메뉴 건너뛰기




Volumn 102, Issue , 2015, Pages 270-275

Sarcolipin is a novel regulator of muscle metabolism and obesity

Author keywords

Energy expenditure; Muscle metabolism; Obesity; Sarcolipin; SERCA; Thermogenesis

Indexed keywords

ADENOSINE TRIPHOSPHATE; REGULATOR PROTEIN; SARCOLIPIN; UNCLASSIFIED DRUG; UNCOUPLING PROTEIN 1; MUSCLE PROTEIN; PROTEOLIPID; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE;

EID: 84946717956     PISSN: 10436618     EISSN: 10961186     Source Type: Journal    
DOI: 10.1016/j.phrs.2015.10.020     Document Type: Review
Times cited : (38)

References (85)
  • 1
    • 1842409029 scopus 로고    scopus 로고
    • Mice lacking mitochondrial uncoupling protein are cold-sensitive but not obese
    • S. Enerback, and et al. Mice lacking mitochondrial uncoupling protein are cold-sensitive but not obese Nature 387 6628 1997 90 94
    • (1997) Nature , vol.387 , Issue.6628 , pp. 90-94
    • Enerback, S.1
  • 2
    • 0347989317 scopus 로고    scopus 로고
    • Brown adipose tissue: Function and physiological significance
    • B. Cannon, and J. Nedergaard Brown adipose tissue: function and physiological significance Physiol. Rev. 84 1 2004 277 359
    • (2004) Physiol. Rev. , vol.84 , Issue.1 , pp. 277-359
    • Cannon, B.1    Nedergaard, J.2
  • 3
    • 84863229962 scopus 로고    scopus 로고
    • Cardiac natriuretic peptides act via p38 MAPK to induce the brown fat thermogenic program in mouse and human adipocytes
    • M. Bordicchia, and et al. Cardiac natriuretic peptides act via p38 MAPK to induce the brown fat thermogenic program in mouse and human adipocytes J. Clin. Invest. 122 3 2012 1022 1036
    • (2012) J. Clin. Invest. , vol.122 , Issue.3 , pp. 1022-1036
    • Bordicchia, M.1
  • 4
    • 58749091645 scopus 로고    scopus 로고
    • UCP1 ablation induces obesity and abolishes diet-induced thermogenesis in mice exempt from thermal stress by living at thermoneutrality
    • H.M. Feldmann, V. Golozoubova, B. Cannon, and J. Nedergaard UCP1 ablation induces obesity and abolishes diet-induced thermogenesis in mice exempt from thermal stress by living at thermoneutrality Cell Metab. 9 2 2009 203 209
    • (2009) Cell Metab. , vol.9 , Issue.2 , pp. 203-209
    • Feldmann, H.M.1    Golozoubova, V.2    Cannon, B.3    Nedergaard, J.4
  • 5
    • 0035210335 scopus 로고    scopus 로고
    • Life without UCP1: Mitochondrial, cellular and organismal characteristics of the UCP1-ablated mice
    • J. Nedergaard, and et al. Life without UCP1: mitochondrial, cellular and organismal characteristics of the UCP1-ablated mice Biochem. Soc. Trans. 29 Pt 6 2001 756 763
    • (2001) Biochem. Soc. Trans. , vol.29 , pp. 756-763
    • Nedergaard, J.1
  • 6
    • 84873854027 scopus 로고    scopus 로고
    • Brown adipose tissue regulates glucose homeostasis and insulin sensitivity
    • K.I. Stanford, and et al. Brown adipose tissue regulates glucose homeostasis and insulin sensitivity J. Clin. Invest. 123 1 2013 215 223
    • (2013) J. Clin. Invest. , vol.123 , Issue.1 , pp. 215-223
    • Stanford, K.I.1
  • 7
    • 0022388553 scopus 로고
    • Size analysis of uncoupling protein and its precursor from brown adipose tissue of different species
    • K.B. Freeman, K. Meyrick, H.V. Patel, and R.G. Ridley Size analysis of uncoupling protein and its precursor from brown adipose tissue of different species Can. J. Biochem. Cell Biol. 63 9 1985 988 991
    • (1985) Can. J. Biochem. Cell Biol. , vol.63 , Issue.9 , pp. 988-991
    • Freeman, K.B.1    Meyrick, K.2    Patel, H.V.3    Ridley, R.G.4
  • 8
    • 84924801832 scopus 로고    scopus 로고
    • Differential metabolism of brown adipose tissue in newborn rabbits in relation to position in the litter huddle
