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Volumn 12, Issue SUPPL. 2, 2010, Pages 134-140

Mitochondrial uncoupling protein 2 in pancreatic β-cells

Author keywords

Glucose stimulated insulin secretion; INS 1E cells; Mitochondria; Proteasome; Protein degradation; Turnover; UCP2; UCP3

Indexed keywords

INSULIN; MESSENGER RNA; MITOCHONDRIAL PROTEIN; UNCOUPLING PROTEIN 2; UNCOUPLING PROTEIN 3;

EID: 77957293638     PISSN: 14628902     EISSN: 14631326     Source Type: Journal    
DOI: 10.1111/j.1463-1326.2010.01264.x     Document Type: Article
Times cited : (25)

References (50)
  • 1
    • 0042661099 scopus 로고    scopus 로고
    • Regulatory mechanisms in the interaction between carbohydrate and lipid oxidation during exercise.
    • Spriet LL, Watt MJ. Regulatory mechanisms in the interaction between carbohydrate and lipid oxidation during exercise. Acta Physiol Scand 2003, 178:443-452..
    • (2003) Acta Physiol Scand , vol.178
    • Spriet, L.L.1    Watt, M.J.2
  • 3
    • 58149307894 scopus 로고    scopus 로고
    • Dissociation between sensing and metabolism of glucose in sugar sensing neurons.
    • Gonzalez JA, Reimann F, Burdakov D. Dissociation between sensing and metabolism of glucose in sugar sensing neurons. J Physiol 2009, 587:41-48..
    • (2009) J Physiol , vol.587
    • Gonzalez, J.A.1    Reimann, F.2    Burdakov, D.3
  • 4
    • 0036444648 scopus 로고    scopus 로고
    • Endogenous regulation of insulin secretion by UCP2.
    • Chan CB. Endogenous regulation of insulin secretion by UCP2. Clin Lab 2002, 48:599-604..
    • (2002) Clin Lab , vol.48
    • Chan, C.B.1
  • 6
    • 33746920386 scopus 로고    scopus 로고
    • Uncoupling proteins: role in insulin resistance and insulin insufficiency.
    • Chan CB, Harper ME. Uncoupling proteins: role in insulin resistance and insulin insufficiency. Curr Diabetes Rev 2006, 2:271-283..
    • (2006) Curr Diabetes Rev , vol.2
    • Chan, C.B.1    Harper, M.E.2
  • 7
    • 33751269135 scopus 로고    scopus 로고
    • Regulation of insulin secretion by uncoupling protein.
    • Chan CB, Kashemsant N. Regulation of insulin secretion by uncoupling protein. Biochem Soc Trans 2006, 34:802-805..
    • (2006) Biochem Soc Trans , vol.34
    • Chan, C.B.1    Kashemsant, N.2
  • 8
    • 10944265062 scopus 로고    scopus 로고
    • Free fatty acid-induced beta-cell defects are dependent on uncoupling protein 2 expression.
    • Joseph JW, Koshkin V, Saleh MC. Free fatty acid-induced beta-cell defects are dependent on uncoupling protein 2 expression. J Biol Chem 2004, 279:51049-51056..
    • (2004) J Biol Chem , vol.279
    • Joseph, J.W.1    Koshkin, V.2    Saleh, M.C.3
  • 9
    • 0036829870 scopus 로고    scopus 로고
    • Uncoupling protein 2 knockout mice have enhanced insulin secretory capacity after a high-fat diet.
    • Joseph JW, Koshkin V, Zhang CY. Uncoupling protein 2 knockout mice have enhanced insulin secretory capacity after a high-fat diet. Diabetes 2002, 51:3211-3219..
    • (2002) Diabetes , vol.51
    • Joseph, J.W.1    Koshkin, V.2    Zhang, C.Y.3
  • 10
    • 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
  • 11
    • 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
  • 13
    • 0035875366 scopus 로고    scopus 로고
    • A mitochondrial uncoupling artifact can be caused by expression of uncoupling protein 1 in yeast.
    • Stuart JA, Harper JA, Brindle KM, Jekabsons MB, Brand MD. A mitochondrial uncoupling artifact can be caused by expression of uncoupling protein 1 in yeast. Biochem J 2001, 356:779-789..
    • (2001) Biochem J , vol.356
    • Stuart, J.A.1    Harper, J.A.2    Brindle, K.M.3    Jekabsons, M.B.4    Brand, M.D.5
  • 14
    • 0035283161 scopus 로고    scopus 로고
