메뉴 건너뛰기




Volumn 12, Issue SUPPL. 2, 2010, Pages 141-148

Reactive oxygen species and uncoupling protein 2 in pancreatic β-cell function

Author keywords

Antioxidant; GSIS; Oxidative stress; ROS signalling; UCP2; cell

Indexed keywords

MITOCHONDRIAL PROTEIN; REACTIVE OXYGEN METABOLITE; UNCOUPLING PROTEIN 2;

EID: 77957304618     PISSN: 14628902     EISSN: 14631326     Source Type: Journal    
DOI: 10.1111/j.1463-1326.2010.01269.x     Document Type: Article
Times cited : (86)

References (90)
  • 1
    • 0037115158 scopus 로고    scopus 로고
    • Reactive oxygen species and cell signaling: respiratory burst in macrophage signaling.
    • Forman HJ, Torres M. Reactive oxygen species and cell signaling: respiratory burst in macrophage signaling. Am J Respir Crit Care Med 2002, 166:S4-S8..
    • (2002) Am J Respir Crit Care Med , vol.166
    • Forman, H.J.1    Torres, M.2
  • 2
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function.
    • Droge W. Free radicals in the physiological control of cell function. Physiol Rev 2002, 82:47-95..
    • (2002) Physiol Rev , vol.82
    • Droge, W.1
  • 3
    • 0032053707 scopus 로고    scopus 로고
    • Oxygen radicals and signaling.
    • Finkel T. Oxygen radicals and signaling. Curr Opin Cell Biol 1998, 10:248-253..
    • (1998) Curr Opin Cell Biol , vol.10
    • Finkel, T.1
  • 4
    • 33745631769 scopus 로고    scopus 로고
    • Cell signaling. H2O2, a necessary evil for cell signaling.
    • Rhee SG. Cell signaling. H2O2, a necessary evil for cell signaling. Science 2006, 312:1882-1883..
    • (2006) Science , vol.312
    • Rhee, S.G.1
  • 5
    • 34247217064 scopus 로고    scopus 로고
    • Measuring H2O2 produced in response to cell surface receptor activation.
    • Rhee SG. Measuring H2O2 produced in response to cell surface receptor activation. Nat Chem Biol 2007, 3:244-246..
    • (2007) Nat Chem Biol , vol.3
    • Rhee, S.G.1
  • 6
    • 33845667532 scopus 로고    scopus 로고
    • Quantification of basal and stimulated ROS levels as predictors of islet potency and function.
    • Armann B, Hanson MS, Hatch E, Steffen A, Fernandez LA. Quantification of basal and stimulated ROS levels as predictors of islet potency and function. Am J Transplant 2007, 7:38-47..
    • (2007) Am J Transplant , vol.7
    • Armann, B.1    Hanson, M.S.2    Hatch, E.3    Steffen, A.4    Fernandez, L.A.5
  • 7
    • 33747039288 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species are required for hypothalamic glucose sensing.
    • Leloup C, Magnan C, Benani A. Mitochondrial reactive oxygen species are required for hypothalamic glucose sensing. Diabetes 2006, 55:2084-2090..
    • (2006) Diabetes , vol.55
    • Leloup, C.1    Magnan, C.2    Benani, A.3
  • 8
    • 0032554611 scopus 로고    scopus 로고
    • Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation.
    • Denu JM, Tanner KG. Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation. Biochemistry 1998, 37:5633-5642..
    • (1998) Biochemistry , vol.37
    • Denu, J.M.1    Tanner, K.G.2
  • 9
    • 12744279326 scopus 로고    scopus 로고
    • Redox paradox: insulin action is facilitated by insulin-stimulated reactive oxygen species with multiple potential signaling targets.
    • Goldstein BJ, Mahadev K, Wu X. Redox paradox: insulin action is facilitated by insulin-stimulated reactive oxygen species with multiple potential signaling targets. Diabetes 2005, 54:311-321..
    • (2005) Diabetes , vol.54
    • Goldstein, B.J.1    Mahadev, K.2    Wu, X.3
  • 10
    • 62749103868 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species are obligatory signals for glucose-induced insulin secretion.
    • Leloup C, Tourrel-Cuzin C, Magnan C. Mitochondrial reactive oxygen species are obligatory signals for glucose-induced insulin secretion. Diabetes 2009, 58:673-681..
    • (2009) Diabetes , vol.58
    • Leloup, C.1    Tourrel-Cuzin, C.2    Magnan, C.3
  • 11
    • 0034607872 scopus 로고    scopus 로고
    • Nerve growth factor-induced neuronal differentiation requires generation of Rac1-regulated reactive oxygen species.
    • Suzukawa K, Miura K, Mitsushita J. Nerve growth factor-induced neuronal differentiation requires generation of Rac1-regulated reactive oxygen species. J Biol Chem 2000, 275:13175-13178..
