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Volumn 1, Issue 3, 2006, Pages 365-374

Thermal sensitivity of uncoupling protein expression in polar and temperate fish

Author keywords

Antarctic fish; Mitochondrial energy metabolism; Temperature acclimation; Uncoupling proteins; Warm stress; Zoarcidae

Indexed keywords

COMPLEMENTARY DNA; MESSENGER RNA; MITOCHONDRIAL PROTEIN; PROTON; UNCOUPLING PROTEIN; UNCOUPLING PROTEIN 1; UNCOUPLING PROTEIN 2; UNCOUPLING PROTEIN 3;

EID: 33749142720     PISSN: 1744117X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbd.2006.08.004     Document Type: Article
Times cited : (50)

References (54)
  • 1
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 2
    • 0033785071 scopus 로고    scopus 로고
    • Uncoupling to survive? The role of mitochondrial inefficiency in ageing
    • Brand M.D. Uncoupling to survive? The role of mitochondrial inefficiency in ageing. Exp. Gerontol. 35 (2000) 811-820
    • (2000) Exp. Gerontol. , vol.35 , pp. 811-820
    • Brand, M.D.1
  • 3
    • 33845349500 scopus 로고    scopus 로고
    • Brodte, E., Knust, R., Pörtner, H.O., in press. Temperature dependent energy allocation to growth in Antarctic and boreal eelpout (Zoarcidae). Polar Biol. (doi:10.1007/s00300-006-0165-ys).
  • 4
    • 0034603760 scopus 로고    scopus 로고
    • First evidence of uncoupling protein-2 (UCP-2) and -3 (UCP-3) gene expression in piglet skeletal muscle and adipose tissue
    • Damon M., Vincent A., Lombardi A., and Herpin P. First evidence of uncoupling protein-2 (UCP-2) and -3 (UCP-3) gene expression in piglet skeletal muscle and adipose tissue. Gene 246 (2000) 133-141
    • (2000) Gene , vol.246 , pp. 133-141
    • Damon, M.1    Vincent, A.2    Lombardi, A.3    Herpin, P.4
  • 5
    • 33747063768 scopus 로고    scopus 로고
    • Mitochondrial proton leak rates in the slow, oxidative myotomal muscle and liver of the endothermic shortfin mako shark (Isurus oxyrinchus) and the ectothermic blue shark (Prionace glauca) and leopard shark (Triakis semifasciata)
    • Duong C.A., Sepulveda C.A., Graham J.B., and Dickson K.A. Mitochondrial proton leak rates in the slow, oxidative myotomal muscle and liver of the endothermic shortfin mako shark (Isurus oxyrinchus) and the ectothermic blue shark (Prionace glauca) and leopard shark (Triakis semifasciata). J. Exp. Biol. 209 (2006) 2678-2685
    • (2006) J. Exp. Biol. , vol.209 , pp. 2678-2685
    • Duong, C.A.1    Sepulveda, C.A.2    Graham, J.B.3    Dickson, K.A.4
  • 7
    • 0032530086 scopus 로고    scopus 로고
    • Hot spots in cold adaptation: localized increases in conformational flexibility in lactate dehydrogenase A4 orthologs of Antarctic notothenioid fishes
    • Fields P.A., and Somero G.N. Hot spots in cold adaptation: localized increases in conformational flexibility in lactate dehydrogenase A4 orthologs of Antarctic notothenioid fishes. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 11476-11481
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 11476-11481
    • Fields, P.A.1    Somero, G.N.2
  • 9
    • 0035994697 scopus 로고    scopus 로고
    • Going with the flow or life in the fast lane: contrasting mitochondrial responses to thermal change
    • Guderley H., and St-Pierre J. Going with the flow or life in the fast lane: contrasting mitochondrial responses to thermal change. J. Exp. Biol. 205 (2002) 2237
    • (2002) J. Exp. Biol. , vol.205 , pp. 2237
    • Guderley, H.1    St-Pierre, J.2
  • 10
    • 0033402862 scopus 로고    scopus 로고
    • Thermal sensitivity of mitochondrial function in the Antarctic notothenioid Lepidonotothen nudifrons
    • Hardewig I., Peck L.S., and Pörtner H.O. Thermal sensitivity of mitochondrial function in the Antarctic notothenioid Lepidonotothen nudifrons. J. Comp. Physiol. B 169 (1999) 597-604