    • Homologues of the uncoupling protein from brown adipose tissue (UCP1): UCP2, UCP3, BMCP1 and UCP4.
    • Bouillaud F, Couplan E, Pecqueur C, Ricquier D. Homologues of the uncoupling protein from brown adipose tissue (UCP1): UCP2, UCP3, BMCP1 and UCP4. Biochim Biophys Acta 2001, 1504:107-119..
    • (2001) Biochim Biophys Acta , vol.1504
    • Bouillaud, F.1    Couplan, E.2    Pecqueur, C.3    Ricquier, D.4
  • 15
    • 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
  • 16
    • 0038168520 scopus 로고    scopus 로고
    • Reconstitution of recombinant uncoupling proteins: UCP1, -2, and -3 have similar affinities for ATP and are unaffected by coenzyme Q10.
    • Jaburek M, Garlid KD. Reconstitution of recombinant uncoupling proteins: UCP1, -2, and -3 have similar affinities for ATP and are unaffected by coenzyme Q10. J Biol Chem 2003, 278:25825-25831..
    • (2003) J Biol Chem , vol.278
    • Jaburek, M.1    Garlid, K.D.2
  • 17
    • 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
  • 18
    • 43549101948 scopus 로고    scopus 로고
    • Energization-dependent endogenous activation of proton conductance in skeletal muscle mitochondria.
    • Parker N, Affourtit C, Vidal-Puig A, Brand MD. Energization-dependent endogenous activation of proton conductance in skeletal muscle mitochondria. Biochem J 2008, 412:131-139..
    • (2008) Biochem J , vol.412
    • Parker, N.1    Affourtit, C.2    Vidal-Puig, A.3    Brand, M.D.4
  • 19
    • 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
  • 20
    • 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
  • 21
    • 0037135559 scopus 로고    scopus 로고
    • No evidence for a basal, retinoic, or superoxide-induced uncoupling activity of the uncoupling protein 2 present in spleen or lung mitochondria.
    • Couplan E, del Mar Gonzalez-Barroso M, Alves-Guerra MC, Ricquier D, Goubern M, Bouillaud F. No evidence for a basal, retinoic, or superoxide-induced uncoupling activity of the uncoupling protein 2 present in spleen or lung mitochondria. J Biol Chem 2002, 277:26268-26275..
    • (2002) J Biol Chem , vol.277
    • Couplan, E.1    del Mar Gonzalez-Barroso, M.2    Alves-Guerra, M.C.3    Ricquier, D.4    Goubern, M.5    Bouillaud, F.6
  • 22
    • 0037253404 scopus 로고    scopus 로고
    • The 'novel''uncoupling' proteins UCP2 and UCP3: what do they really do? Pros and cons for suggested functions.
    • Nedergaard J, Cannon B. The 'novel''uncoupling' proteins UCP2 and UCP3: what do they really do? Pros and cons for suggested functions. Exp Physiol 2003, 88:65-84..
    • (2003) Exp Physiol , vol.88
    • Nedergaard, J.1    Cannon, B.2
  • 23
    • 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
  • 24
    • 23244454768 scopus 로고    scopus 로고
    • The reactions catalysed by the mitochondrial uncoupling proteins UCP2 and UCP3.
    • Esteves TC, Brand MD. The reactions catalysed by the mitochondrial uncoupling proteins UCP2 and UCP3. Biochim Biophys Acta 2005, 1709:35-44..
    • (2005) Biochim Biophys Acta , vol.1709
    • Esteves, T.C.1    Brand, M.D.2
  • 25
    • 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
  • 26
    • 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
  • 27
    • 69249205581 scopus 로고    scopus 로고
    • Dysregulation of glucose homeostasis in nicotinamide nucleotide transhydrogenase knockout mice is independent of uncoupling protein 2.
    • Parker N, Vidal-Puig AJ, Azzu V, Brand MD. Dysregulation of glucose homeostasis in nicotinamide nucleotide transhydrogenase knockout mice is independent of uncoupling protein 2. Biochim Biophys Acta 2009, 1787:1451-1457..
    • (2009) Biochim Biophys Acta , vol.1787
    • Parker, N.1    Vidal-Puig, A.J.2    Azzu, V.3    Brand, M.D.4