    • E. Garcia-Torres, and et al. Differential metabolism of brown adipose tissue in newborn rabbits in relation to position in the litter huddle J. Therm. Biol. 51 2015 33 41
    • (2015) J. Therm. Biol. , vol.51 , pp. 33-41
    • Garcia-Torres, E.1
  • 9
    • 0015042967 scopus 로고
    • The effect of environmental conditions on the growth and function of brown adipose tissue
    • M.J. Hardman, and D. Hull The effect of environmental conditions on the growth and function of brown adipose tissue J. Physiol. 214 2 1971 191 199
    • (1971) J. Physiol. , vol.214 , Issue.2 , pp. 191-199
    • Hardman, M.J.1    Hull, D.2
  • 10
    • 64349105205 scopus 로고    scopus 로고
    • Identification and importance of brown adipose tissue in adult humans
    • A.M. Cypess, and et al. Identification and importance of brown adipose tissue in adult humans N. Engl. J. Med. 360 15 2009 1509 1517
    • (2009) N. Engl. J. Med. , vol.360 , Issue.15 , pp. 1509-1517
    • Cypess, A.M.1
  • 11
    • 0025047553 scopus 로고
    • Skeletal muscle metabolism is a major determinant of resting energy expenditure
    • F. Zurlo, K. Larson, C. Bogardus, and E. Ravussin Skeletal muscle metabolism is a major determinant of resting energy expenditure J. Clin. Invest. 86 5 1990 1423 1427
    • (1990) J. Clin. Invest. , vol.86 , Issue.5 , pp. 1423-1427
    • Zurlo, F.1    Larson, K.2    Bogardus, C.3    Ravussin, E.4
  • 12
    • 84903184157 scopus 로고    scopus 로고
    • Sarcolipin provides a novel muscle-based mechanism for adaptive thermogenesis
    • D. Gamu, and et al. Sarcolipin provides a novel muscle-based mechanism for adaptive thermogenesis Exerc. Sport Sci. Rev. 42 3 2014 136 142
    • (2014) Exerc. Sport Sci. Rev. , vol.42 , Issue.3 , pp. 136-142
    • Gamu, D.1
  • 13
    • 0034611678 scopus 로고    scopus 로고
    • Towards a molecular understanding of adaptive thermogenesis
    • B.B. Lowell, and B.M. Spiegelman Towards a molecular understanding of adaptive thermogenesis Nature 404 6778 2000 652 660
    • (2000) Nature , vol.404 , Issue.6778 , pp. 652-660
    • Lowell, B.B.1    Spiegelman, B.M.2
  • 14
    • 84928406067 scopus 로고    scopus 로고
    • Sarcolipin is a key determinant of the basal metabolic rate, and its overexpression enhances energy expenditure and resistance against diet-induced obesity
    • S.K. Maurya, and et al. Sarcolipin is a key determinant of the basal metabolic rate, and its overexpression enhances energy expenditure and resistance against diet-induced obesity J. Biol. Chem. 290 17 2015 10840 10849
    • (2015) J. Biol. Chem. , vol.290 , Issue.17 , pp. 10840-10849
    • Maurya, S.K.1
  • 15
    • 84928341070 scopus 로고    scopus 로고
    • The role of skeletal-muscle-based thermogenic mechanisms in vertebrate endothermy
    • L.A. Rowland, N.C. Bal, and M. Periasamy The role of skeletal-muscle-based thermogenic mechanisms in vertebrate endothermy Biol. Rev. Camb. Philos. Soc. 2014
    • (2014) Biol. Rev. Camb. Philos. Soc.
    • Rowland, L.A.1    Bal, N.C.2    Periasamy, M.3
  • 16
    • 84870265848 scopus 로고    scopus 로고
    • Sarcolipin is a newly identified regulator of muscle-based thermogenesis in mammals
    • N.C. Bal, and et al. Sarcolipin is a newly identified regulator of muscle-based thermogenesis in mammals Nat. Med. 18 10 2012 1575 1579
    • (2012) Nat. Med. , vol.18 , Issue.10 , pp. 1575-1579
    • Bal, N.C.1
  • 17
    • 84929223175 scopus 로고    scopus 로고
    • Uncoupling protein 1 and sarcolipin are required to maintain optimal thermogenesis, and loss of both systems compromises survival of mice under cold stress