    • (1999) J. Comp. Physiol. B , vol.169 , pp. 597-604
    • Hardewig, I.1    Peck, L.S.2    Pörtner, H.O.3
  • 11
    • 0032878318 scopus 로고    scopus 로고
    • Temperature-dependent expression of cytochrome-c oxidase in Antarctic and temperate fish
    • Hardewig I., Van Dijk P.L.M., Moyes C.D., and Pörtner H.O. Temperature-dependent expression of cytochrome-c oxidase in Antarctic and temperate fish. Am. J. Physiol. 277 (1999) R508-R516
    • (1999) Am. J. Physiol. , vol.277
    • Hardewig, I.1    Van Dijk, P.L.M.2    Moyes, C.D.3    Pörtner, H.O.4
  • 14
    • 2342527243 scopus 로고    scopus 로고
    • The plant uncoupling protein homologues: a new family of energy-dissipating proteins in plant mitochondria
    • Hourton-Cabassa C., Rita Matos A., Zachowski A., and Moreau F. The plant uncoupling protein homologues: a new family of energy-dissipating proteins in plant mitochondria. Plant Physiol. Biochem. 42 (2004) 283-290
    • (2004) Plant Physiol. Biochem. , vol.42 , pp. 283-290
    • Hourton-Cabassa, C.1    Rita Matos, A.2    Zachowski, A.3    Moreau, F.4
  • 15
    • 0038053908 scopus 로고    scopus 로고
    • Proton translocation by transhydrogenase
    • Jackson J.B. Proton translocation by transhydrogenase. FEBS Lett. 545 (2003) 18-24
    • (2003) FEBS Lett. , vol.545 , pp. 18-24
    • Jackson, J.B.1
  • 16
    • 0033551842 scopus 로고    scopus 로고
    • Identification and characterization of a protozoan uncoupling protein in Acanthamoeba castellanii
    • Jarmuszkiewicz W., Sluse-Goffart C.M., Hryniewiecka L., and Sluse F.E. Identification and characterization of a protozoan uncoupling protein in Acanthamoeba castellanii. J. Biol. Chem. 274 (1999) 23198-23202
    • (1999) J. Biol. Chem. , vol.274 , pp. 23198-23202
    • Jarmuszkiewicz, W.1    Sluse-Goffart, C.M.2    Hryniewiecka, L.3    Sluse, F.E.4
  • 17
    • 0033980875 scopus 로고    scopus 로고
    • First evidence and characterization of an uncoupling protein in fungi kingdom: CpUCP of Candida parapsilosis
    • Jarmuszkiewicz W., Milani G., Fortes F., Schreiber A.Z., Sluse F.E., and Vercesi A.E. First evidence and characterization of an uncoupling protein in fungi kingdom: CpUCP of Candida parapsilosis. FEBS Lett. 467 (2000) 145-149
    • (2000) FEBS Lett. , vol.467 , pp. 145-149
    • Jarmuszkiewicz, W.1    Milani, G.2    Fortes, F.3    Schreiber, A.Z.4    Sluse, F.E.5    Vercesi, A.E.6
  • 18
    • 3042693356 scopus 로고    scopus 로고
    • The effect of growth at low temperature on the activity and expression of the uncoupling protein in Acanthamoeba castellanii mitochondria
    • Jarmuszkiewicz W., Antos N., Swida A., Czarna M., and Sluse F.E. The effect of growth at low temperature on the activity and expression of the uncoupling protein in Acanthamoeba castellanii mitochondria. FEBS Lett. 569 (2004) 178-184
    • (2004) FEBS Lett. , vol.569 , pp. 178-184
    • Jarmuszkiewicz, W.1    Antos, N.2    Swida, A.3    Czarna, M.4    Sluse, F.E.5
  • 19
    • 3142659657 scopus 로고    scopus 로고
    • Uncoupling protein 2 and 3 in marsupials: identification, phylogeny, and gene expression in response to cold and fasting in Antechinus flavipes
    • Jastroch M., Withers K., and Klingenspor M. Uncoupling protein 2 and 3 in marsupials: identification, phylogeny, and gene expression in response to cold and fasting in Antechinus flavipes. Physiol. Genomics 17 (2004) 130-139
    • (2004) Physiol. Genomics , vol.17 , pp. 130-139
    • Jastroch, M.1    Withers, K.2    Klingenspor, M.3
  • 20
    • 25144489463 scopus 로고    scopus 로고
    • Uncoupling protein 1 in fish uncovers an ancient evolutionary history of mammalian nonshivering thermogenesis
    • Jastroch M., Wuertz S., Kloas W., and Klingenspor M. Uncoupling protein 1 in fish uncovers an ancient evolutionary history of mammalian nonshivering thermogenesis. Physiol. Genomics 22 (2005) 150-156