    • (2000) J Biol Chem , vol.275
    • Suzukawa, K.1    Miura, K.2    Mitsushita, J.3
  • 13
    • 34347399043 scopus 로고    scopus 로고
    • Reactive oxygen species as a signal in glucose-stimulated insulin secretion.
    • Pi J, Bai Y, Zhang Q. Reactive oxygen species as a signal in glucose-stimulated insulin secretion. Diabetes 2007, 56:1783-1791..
    • (2007) Diabetes , vol.56
    • Pi, J.1    Bai, Y.2    Zhang, Q.3
  • 14
    • 0034650763 scopus 로고    scopus 로고
    • The uncoupling protein homologues: UCP1, UCP2, UCP3, StUCP and AtUCP.
    • Ricquier D, Bouillaud F. The uncoupling protein homologues: UCP1, UCP2, UCP3, StUCP and AtUCP. Biochem J 2000, 345:161-179..
    • (2000) Biochem J , vol.345
    • Ricquier, D.1    Bouillaud, F.2
  • 15
    • 0037039366 scopus 로고    scopus 로고
    • A significant portion of mitochondrial proton leak in intact thymocytes depends on expression of UCP2.
    • Krauss S, Zhang CY, Lowell BB. A significant portion of mitochondrial proton leak in intact thymocytes depends on expression of UCP2. Proc Natl Acad Sci U S A 2002, 99:118-122..
    • (2002) Proc Natl Acad Sci U S A , vol.99
    • Krauss, S.1    Zhang, C.Y.2    Lowell, B.B.3
  • 16
    • 0842306477 scopus 로고    scopus 로고
    • The biology of mitochondrial uncoupling proteins.
    • Rousset S, Alves-Guerra MC, Mozo J. The biology of mitochondrial uncoupling proteins. Diabetes 2004, 53((Suppl. 1)):S130-S135..
    • (2004) Diabetes , vol.53 , Issue.SUPPL. 1
    • Rousset, S.1    Alves-Guerra, M.C.2    Mozo, J.3
  • 17
    • 25144476923 scopus 로고    scopus 로고
    • Physiological functions of the mitochondrial uncoupling proteins UCP2 and UCP3.
    • Brand MD, Esteves TC. Physiological functions of the mitochondrial uncoupling proteins UCP2 and UCP3. Cell Metab 2005, 2:85-93..
    • (2005) Cell Metab , vol.2
    • Brand, M.D.1    Esteves, T.C.2
  • 18
  • 19
    • 4344716628 scopus 로고    scopus 로고
    • Mitochondrial catalase overexpression protects insulin-producing cells against toxicity of reactive oxygen species and proinflammatory cytokines.
    • Gurgul E, Lortz S, Tiedge M, Jorns A, Lenzen S. Mitochondrial catalase overexpression protects insulin-producing cells against toxicity of reactive oxygen species and proinflammatory cytokines. Diabetes 2004, 53:2271-2280..
    • (2004) Diabetes , vol.53
    • Gurgul, E.1    Lortz, S.2    Tiedge, M.3    Jorns, A.4    Lenzen, S.5
  • 20
    • 0030689041 scopus 로고    scopus 로고
    • Relation between antioxidant enzyme gene expression and antioxidative defense status of insulin-producing cells.
    • Tiedge M, Lortz S, Drinkgern J, Lenzen S. Relation between antioxidant enzyme gene expression and antioxidative defense status of insulin-producing cells. Diabetes 1997, 46:1733-1742..
    • (1997) Diabetes , vol.46
    • Tiedge, M.1    Lortz, S.2    Drinkgern, J.3    Lenzen, S.4
  • 21
    • 0036194529 scopus 로고    scopus 로고
    • Mitochondria as a pharmacological target.
    • Szewczyk A, Wojtczak L. Mitochondria as a pharmacological target. Pharmacol Rev 2002, 54:101-127..
    • (2002) Pharmacol Rev , vol.54
    • Szewczyk, A.1    Wojtczak, L.2
  • 22
    • 3242789423 scopus 로고    scopus 로고
    • Does the glucose-dependent insulin secretion mechanism itself cause oxidative stress in pancreatic beta-cells?
    • Fridlyand LE, Philipson LH. Does the glucose-dependent insulin secretion mechanism itself cause oxidative stress in pancreatic beta-cells? Diabetes 2004, 53:1942-1948..
    • (2004) Diabetes , vol.53
    • Fridlyand, L.E.1    Philipson, L.H.2
  • 23
    • 0034643340 scopus 로고    scopus 로고
    • Normalizing mitochondrial superoxide production blocks three pathways of hyperglycaemic damage.
    • Nishikawa T, Edelstein D, Du XL. Normalizing mitochondrial superoxide production blocks three pathways of hyperglycaemic damage. Nature 2000, 404:787-790..
    • (2000) Nature , vol.404
    • Nishikawa, T.1    Edelstein, D.2    Du, X.L.3
  • 24
    • 44449125132 scopus 로고    scopus 로고
    • Reactive oxygen species and angiogenesis: NADPH oxidase as target for cancer therapy.