  • 29
    • 37649024444 scopus 로고    scopus 로고
    • Role of uncoupling protein UCP2 in cell-mediated immunity: how macrophage-mediated insulitis is accelerated in a model of autoimmune diabetes.
    • Emre Y, Hurtaud C, Karaca M, Nubel T, Zavala F, Ricquier D. Role of uncoupling protein UCP2 in cell-mediated immunity: how macrophage-mediated insulitis is accelerated in a model of autoimmune diabetes. Proc Natl Acad Sci U S A 2007, 104:19085-19090..
    • (2007) Proc Natl Acad Sci U S A , vol.104
    • Emre, Y.1    Hurtaud, C.2    Karaca, M.3    Nubel, T.4    Zavala, F.5    Ricquier, D.6
  • 30
    • 0842291578 scopus 로고    scopus 로고
    • Glucose sensitivity and metabolism-secretion coupling studied during two-year continuous culture in INS-1E insulinoma cells.
    • Merglen A, Theander S, Rubi B, Chaffard G, Wollheim CB, Maechler P. Glucose sensitivity and metabolism-secretion coupling studied during two-year continuous culture in INS-1E insulinoma cells. Endocrinology 2004, 145:667-678..
    • (2004) Endocrinology , vol.145
    • Merglen, A.1    Theander, S.2    Rubi, B.3    Chaffard, G.4    Wollheim, C.B.5    Maechler, P.6
  • 31
    • 38149130672 scopus 로고    scopus 로고
    • Uncoupling protein-2 contributes significantly to high mitochondrial proton leak in INS-1E insulinoma cells and attenuates glucose-stimulated insulin secretion.
    • Affourtit C, Brand MD. Uncoupling protein-2 contributes significantly to high mitochondrial proton leak in INS-1E insulinoma cells and attenuates glucose-stimulated insulin secretion. Biochem J 2008, 409:199-204..
    • (2008) Biochem J , vol.409
    • Affourtit, C.1    Brand, M.D.2
  • 32
    • 65449174289 scopus 로고    scopus 로고
    • Measuring mitochondrial bioenergetics in INS-1E insulinoma cells.
    • Affourtit C, Brand MD. Measuring mitochondrial bioenergetics in INS-1E insulinoma cells. Methods Enzymol 2009, 457:405-424..
    • (2009) Methods Enzymol , vol.457
    • Affourtit, C.1    Brand, M.D.2
  • 33
    • 0027241092 scopus 로고
    • Control of the effective P/O ratio of oxidative phosphorylation in liver mitochondria and hepatocytes.
    • Brand MD, Harper ME, Taylor HC. Control of the effective P/O ratio of oxidative phosphorylation in liver mitochondria and hepatocytes. Biochem J 1993, 291:739-748..
    • (1993) Biochem J , vol.291
    • Brand, M.D.1    Harper, M.E.2    Taylor, H.C.3
  • 34
    • 33646678667 scopus 로고    scopus 로고
    • UCP2 knockout mouse islets have lower consumption and faster oscillations of beta cell oxygen.
    • Joseph JW, Chan CB, Wheeler MB. UCP2 knockout mouse islets have lower consumption and faster oscillations of beta cell oxygen. Can J Diabetes 2005, 29:19-26..
    • (2005) Can J Diabetes , vol.29
    • Joseph, J.W.1    Chan, C.B.2    Wheeler, M.B.3
  • 35
    • 33745615380 scopus 로고    scopus 로고
    • The physiological regulation of uncoupling proteins.
    • Nicholls DG. The physiological regulation of uncoupling proteins. Biochim Biophys Acta 2006, 1757:459-466..
    • (2006) Biochim Biophys Acta , vol.1757
    • Nicholls, D.G.1
  • 36
    • 33846446089 scopus 로고    scopus 로고
    • UCP2 is a mitochondrial transporter with an unusual very short half-life.
    • Rousset S, Mozo J, Dujardin G. UCP2 is a mitochondrial transporter with an unusual very short half-life. FEBS Lett 2007, 581:479-482..
    • (2007) FEBS Lett , vol.581
    • Rousset, S.1    Mozo, J.2    Dujardin, G.3
  • 37
    • 38549120705 scopus 로고    scopus 로고
    • Uncoupling protein-2 accumulates rapidly in the inner mitochondrial membrane during mitochondrial reactive oxygen stress in macrophages.