    • (2005) Physiol. Genomics , vol.22 , pp. 150-156
    • Jastroch, M.1    Wuertz, S.2    Kloas, W.3    Klingenspor, M.4
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 4644221310 scopus 로고    scopus 로고
    • Oxygen limitation of thermal tolerance in cod, Gadus morhua L., studied by magnetic resonance imaging and on-line venous oxygen monitoring
    • Lannig G., Bock C., Sartoris F.J., and Pörtner H.O. Oxygen limitation of thermal tolerance in cod, Gadus morhua L., studied by magnetic resonance imaging and on-line venous oxygen monitoring. Am. J. Physiol. 287 (2004) R902-R910
    • (2004) Am. J. Physiol. , vol.287
    • Lannig, G.1    Bock, C.2    Sartoris, F.J.3    Pörtner, H.O.4
  • 24
    • 21744434370 scopus 로고    scopus 로고
    • Aerobic mitochondrial capacities in Antarctic and temperate eelpout (Zoarcidae) subjected to warm versus cold acclimation
    • Lannig G., Storch D., and Pörtner H.O. Aerobic mitochondrial capacities in Antarctic and temperate eelpout (Zoarcidae) subjected to warm versus cold acclimation. Polar Biol. 28 (2005) 575-584
    • (2005) Polar Biol. , vol.28 , pp. 575-584
    • Lannig, G.1    Storch, D.2    Pörtner, H.O.3
  • 26
    • 0344851925 scopus 로고    scopus 로고
    • Mitochondrial proliferation in the permanent vs. temporary cold: enzyme activities and mRNA levels in Antarctic and temperate zoarcid fish
    • Lucassen M., Schmidt A., Eckerle L.G., and Pörtner H.O. Mitochondrial proliferation in the permanent vs. temporary cold: enzyme activities and mRNA levels in Antarctic and temperate zoarcid fish. Am. J. Physiol. 285 (2003) R1410-R1420
    • (2003) Am. J. Physiol. , vol.285
    • Lucassen, M.1    Schmidt, A.2    Eckerle, L.G.3    Pörtner, H.O.4
  • 27
    • 33749139113 scopus 로고    scopus 로고
    • +-ATPase in temperate versus cold-adapted fish.
  • 30
    • 0035815650 scopus 로고    scopus 로고
    • Transcriptional regulation of the mouse uncoupling protein-2 gene. Double E-box motif is required for peroxisome proliferator-activated receptor-gamma-dependent activation
    • Medvedev A.V., Snedden S.K., Raimbault S., Ricquier D., and Collins S. Transcriptional regulation of the mouse uncoupling protein-2 gene. Double E-box motif is required for peroxisome proliferator-activated receptor-gamma-dependent activation. J. Biol. Chem. 276 (2001) 10817-10823
    • (2001) J. Biol. Chem. , vol.276 , pp. 10817-10823
    • Medvedev, A.V.1    Snedden, S.K.2    Raimbault, S.3    Ricquier, D.4    Collins, S.5
  • 31
    • 0037088649 scopus 로고    scopus 로고
    • Mechanism for peroxisome proliferator-activated receptor-alpha activator-induced up-regulation of UCP2 mRNA in rodent hepatocytes
    • Nakatani T., Tsuboyama-Kasaoka N., Takahashi M., Miura S., and Ezaki O. Mechanism for peroxisome proliferator-activated receptor-alpha activator-induced up-regulation of UCP2 mRNA in rodent hepatocytes. J. Biol. Chem. 277 (2002) 9562-9569
    • (2002) J. Biol. Chem. , vol.277 , pp. 9562-9569
    • Nakatani, T.1    Tsuboyama-Kasaoka, N.2    Takahashi, M.3    Miura, S.4    Ezaki, O.5
  • 32
    • 0017927437 scopus 로고
    • The identification of the component in the inner membrane of brown adipose tissue mitochondria responsible for regulating energy dissipation
    • Nicholls D.G., Bernson V.S., and Heaton G.M. The identification of the component in the inner membrane of brown adipose tissue mitochondria responsible for regulating energy dissipation. Experientia, Suppl. 32 (1978) 89-93
    • (1978) Experientia, Suppl. , vol.32 , pp. 89-93
    • Nicholls, D.G.1    Bernson, V.S.2    Heaton, G.M.3
  • 34
    • 0035282777 scopus 로고    scopus 로고
    • Mitochondrial proton leak: a role for uncoupling proteins 2 and 3?