    • Ushio-Fukai M, Nakamura Y. Reactive oxygen species and angiogenesis: NADPH oxidase as target for cancer therapy. Cancer Lett 2008, 266:37-52..
    • (2008) Cancer Lett , vol.266
    • Ushio-Fukai, M.1    Nakamura, Y.2
  • 25
    • 65349100528 scopus 로고    scopus 로고
    • Redox signaling across cell membranes.
    • Fisher AB. Redox signaling across cell membranes. Antioxid Redox Signal 2009, 11:1349-1356..
    • (2009) Antioxid Redox Signal , vol.11
    • Fisher, A.B.1
  • 26
    • 33845194611 scopus 로고    scopus 로고
    • Expression of isoforms of NADPH oxidase components in rat pancreatic islets.
    • Uchizono Y, Takeya R, Iwase M. Expression of isoforms of NADPH oxidase components in rat pancreatic islets. Life Sci 2006, 80:133-139..
    • (2006) Life Sci , vol.80
    • Uchizono, Y.1    Takeya, R.2    Iwase, M.3
  • 27
    • 66449112021 scopus 로고    scopus 로고
    • Association of NAD(P)H oxidase with glucose-induced insulin secretion by pancreatic beta-cells.
    • Morgan D, Rebelato E, Abdulkader F. Association of NAD(P)H oxidase with glucose-induced insulin secretion by pancreatic beta-cells. Endocrinology 2009, 150:2197-2201..
    • (2009) Endocrinology , vol.150
    • Morgan, D.1    Rebelato, E.2    Abdulkader, F.3
  • 28
    • 0032889677 scopus 로고    scopus 로고
    • Redox regulation of cellular signalling.
    • Kamata H, Hirata H. Redox regulation of cellular signalling. Cell Signal 1999, 11:1-14..
    • (1999) Cell Signal , vol.11
    • Kamata, H.1    Hirata, H.2
  • 29
    • 0033231351 scopus 로고    scopus 로고
    • Gene expression and the thiol redox state.
    • Arrigo AP. Gene expression and the thiol redox state. Free Radic Biol Med 1999, 27:936-944..
    • (1999) Free Radic Biol Med , vol.27
    • Arrigo, A.P.1
  • 31
    • 0031857290 scopus 로고    scopus 로고
    • Interaction of reactive oxygen species with ion transport mechanisms.
    • Kourie JI. Interaction of reactive oxygen species with ion transport mechanisms. Am J Physiol 1998, 275:C1-C24..
    • (1998) Am J Physiol , vol.275
    • Kourie, J.I.1
  • 32
    • 75749123115 scopus 로고    scopus 로고
    • Orchestrating redox signaling networks through regulatory cysteine switches.
    • Paulsen CE, Carroll KS. Orchestrating redox signaling networks through regulatory cysteine switches. ACS Chem Biol 2010, 5:47-62..
    • (2010) ACS Chem Biol , vol.5
    • Paulsen, C.E.1    Carroll, K.S.2
  • 33
    • 1342304048 scopus 로고    scopus 로고
    • The NAD(P)H oxidase homolog Nox4 modulates insulin-stimulated generation of H2O2 and plays an integral role in insulin signal transduction.
    • Mahadev K, Motoshima H, Wu X. The NAD(P)H oxidase homolog Nox4 modulates insulin-stimulated generation of H2O2 and plays an integral role in insulin signal transduction. Mol Cell Biol 2004, 24:1844-1854..
    • (2004) Mol Cell Biol , vol.24
    • Mahadev, K.1    Motoshima, H.2    Wu, X.3
  • 34
    • 3142707374 scopus 로고    scopus 로고
    • Hydrogen peroxide as a diffusible signal molecule in synaptic plasticity.
    • Kamsler A, Segal M. Hydrogen peroxide as a diffusible signal molecule in synaptic plasticity. Mol Neurobiol 2004, 29:167-178..
    • (2004) Mol Neurobiol , vol.29
    • Kamsler, A.1    Segal, M.2
  • 35
    • 22544454482 scopus 로고    scopus 로고
    • Involvement of a mitochondrial phosphatase in the regulation of ATP production and insulin secretion in pancreatic beta cells.
    • Pagliarini DJ, Wiley SE, Kimple ME. Involvement of a mitochondrial phosphatase in the regulation of ATP production and insulin secretion in pancreatic beta cells. Mol Cell 2005, 19:197-207..
    • (2005) Mol Cell , vol.19
    • Pagliarini, D.J.1    Wiley, S.E.2    Kimple, M.E.3
  • 36
    • 2542435891 scopus 로고    scopus 로고
    • O2 sensing in the human ductus arteriosus: redox-sensitive K+ channels are regulated by mitochondria-derived hydrogen peroxide.