    • L.A. Rowland, N.C. Bal, L.P. Kozak, and M. Periasamy Uncoupling protein 1 and sarcolipin are required to maintain optimal thermogenesis, and loss of both systems compromises survival of mice under cold stress J. Biol. Chem. 290 19 2015 12282 12289
    • (2015) J. Biol. Chem. , vol.290 , Issue.19 , pp. 12282-12289
    • Rowland, L.A.1    Bal, N.C.2    Kozak, L.P.3    Periasamy, M.4
  • 18
    • 0024426107 scopus 로고
    • Epinephrine mediates facultative carbohydrate-induced thermogenesis in human skeletal muscle
    • A. Astrup, and et al. Epinephrine mediates facultative carbohydrate-induced thermogenesis in human skeletal muscle Am. J. Physiol. 257 Pt 1 1989 E340 E345
    • (1989) Am. J. Physiol. , vol.257 , pp. E340-E345
    • Astrup, A.1
  • 19
    • 0026443844 scopus 로고
    • Thermogenic response to epinephrine in the forearm and abdominal subcutaneous adipose tissue
    • L. Simonsen, J. Bulow, J. Madsen, and N.J. Christensen Thermogenic response to epinephrine in the forearm and abdominal subcutaneous adipose tissue Am. J. Physiol. 263 Pt 1 1992 E850 E855
    • (1992) Am. J. Physiol. , vol.263 , pp. E850-E855
    • Simonsen, L.1    Bulow, J.2    Madsen, J.3    Christensen, N.J.4
  • 20
    • 84888212859 scopus 로고    scopus 로고
    • Lipidomics analysis revealed the phospholipid compositional changes in muscle by chronic exercise and high-fat diet
    • N. Goto-Inoue, and et al. Lipidomics analysis revealed the phospholipid compositional changes in muscle by chronic exercise and high-fat diet Sci. Rep. 3 2013 3267
    • (2013) Sci. Rep. , vol.3 , pp. 3267
    • Goto-Inoue, N.1
  • 22
    • 84946796497 scopus 로고    scopus 로고
    • Role of PKCdelta in Insulin Sensitivity and Skeletal Muscle Metabolism
    • M. Li, and et al. Role of PKCdelta in Insulin Sensitivity and Skeletal Muscle Metabolism Diabetes 2015
    • (2015) Diabetes
    • Li, M.1
  • 23
    • 84883311340 scopus 로고    scopus 로고
    • Sarcolipin trumps beta-adrenergic receptor signaling as the favored mechanism for muscle-based diet-induced thermogenesis
    • E. Bombardier, and et al. Sarcolipin trumps beta-adrenergic receptor signaling as the favored mechanism for muscle-based diet-induced thermogenesis FASEB J. 27 9 2013 3078 3871
    • (2013) FASEB J. , vol.27 , Issue.9 , pp. 3078-3871
    • Bombardier, E.1
  • 24
    • 84879736175 scopus 로고    scopus 로고
    • 2+ pumps accounts for 40-50% of resting metabolic rate in mouse fast and slow twitch skeletal muscle
    • 2+ pumps accounts for 40-50% of resting metabolic rate in mouse fast and slow twitch skeletal muscle PLoS One 8 7 2013 e68924
    • (2013) PLoS One , vol.8 , Issue.7 , pp. e68924
    • Smith, I.C.1    Bombardier, E.2    Vigna, C.3    Tupling, A.R.4
  • 25
    • 84874846595 scopus 로고    scopus 로고
    • 2+ ATPase (SERCA) is distinct from phospholamban protein, and only sarcolipin can promote uncoupling of the SERCA pump
    • 2+ ATPase (SERCA) is distinct from phospholamban protein, and only sarcolipin can promote uncoupling of the SERCA pump J. Biol. Chem. 288 10 2013 6881 6889
    • (2013) J. Biol. Chem. , vol.288 , Issue.10 , pp. 6881-6889
    • Sahoo, S.K.1
  • 26
    • 33846026367 scopus 로고    scopus 로고
    • 2+-ATPase
    • 2+-ATPase J. Biol. Chem. 281 48 2006 36597 36602
    • (2006) J. Biol. Chem. , vol.281 , Issue.48 , pp. 36597-36602
    • Mall, S.1
  • 27
    • 84928310000 scopus 로고    scopus 로고
    • Sarcolipin overexpression improves muscle energetics and reduces fatigue
    • D.H. Sopariwala, and et al. Sarcolipin overexpression improves muscle energetics and reduces fatigue J. Appl. Physiol. (1985) 118 8 2015 1050 1058
    • (2015) J. Appl. Physiol. (1985) , vol.118 , Issue.8 , pp. 1050-1058
    • Sopariwala, D.H.1
  • 28
