldlr-/- mice lacking CHOP
    • Thorp E, Li G, Seimon TA, Kuriakose G, Ron D, Tabas I. Reduced apoptosis and plaque necrosis in advanced atherosclerotic lesions of Apoe-/- and Ldlr-/- mice lacking CHOP. Cell Metab 2009; 9: 474-481.
    • (2009) Cell Metab , vol.9 , pp. 474-481
    • Thorp, E.1    Li, G.2    Seimon, T.A.3    Kuriakose, G.4    Ron, D.5    Tabas, I.6
  • 36
    • 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 et al. Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science 2000; 287: 664-666. (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
  • 37
    • 68949196897 scopus 로고    scopus 로고
    • Oxidative folding: Cellular strategies for dealing with the resultant equimolar production of reactive oxygen species
    • Shimizu Y, Hendershot LM. Oxidative folding: cellular strategies for dealing with the resultant equimolar production of reactive oxygen species. Antioxid Redox Signal 2009; 11: 2317-2331.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 2317-2331
    • Shimizu, Y.1    Hendershot, L.M.2
  • 38
    • 70449730482 scopus 로고    scopus 로고
    • Urokinase activates macrophage PON2 gene transcription via the PI3K/ROS/MEK/SREBP-2 signalling cascade mediated by the PDGFR-beta
    • Fuhrman B, Gantman A, Khateeb J, Volkova N, Horke S, Kiyan J et al. Urokinase activates macrophage PON2 gene transcription via the PI3K/ROS/MEK/SREBP-2 signalling cascade mediated by the PDGFR-beta. Cardiovasc Res 2009; 84: 145-154.
    • (2009) Cardiovasc Res , vol.84 , pp. 145-154
    • Fuhrman, B.1    Gantman, A.2    Khateeb, J.3    Volkova, N.4    Horke, S.5    Kiyan, J.6
  • 40
    • 0037066741 scopus 로고    scopus 로고
    • The luminal domain of ATF6 senses endoplasmic reticulum (ER) stress and causes translocation of ATF6 from the er to the Golgi
    • DOI 10.1074/jbc.M110636200
    • Chen X, Shen J, Prywes R. The luminal domain of ATF6 senses endoplasmic reticulum (ER) stress and causes translocation of ATF6 from the ER to the Golgi. J Biol Chem 2002; 277: 13045-13052. (Pubitemid 34952673)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.15 , pp. 13045-13052
    • Chen, X.1    Shen, J.2    Prywes, R.3


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