    • Archer SL, Wu XC, Thebaud B, Moudgil R, Hashimoto K, Michelakis ED. O2 sensing in the human ductus arteriosus: redox-sensitive K+ channels are regulated by mitochondria-derived hydrogen peroxide. Biol Chem 2004, 385:205-216..
    • (2004) Biol Chem , vol.385
    • Archer, S.L.1    Wu, X.C.2    Thebaud, B.3    Moudgil, R.4    Hashimoto, K.5    Michelakis, E.D.6
  • 37
    • 0034998234 scopus 로고    scopus 로고
    • Hydrogen peroxide inhibits gap junctional coupling and modulates intracellular free calcium in cochlear Hensen cells.
    • Todt I, Ngezahayo A, Ernst A, Kolb HA. Hydrogen peroxide inhibits gap junctional coupling and modulates intracellular free calcium in cochlear Hensen cells. J Membr Biol 2001, 181:107-114..
    • (2001) J Membr Biol , vol.181
    • Todt, I.1    Ngezahayo, A.2    Ernst, A.3    Kolb, H.A.4
  • 38
    • 0346727508 scopus 로고    scopus 로고
    • Hydrogen peroxide and ADP-ribose induce TRPM2-mediated calcium influx and cation currents in microglia.
    • Kraft R, Grimm C, Grosse K. Hydrogen peroxide and ADP-ribose induce TRPM2-mediated calcium influx and cation currents in microglia. Am J Physiol Cell Physiol 2004, 286:C129-C137..
    • (2004) Am J Physiol Cell Physiol , vol.286
    • Kraft, R.1    Grimm, C.2    Grosse, K.3
  • 39
    • 3242813758 scopus 로고    scopus 로고
    • Differential calcium regulation by hydrogen peroxide and superoxide in vascular smooth muscle cells from spontaneously hypertensive rats.
    • Tabet F, Savoia C, Schiffrin EL, Touyz RM. Differential calcium regulation by hydrogen peroxide and superoxide in vascular smooth muscle cells from spontaneously hypertensive rats. J Cardiovasc Pharmacol 2004, 44:200-208..
    • (2004) J Cardiovasc Pharmacol , vol.44
    • Tabet, F.1    Savoia, C.2    Schiffrin, E.L.3    Touyz, R.M.4
  • 41
  • 42
    • 0030886770 scopus 로고    scopus 로고
    • Oxidative stress activates extracellular signal-regulated kinases through Src and Ras in cultured cardiac myocytes of neonatal rats.
    • Aikawa R, Komuro I, Yamazaki T. Oxidative stress activates extracellular signal-regulated kinases through Src and Ras in cultured cardiac myocytes of neonatal rats. J Clin Invest 1997, 100:1813-1821..
    • (1997) J Clin Invest , vol.100
    • Aikawa, R.1    Komuro, I.2    Yamazaki, T.3
  • 43
    • 0029739428 scopus 로고    scopus 로고
    • Identification of hydrogen peroxide as the relevant messenger in the activation pathway of transcription factor NF-kappaB.
    • Schmidt KN, Amstad P, Cerutti P, Baeuerle PA. Identification of hydrogen peroxide as the relevant messenger in the activation pathway of transcription factor NF-kappaB. Adv Exp Med Biol 1996, 387:63-68..
    • (1996) Adv Exp Med Biol , vol.387
    • Schmidt, K.N.1    Amstad, P.2    Cerutti, P.3    Baeuerle, P.A.4
  • 44
    • 12144290563 scopus 로고    scopus 로고
    • Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase.
    • Brunet A, Sweeney LB, Sturgill JF. Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase. Science 2004, 303:2011-2015..
    • (2004) Science , vol.303
    • Brunet, A.1    Sweeney, L.B.2    Sturgill, J.F.3
  • 45
    • 25144454432 scopus 로고    scopus 로고
    • Increased dosage of mammalian Sir2 in pancreatic beta cells enhances glucose-stimulated insulin secretion in mice.
    • Moynihan KA, Grimm AA, Plueger MM. Increased dosage of mammalian Sir2 in pancreatic beta cells enhances glucose-stimulated insulin secretion in mice. Cell Metab 2005, 2:105-117..
    • (2005) Cell Metab , vol.2
    • Moynihan, K.A.1    Grimm, A.A.2    Plueger, M.M.3
  • 46
    • 0026632641 scopus 로고
    • Evidence that glucose can control insulin release independently from its action on ATP-sensitive K+ channels in mouse B cells.
    • Gembal M, Gilon P, Henquin JC. Evidence that glucose can control insulin release independently from its action on ATP-sensitive K+ channels in mouse B cells. J Clin Invest 1992, 89:1288-1295..
    • (1992) J Clin Invest , vol.89
    • Gembal, M.1    Gilon, P.2    Henquin, J.C.3
  • 48
    • 0037376674 scopus 로고    scopus 로고
    • Oxidant signals and oxidative stress.