    • Giardina TM, Steer JH, Lo SZ, Joyce DA. Uncoupling protein-2 accumulates rapidly in the inner mitochondrial membrane during mitochondrial reactive oxygen stress in macrophages. Biochim Biophys Acta 2008, 1777:118-129..
    • (2008) Biochim Biophys Acta , vol.1777
    • Giardina, T.M.1    Steer, J.H.2    Lo, S.Z.3    Joyce, D.A.4
  • 38
    • 46349101669 scopus 로고    scopus 로고
    • On the role of uncoupling protein-2 in pancreatic beta cells.
    • Affourtit C, Brand MD. On the role of uncoupling protein-2 in pancreatic beta cells. Biochim Biophys Acta 2008, 1777:973-979..
    • (2008) Biochim Biophys Acta , vol.1777
    • Affourtit, C.1    Brand, M.D.2
  • 39
    • 33244486764 scopus 로고    scopus 로고
    • Sirt1 regulates insulin secretion by repressing UCP2 in pancreatic beta cells.
    • Bordone L, Motta MC, Picard F. Sirt1 regulates insulin secretion by repressing UCP2 in pancreatic beta cells. PLoS Biol 2006, 4:e31..
    • (2006) PLoS Biol , vol.4
    • Bordone, L.1    Motta, M.C.2    Picard, F.3
  • 40
    • 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
  • 41
  • 44
    • 76649093912 scopus 로고    scopus 로고
    • Degradation of an intramitochondrial protein by the cytosolic proteasome.
    • Azzu V, Brand MD. Degradation of an intramitochondrial protein by the cytosolic proteasome. J Cell Sci 2010, 123:578-585..
    • (2010) J Cell Sci , vol.123
    • Azzu, V.1    Brand, M.D.2
  • 45
    • 76549091356 scopus 로고    scopus 로고
    • Rapid turnover of mitochondrial uncoupling protein 3.
    • Azzu V, Mookerjee SA, Brand MD. Rapid turnover of mitochondrial uncoupling protein 3. Biochem J 2010, 426:13-17..
    • (2010) Biochem J , vol.426
    • Azzu, V.1    Mookerjee, S.A.2    Brand, M.D.3
  • 46
    • 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
  • 47
    • 26844459794 scopus 로고    scopus 로고
    • Role of ubiquitin-proteasome degradation pathway in biogenesis efficiency of β-cell ATP-sensitive potassium channels.
    • Yan FF, Lin CW, Cartier EA, Shyng SL. Role of ubiquitin-proteasome degradation pathway in biogenesis efficiency of β-cell ATP-sensitive potassium channels. Am J Physiol Cell Physiol 2005, 289:C1351-C1359..
    • (2005) Am J Physiol Cell Physiol , vol.289
    • Yan, F.F.1    Lin, C.W.2    Cartier, E.A.3    Shyng, S.L.4
  • 48
    • 33744965755 scopus 로고    scopus 로고
    • Essential role of ubiquitin-proteasome system in normal regulation of insulin secretion.
    • Kawaguchi M, Minami K, Nagashima K, Seino S. Essential role of ubiquitin-proteasome system in normal regulation of insulin secretion. J Biol Chem 2006, 281:13015-13020..
    • (2006) J Biol Chem , vol.281
    • Kawaguchi, M.1    Minami, K.2    Nagashima, K.3    Seino, S.4
  • 49
    • 18144363161 scopus 로고    scopus 로고
    • Proteasome inhibition alters glucose-stimulated (pro)insulin secretion and turnover in pancreatic β-cells.
    • Kitiphongspattana K, Mathews CE, Leiter EH, Gaskins HR. Proteasome inhibition alters glucose-stimulated (pro)insulin secretion and turnover in pancreatic β-cells. J Biol Chem 2005, 280:15727-15734..
    • (2005) J Biol Chem , vol.280
    • Kitiphongspattana, K.1    Mathews, C.E.2    Leiter, E.H.3    Gaskins, H.R.4
  • 50
    • 10744222893 scopus 로고    scopus 로고
    • Uncoupling protein 2 promoter polymorphism -866G/A affects its expression in beta-cells and modulates clinical profiles of Japanese type 2 diabetic patients.
    • Sasahara M, Nishi M, Kawashima H. Uncoupling protein 2 promoter polymorphism -866G/A affects its expression in beta-cells and modulates clinical profiles of Japanese type 2 diabetic patients. Diabetes 2004, 53:482-485..
    • (2004) Diabetes , vol.53
    • Sasahara, M.1    Nishi, M.2    Kawashima, H.3


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