    • Porter R.K. Mitochondrial proton leak: a role for uncoupling proteins 2 and 3?. Biochim. Biophys. Acta 1504 (2001) 120-127
    • (2001) Biochim. Biophys. Acta , vol.1504 , pp. 120-127
    • Porter, R.K.1
  • 35
    • 0035994688 scopus 로고    scopus 로고
    • Physiological basis of temperature-dependent biogeography: trade-offs in muscle design and performance in polar ectotherms
    • Pörtner H.O. Physiological basis of temperature-dependent biogeography: trade-offs in muscle design and performance in polar ectotherms. J. Exp. Biol. 205 (2002) 2217-2230
    • (2002) J. Exp. Biol. , vol.205 , pp. 2217-2230
    • Pörtner, H.O.1
  • 36
    • 0001505995 scopus 로고    scopus 로고
    • Levels of metabolic cold adaptation: tradeoffs in eurythermal and stenothermal ectotherms
    • Davison W., and Williams C.W. (Eds), Caxton Press, Christchurch, New Zealand
    • Pörtner H.O., van Dijk P.L.M., Hardewig I., and Sommer A. Levels of metabolic cold adaptation: tradeoffs in eurythermal and stenothermal ectotherms. In: Davison W., and Williams C.W. (Eds). Antarctic Ecosystems: Models for a Wider Understanding (2000), Caxton Press, Christchurch, New Zealand 109-122
    • (2000) Antarctic Ecosystems: Models for a Wider Understanding , pp. 109-122
    • Pörtner, H.O.1    van Dijk, P.L.M.2    Hardewig, I.3    Sommer, A.4
  • 37
    • 77956767461 scopus 로고    scopus 로고
    • Metabolic biochemistry: its role in thermal tolerance and in the capacities of physiological and ecological function
    • Farrell A.P., and Steffensen J.F. (Eds), Elsevier Academic Press, San Diego
    • Pörtner H.O., Lucassen M., and Storch D. Metabolic biochemistry: its role in thermal tolerance and in the capacities of physiological and ecological function. In: Farrell A.P., and Steffensen J.F. (Eds). The Physiology of Polar Fishes vol. 21 (2005), Elsevier Academic Press, San Diego 79-154
    • (2005) The Physiology of Polar Fishes , vol.21 , pp. 79-154
    • Pörtner, H.O.1    Lucassen, M.2    Storch, D.3
  • 40
    • 0034650763 scopus 로고    scopus 로고
    • The uncoupling protein homologues: UCP1, UCP2, UCP3, StUCP and AtUCP
    • Ricquier D., and Bouillaud F. The uncoupling protein homologues: UCP1, UCP2, UCP3, StUCP and AtUCP. Biochem. J. 345 Pt 2 (2000) 161-179
    • (2000) Biochem. J. , vol.345 , Issue.PART 2 , pp. 161-179
    • Ricquier, D.1    Bouillaud, F.2
  • 41
    • 0030573675 scopus 로고    scopus 로고
    • Proton leak and control of oxidative phosphorylation in perfused, resting rat skeletal muscle
    • Rolfe D.F., and Brand M.D. Proton leak and control of oxidative phosphorylation in perfused, resting rat skeletal muscle. Biochim. Biophys. Acta 1276 (1996) 45-50
    • (1996) Biochim. Biophys. Acta , vol.1276 , pp. 45-50
    • Rolfe, D.F.1    Brand, M.D.2
  • 42
    • 0032953969 scopus 로고    scopus 로고
    • Contribution of mitochondrial proton leak to respiration rate in working skeletal muscle and liver and to SMR
    • Rolfe D.F., Newman J.M., Buckingham J.A., Clark M.G., and Brand M.D. Contribution of mitochondrial proton leak to respiration rate in working skeletal muscle and liver and to SMR. Am. J. Physiol. 276 (1999) C692-C699
    • (1999) Am. J. Physiol. , vol.276
    • Rolfe, D.F.1    Newman, J.M.2    Buckingham, J.A.3    Clark, M.G.4    Brand, M.D.5
  • 44
    • 0032564864 scopus 로고    scopus 로고
    • Uncoupling: new approaches to an old problem of bioenergetics
    • Skulachev V.P. Uncoupling: new approaches to an old problem of bioenergetics. Biochim. Biophys. Acta, Bioenerg. 1363 (1998) 100-124
    • (1998) Biochim. Biophys. Acta, Bioenerg. , vol.1363 , pp. 100-124
    • Skulachev, V.P.1
  • 45
    • 11844255438 scopus 로고    scopus 로고
    • Evolution of mitochondrial uncoupling proteins: novel invertebrate UCP homologues suggest early evolutionary divergence of the UCP family
    • Sokolova I.M., and Sokolov E.P. Evolution of mitochondrial uncoupling proteins: novel invertebrate UCP homologues suggest early evolutionary divergence of the UCP family. FEBS Lett. 579 (2005) 313-317
    • (2005) FEBS Lett. , vol.579 , pp. 313-317
    • Sokolova, I.M.1    Sokolov, E.P.2
  • 46
    • 0014202437 scopus 로고
    • Temperature tolerance of some Antarctic fishes
    • Somero G.N., and DeVries A.L. Temperature tolerance of some Antarctic fishes. Science 156 (1967) 257-258
    • (1967) Science , vol.156 , pp. 257-258
    • Somero, G.N.1    DeVries, A.L.2
  • 47
    • 0033793299 scopus 로고    scopus 로고
    • Muscle temperature in free-swimming giant Atlantic bluefin tuna (Thunnus thynnus L.)