    • Finkel T. Oxidant signals and oxidative stress. Curr Opin Cell Biol 2003, 15:247-254..
    • (2003) Curr Opin Cell Biol , vol.15
    • Finkel, T.1
  • 50
    • 0346788896 scopus 로고    scopus 로고
    • Mitochondrial matrix reactive oxygen species production is very sensitive to mild uncoupling.
    • Miwa S, Brand MD. Mitochondrial matrix reactive oxygen species production is very sensitive to mild uncoupling. Biochem Soc Trans 2003, 31:1300-1301..
    • (2003) Biochem Soc Trans , vol.31
    • Miwa, S.1    Brand, M.D.2
  • 51
    • 4043147798 scopus 로고    scopus 로고
    • Mitochondrial superoxide: production, biological effects, and activation of uncoupling proteins.
    • Brand MD, Affourtit C, Esteves TC. Mitochondrial superoxide: production, biological effects, and activation of uncoupling proteins. Free Radic Biol Med 2004, 37:755-767..
    • (2004) Free Radic Biol Med , vol.37
    • Brand, M.D.1    Affourtit, C.2    Esteves, T.C.3
  • 52
    • 27344449065 scopus 로고    scopus 로고
    • Uncoupling proteins: current status and therapeutic prospects.
    • Nedergaard J, Ricquier D, Kozak LP. Uncoupling proteins: current status and therapeutic prospects. EMBO Rep 2005, 6:917-921..
    • (2005) EMBO Rep , vol.6
    • Nedergaard, J.1    Ricquier, D.2    Kozak, L.P.3
  • 54
    • 0033667705 scopus 로고    scopus 로고
    • Disruption of the uncoupling protein-2 gene in mice reveals a role in immunity and reactive oxygen species production.
    • Arsenijevic D, Onuma H, Pecqueur C. Disruption of the uncoupling protein-2 gene in mice reveals a role in immunity and reactive oxygen species production. Nat Genet 2000, 26:435-439..
    • (2000) Nat Genet , vol.26
    • Arsenijevic, D.1    Onuma, H.2    Pecqueur, C.3
  • 55
    • 21444440464 scopus 로고    scopus 로고
    • Persistent nuclear factor-kappa B activation in Ucp2-/- mice leads to enhanced nitric oxide and inflammatory cytokine production.
    • Bai Y, Onuma H, Bai X. Persistent nuclear factor-kappa B activation in Ucp2-/- mice leads to enhanced nitric oxide and inflammatory cytokine production. J Biol Chem 2005, 280:19062-19069..
    • (2005) J Biol Chem , vol.280
    • Bai, Y.1    Onuma, H.2    Bai, X.3
  • 56
    • 0034804062 scopus 로고    scopus 로고
    • Uncoupling protein-2 participates in cellular defense against oxidative stress in clonal beta-cells.
    • Li LX, Skorpen F, Egeberg K, Jorgensen IH, Grill V. Uncoupling protein-2 participates in cellular defense against oxidative stress in clonal beta-cells. Biochem Biophys Res Commun 2001, 282:273-277..
    • (2001) Biochem Biophys Res Commun , vol.282
    • Li, L.X.1    Skorpen, F.2    Egeberg, K.3    Jorgensen, I.H.4    Grill, V.5
  • 57
    • 0041464712 scopus 로고    scopus 로고
    • Uncoupling protein-2 prevents neuronal death and diminishes brain dysfunction after stroke and brain trauma.
    • Mattiasson G, Shamloo M, Gido G. Uncoupling protein-2 prevents neuronal death and diminishes brain dysfunction after stroke and brain trauma. Nat Med 2003, 9:1062-1068..
    • (2003) Nat Med , vol.9
    • Mattiasson, G.1    Shamloo, M.2    Gido, G.3
  • 58
    • 49649122302 scopus 로고    scopus 로고
    • UCP2 mediates ghrelin's action on NPY/AgRP neurons by lowering free radicals.
    • Andrews ZB, Liu ZW, Walllingford N. UCP2 mediates ghrelin's action on NPY/AgRP neurons by lowering free radicals. Nature 2008, 454:846-851..
    • (2008) Nature , vol.454
    • Andrews, Z.B.1    Liu, Z.W.2    Walllingford, N.3
  • 59
    • 13444282314 scopus 로고    scopus 로고
    • Recruitment of mitochondrial uncoupling protein UCP2 after lipopolysaccharide induction.
    • Ruzicka M, Skobisova E, Dlaskova A. Recruitment of mitochondrial uncoupling protein UCP2 after lipopolysaccharide induction. Int J Biochem Cell Biol 2005, 37:809-821..
    • (2005) Int J Biochem Cell Biol , vol.37
    • Ruzicka, M.1    Skobisova, E.2    Dlaskova, A.3
  • 60
    • 20644466225 scopus 로고    scopus 로고
    • Tumor necrosis factor increases mitochondrial oxidant production and induces expression of uncoupling protein-2 in the regenerating rat liver.
    • Lee FY, Li Y, Zhu H. Tumor necrosis factor increases mitochondrial oxidant production and induces expression of uncoupling protein-2 in the regenerating rat liver. Hepatology 1999, 29:677-687..
    • (1999) Hepatology , vol.29
    • Lee, F.Y.1    Li, Y.2    Zhu, H.3
  • 61
    • 0037044822 scopus 로고    scopus 로고
    • Regulation of the uncoupling protein-2 gene in INS-1 beta-cells by oleic acid.
    • Medvedev AV, Robidoux J, Bai X. Regulation of the uncoupling protein-2 gene in INS-1 beta-cells by oleic acid. J Biol Chem 2002, 277:42639-42644..
    • (2002) J Biol Chem , vol.277
    • Medvedev, A.V.1    Robidoux, J.2    Bai, X.3
  • 62
    • 0034646232 scopus 로고    scopus 로고
    • Gene microarray identification of redox and mitochondrial elements that control resistance or sensitivity to apoptosis.
    • Voehringer DW, Hirschberg DL, Xiao J. Gene microarray identification of redox and mitochondrial elements that control resistance or sensitivity to apoptosis. Proc Natl Acad Sci U S A 2000, 97:2680-2685..
    • (2000) Proc Natl Acad Sci U S A , vol.97
    • Voehringer, D.W.1    Hirschberg, D.L.2    Xiao, J.3
  • 63
    • 0032584237 scopus 로고    scopus 로고
    • Diet-induced changes in uncoupling proteins in obesity-prone and obesity-resistant strains of mice.
    • Surwit RS, Wang S, Petro AE. Diet-induced changes in uncoupling proteins in obesity-prone and obesity-resistant strains of mice. Proc Natl Acad Sci U S A 1998, 95:4061-4065..
    • (1998) Proc Natl Acad Sci U S A , vol.95
    • Surwit, R.S.1    Wang, S.2    Petro, A.E.3
  • 64
    • 34548604499 scopus 로고    scopus 로고
    • Glucose sensing by POMC neurons regulates glucose homeostasis and is impaired in obesity.
    • Parton LE, Ye CP, Coppari R. Glucose sensing by POMC neurons regulates glucose homeostasis and is impaired in obesity. Nature 2007, 449:228-232..
    • (2007) Nature , vol.449
    • Parton, L.E.1    Ye, C.P.2    Coppari, R.3
  • 65
    • 18244379331 scopus 로고    scopus 로고
    • Superoxide activates mitochondrial uncoupling proteins.
    • Echtay KS, Roussel D, St-Pierre J. Superoxide activates mitochondrial uncoupling proteins. Nature 2002, 415:96-99..
    • (2002) Nature , vol.415
    • Echtay, K.S.1    Roussel, D.2    St-Pierre, J.3
  • 66
    • 0037033039 scopus 로고    scopus 로고
    • Superoxide activates mitochondrial uncoupling protein 2 from the matrix side. Studies using targeted antioxidants.
    • Echtay KS, Murphy MP, Smith RA, Talbot DA, Brand MD. Superoxide activates mitochondrial uncoupling protein 2 from the matrix side. Studies using targeted antioxidants. J Biol Chem 2002, 277:47129-47135..
    • (2002) J Biol Chem , vol.277
    • Echtay, K.S.1    Murphy, M.P.2    Smith, R.A.3    Talbot, D.A.4    Brand, M.D.5
  • 67
    • 0041465009 scopus 로고    scopus 로고
    • A signalling role for 4-hydroxy-2-nonenal in regulation of mitochondrial uncoupling.
    • Echtay KS, Esteves TC, Pakay JL. A signalling role for 4-hydroxy-2-nonenal in regulation of mitochondrial uncoupling. EMBO J 2003, 22:4103-4110..
    • (2003) EMBO J , vol.22
    • Echtay, K.S.1    Esteves, T.C.2    Pakay, J.L.3
  • 68
    • 0035875087 scopus 로고    scopus 로고
    • Uncoupling protein-2 negatively regulates insulin secretion and is a major link between obesity, beta cell dysfunction, and type 2 diabetes.
    • Zhang CY, Baffy G, Perret P. Uncoupling protein-2 negatively regulates insulin secretion and is a major link between obesity, beta cell dysfunction, and type 2 diabetes. Cell 2001, 105:745-755..
    • (2001) Cell , vol.105
    • Zhang, C.Y.1    Baffy, G.2    Perret, P.3
  • 69
    • 0032991716 scopus 로고    scopus 로고
    • Overexpression of uncoupling protein 2 inhibits glucose-stimulated insulin secretion from rat islets.
    • Chan CB, MacDonald PE, Saleh MC, Johns DC, Marban E, Wheeler MB. Overexpression of uncoupling protein 2 inhibits glucose-stimulated insulin secretion from rat islets. Diabetes 1999, 48:1482-1486..