    • Stevens E.D., Kanwisher J.W., and Carey F.G. Muscle temperature in free-swimming giant Atlantic bluefin tuna (Thunnus thynnus L.). J. Therm. Biol. 25 (2000) 419-423
    • (2000) J. Therm. Biol. , vol.25 , pp. 419-423
    • Stevens, E.D.1    Kanwisher, J.W.2    Carey, F.G.3
  • 48
  • 49
    • 4043178347 scopus 로고    scopus 로고
    • Uncoupling protein and ATP/ADP carrier increase mitochondrial proton conductance after cold adaptation of king penguins
    • Talbot D.A., Duchamp C., Rey B., Hanuise N., Rouanet J.L., Sibille B., and Brand M. Uncoupling protein and ATP/ADP carrier increase mitochondrial proton conductance after cold adaptation of king penguins. J. Physiol. 558 (2004) 123-135
    • (2004) J. Physiol. , vol.558 , pp. 123-135
    • Talbot, D.A.1    Duchamp, C.2    Rey, B.3    Hanuise, N.4    Rouanet, J.L.5    Sibille, B.6    Brand, M.7
  • 51
    • 0000038790 scopus 로고
    • The mitochondrial transporter family
    • Walker J.E. The mitochondrial transporter family. Curr. Opin. Struct. Biol. 2 (1992) 519-526
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 519-526
    • Walker, J.E.1
  • 52
    • 0019873865 scopus 로고
    • Temperature adaptation of biological membranes: compensation of the molar activity of cytochrome c oxidase in the mitochondrial energy-transducing membrane during thermal acclimation of the carp (Cyprinus carpio L.)
    • Wodtke E. Temperature adaptation of biological membranes: compensation of the molar activity of cytochrome c oxidase in the mitochondrial energy-transducing membrane during thermal acclimation of the carp (Cyprinus carpio L.). Biochim. Biophys. Acta 640 (1981) 710-720
    • (1981) Biochim. Biophys. Acta , vol.640 , pp. 710-720
    • Wodtke, E.1
  • 53
    • 0019873861 scopus 로고
    • Temperature adaptation of biological membranes. The effects of acclimation temperature on the unsaturation of the main neutral and charged phospholipids in mitochondrial membranes of the carp (Cyprinus carpio L.)
    • Wodtke E. Temperature adaptation of biological membranes. The effects of acclimation temperature on the unsaturation of the main neutral and charged phospholipids in mitochondrial membranes of the carp (Cyprinus carpio L.). Biochim. Biophys. Acta 640 (1981) 698-709
    • (1981) Biochim. Biophys. Acta , vol.640 , pp. 698-709
    • Wodtke, E.1
  • 54
    • 0342614207 scopus 로고    scopus 로고
    • The mechanisms of fatty acid-induced proton permeability of the inner mitochondrial membrane
    • Wojtczak L., and Wiecedilckowski M.R. The mechanisms of fatty acid-induced proton permeability of the inner mitochondrial membrane. J. Bioenerg. Biomembranes 31 (1999) 447-455
    • (1999) J. Bioenerg. Biomembranes , vol.31 , pp. 447-455
    • Wojtczak, L.1    Wiecedilckowski, M.R.2


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