    • (1999) Diabetes , vol.48
    • Chan, C.B.1    MacDonald, P.E.2    Saleh, M.C.3    Johns, D.C.4    Marban, E.5    Wheeler, M.B.6
  • 70
    • 0035117975 scopus 로고    scopus 로고
    • Effects of adenoviral overexpression of uncoupling protein-2 and -3 on mitochondrial respiration in insulinoma cells.
    • Hong Y, Fink BD, Dillon JS, Sivitz WI. Effects of adenoviral overexpression of uncoupling protein-2 and -3 on mitochondrial respiration in insulinoma cells. Endocrinology 2001, 142:249-256..
    • (2001) Endocrinology , vol.142
    • Hong, Y.1    Fink, B.D.2    Dillon, J.S.3    Sivitz, W.I.4
  • 71
    • 0034990987 scopus 로고    scopus 로고
    • Increased uncoupling protein-2 levels in beta-cells are associated with impaired glucose-stimulated insulin secretion: mechanism of action.
    • Chan CB, De Leo D, Joseph JW. Increased uncoupling protein-2 levels in beta-cells are associated with impaired glucose-stimulated insulin secretion: mechanism of action. Diabetes 2001, 50:1302-1310..
    • (2001) Diabetes , vol.50
    • Chan, C.B.1    De Leo, D.2    Joseph, J.W.3
  • 72
    • 33749873671 scopus 로고    scopus 로고
    • Endogenous islet uncoupling protein-2 expression and loss of glucose homeostasis in ob/ob mice.
    • Saleh MC, Wheeler MB, Chan CB. Endogenous islet uncoupling protein-2 expression and loss of glucose homeostasis in ob/ob mice. J Endocrinol 2006, 190:659-667..
    • (2006) J Endocrinol , vol.190
    • Saleh, M.C.1    Wheeler, M.B.2    Chan, C.B.3
  • 73
    • 33744548069 scopus 로고    scopus 로고
    • Genipin inhibits UCP2-mediated proton leak and acutely reverses obesity- and high glucose-induced beta cell dysfunction in isolated pancreatic islets.
    • Zhang CY, Parton LE, Ye CP. Genipin inhibits UCP2-mediated proton leak and acutely reverses obesity- and high glucose-induced beta cell dysfunction in isolated pancreatic islets. Cell Metab 2006, 3:417-427..
    • (2006) Cell Metab , vol.3
    • Zhang, C.Y.1    Parton, L.E.2    Ye, C.P.3
  • 74
    • 67649641804 scopus 로고    scopus 로고
    • Persistent oxidative stress due to absence of uncoupling protein 2 associated with impaired pancreatic beta-cell function.
    • Pi J, Bai Y, Daniel KW. Persistent oxidative stress due to absence of uncoupling protein 2 associated with impaired pancreatic beta-cell function. Endocrinology 2009, 150:3040-3048..
    • (2009) Endocrinology , vol.150
    • Pi, J.1    Bai, Y.2    Daniel, K.W.3
  • 75
    • 0037219409 scopus 로고    scopus 로고
    • Are oxidative stress-activated signaling pathways mediators of insulin resistance and beta-cell dysfunction?
    • Evans JL, Goldfine ID, Maddux BA, Grodsky GM. Are oxidative stress-activated signaling pathways mediators of insulin resistance and beta-cell dysfunction? Diabetes 2003, 52:1-8.
    • (2003) Diabetes , vol.52 , pp. 1-8
    • Evans, J.L.1    Goldfine, I.D.2    Maddux, B.A.3    Grodsky, G.M.4
  • 76
    • 14944340746 scopus 로고    scopus 로고
    • Oxidative stress and antioxidant treatment in diabetes.
    • Scott JA, King GL. Oxidative stress and antioxidant treatment in diabetes. Ann N Y Acad Sci 2004, 1031:204-213..
    • (2004) Ann N Y Acad Sci , vol.1031
    • Scott, J.A.1    King, G.L.2
  • 77
    • 17044386953 scopus 로고    scopus 로고
    • Type 2 diabetes: principles of pathogenesis and therapy.
    • Stumvoll M, Goldstein BJ, van Haeften TW. Type 2 diabetes: principles of pathogenesis and therapy. Lancet 2005, 365:1333-1346..
    • (2005) Lancet , vol.365
    • Stumvoll, M.1    Goldstein, B.J.2    van Haeften, T.W.3
  • 78
    • 33748052967 scopus 로고    scopus 로고
    • Nrf2-Keap1 regulation of cellular defense mechanisms against electrophiles and reactive oxygen species.
    • Kobayashi M, Yamamoto M. Nrf2-Keap1 regulation of cellular defense mechanisms against electrophiles and reactive oxygen species. Adv Enzyme Regul 2006, 46:113-140..
    • (2006) Adv Enzyme Regul , vol.46
    • Kobayashi, M.1    Yamamoto, M.2
  • 79
    • 0037469183 scopus 로고    scopus 로고
    • Protective role of uncoupling protein 2 in atherosclerosis.
    • Blanc J, Alves-Guerra MC, Esposito B. Protective role of uncoupling protein 2 in atherosclerosis. Circulation 2003, 107:388-390..
    • (2003) Circulation , vol.107
    • Blanc, J.1    Alves-Guerra, M.C.2    Esposito, B.3
  • 80
    • 63449141267 scopus 로고    scopus 로고
    • Reduced antioxidant capacity and diet-induced atherosclerosis in uncoupling protein-2-deficient mice.
    • Moukdar F, Robidoux J, Lyght O, Pi J, Daniel KW, Collins S. Reduced antioxidant capacity and diet-induced atherosclerosis in uncoupling protein-2-deficient mice. J Lipid Res 2009, 50:59-70..
    • (2009) J Lipid Res , vol.50
    • Moukdar, F.1    Robidoux, J.2    Lyght, O.3    Pi, J.4    Daniel, K.W.5    Collins, S.6
  • 81
    • 27644448810 scopus 로고    scopus 로고
    • Mitochondrial uncoupling proteins in the CNS: in support of function and survival.
    • Andrews ZB, Diano S, Horvath TL. Mitochondrial uncoupling proteins in the CNS: in support of function and survival. Nat Rev Neurosci 2005, 6:829-840..
    • (2005) Nat Rev Neurosci , vol.6
    • Andrews, Z.B.1    Diano, S.2    Horvath, T.L.3
  • 82
    • 33646188854 scopus 로고    scopus 로고
    • Enhanced colon tumor induction in uncoupling protein-2 deficient mice is associated with NF-kappaB activation and oxidative stress.
    • Derdak Z, Fulop P, Sabo E. Enhanced colon tumor induction in uncoupling protein-2 deficient mice is associated with NF-kappaB activation and oxidative stress. Carcinogenesis 2006, 27:956-961..
    • (2006) Carcinogenesis , vol.27
    • Derdak, Z.1    Fulop, P.2    Sabo, E.3
  • 83
    • 0342449328 scopus 로고    scopus 로고
    • Ten years of gene targeting: targeted mouse mutants, from vector design to phenotype analysis.
    • Muller U. Ten years of gene targeting: targeted mouse mutants, from vector design to phenotype analysis. Mech Dev 1999, 82:3-21..
    • (1999) Mech Dev , vol.82
    • Muller, U.1
  • 84
    • 0036207648 scopus 로고    scopus 로고
    • Mice with targeted gene disruptions or gene insertions for diabetes research: problems, pitfalls, and potential solutions.
    • Leiter EH. Mice with targeted gene disruptions or gene insertions for diabetes research: problems, pitfalls, and potential solutions. Diabetologia 2002, 45:296-308..
    • (2002) Diabetologia , vol.45
    • Leiter, E.H.1
  • 86
    • 4444264384 scopus 로고    scopus 로고
    • Flanking gene and genetic background problems in genetically manipulated mice.
    • Crusio WE. Flanking gene and genetic background problems in genetically manipulated mice. Biol Psychiatry 2004, 56:381-385..
    • (2004) Biol Psychiatry , vol.56
    • Crusio, W.E.1
  • 87
    • 0029027767 scopus 로고
    • Defective glucose-stimulated insulin release from perifused islets of C57BL/6J mice.
    • Lee SK, Opara EC, Surwit RS, Feinglos MN, Akwari OE. Defective glucose-stimulated insulin release from perifused islets of C57BL/6J mice. Pancreas 1995, 11:206-211..
    • (1995) Pancreas , vol.11
    • Lee, S.K.1    Opara, E.C.2    Surwit, R.S.3    Feinglos, M.N.4    Akwari, O.E.5
  • 88
    • 3042636409 scopus 로고    scopus 로고
    • Glucose homeostasis and tissue transcript content of insulin signaling intermediates in four inbred strains of mice: C57BL/6, C57BLKS/6, DBA/2, and 129X1.
    • Goren HJ, Kulkarni RN, Kahn CR. Glucose homeostasis and tissue transcript content of insulin signaling intermediates in four inbred strains of mice: C57BL/6, C57BLKS/6, DBA/2, and 129X1. Endocrinology 2004, 145:3307-3323..
    • (2004) Endocrinology , vol.145
    • Goren, H.J.1    Kulkarni, R.N.2    Kahn, C.R.3
  • 89
    • 20944448234 scopus 로고    scopus 로고
    • A genetic and physiological study of impaired glucose homeostasis control in C57BL/6J mice.
    • Toye AA, Lippiat JD, Proks P. A genetic and physiological study of impaired glucose homeostasis control in C57BL/6J mice. Diabetologia 2005, 48:675-686..
    • (2005) Diabetologia , vol.48
    • Toye, A.A.1    Lippiat, J.D.2    Proks, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.