    • 84989156447 scopus 로고    scopus 로고
    • Persistence of diet-induced obesity despite access to voluntary activity in mice lacking sarcolipin
    • D. Gamu, A. Trinh, E. Bombardier, and A.R. Tupling Persistence of diet-induced obesity despite access to voluntary activity in mice lacking sarcolipin Physiol. Rep. 3 2015 9
    • (2015) Physiol. Rep. , vol.3 , pp. 9
    • Gamu, D.1    Trinh, A.2    Bombardier, E.3    Tupling, A.R.4
  • 29
    • 0014940130 scopus 로고
    • Purification and properties of an adenosine triphosphatase from sarcoplasmic reticulum
    • D.H. MacLennan Purification and properties of an adenosine triphosphatase from sarcoplasmic reticulum J. Biol. Chem. 245 17 1970 4508 4518
    • (1970) J. Biol. Chem. , vol.245 , Issue.17 , pp. 4508-4518
    • MacLennan, D.H.1
  • 30
    • 34047219171 scopus 로고    scopus 로고
    • SERCA pump isoforms: Their role in calcium transport and disease
    • M. Periasamy, and A. Kalyanasundaram SERCA pump isoforms: their role in calcium transport and disease Muscle Nerve 35 4 2007 430 442
    • (2007) Muscle Nerve , vol.35 , Issue.4 , pp. 430-442
    • Periasamy, M.1    Kalyanasundaram, A.2
  • 31
    • 0034961272 scopus 로고    scopus 로고
    • 2+ homeostasis and cardiac contractility
    • 2+ homeostasis and cardiac contractility J. Mol. Cell. Cardiol 33 6 2001 1053 1063
    • (2001) J. Mol. Cell. Cardiol , vol.33 , Issue.6 , pp. 1053-1063
    • Periasamy, M.1    Huke, S.2
  • 32
    • 0038464639 scopus 로고    scopus 로고
    • Phospholamban: a crucial regulator of cardiac contractility
    • D.H. MacLennan, and E.G. Kranias Phospholamban: a crucial regulator of cardiac contractility Nat. Rev. Mol. Cell Biol. 4 7 2003 566 577
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , Issue.7 , pp. 566-577
    • MacLennan, D.H.1    Kranias, E.G.2
  • 33
    • 0031722958 scopus 로고    scopus 로고
    • Phospholamban: Protein structure, mechanism of action, and role in cardiac function
    • H.K. Simmerman, and L.R. Jones Phospholamban: protein structure, mechanism of action, and role in cardiac function Physiol. Rev. 78 4 1998 921 947
    • (1998) Physiol. Rev. , vol.78 , Issue.4 , pp. 921-947
    • Simmerman, H.K.1    Jones, L.R.2
  • 34
    • 34447501977 scopus 로고    scopus 로고
    • Differential expression of sarcolipin protein during muscle development and cardiac pathophysiology
    • G.J. Babu, and et al. Differential expression of sarcolipin protein during muscle development and cardiac pathophysiology J. Mol. Cell. Cardiol. 43 2 2007 215 222
    • (2007) J. Mol. Cell. Cardiol. , vol.43 , Issue.2 , pp. 215-222
    • Babu, G.J.1
  • 35
    • 84890031164 scopus 로고    scopus 로고
    • 2+ uptake in skeletal muscles of mouse models of Duchenne muscular dystrophy
    • 2+ uptake in skeletal muscles of mouse models of Duchenne muscular dystrophy J. Muscle Res. Cell Motil. 34 5-6 2013 349 356
    • (2013) J. Muscle Res. Cell Motil. , vol.34 , Issue.5-6 , pp. 349-356
    • Schneider, J.S.1
  • 36
    • 84939551519 scopus 로고    scopus 로고
    • Phospholamban overexpression in mice causes a centronuclear myopathy-like phenotype
    • V.A. Fajardo, and et al. Phospholamban overexpression in mice causes a centronuclear myopathy-like phenotype Dis. Model Mech. 8 8 2015 999 1009
    • (2015) Dis. Model Mech. , vol.8 , Issue.8 , pp. 999-1009
    • Fajardo, V.A.1
  • 37
    • 0031281867 scopus 로고    scopus 로고
    • Characterization of the gene encoding human sarcolipin (SLN), a proteolipid associated with SERCA1: Absence of structural mutations in five patients with Brody disease
    • A. Odermatt, and et al. Characterization of the gene encoding human sarcolipin (SLN), a proteolipid associated with SERCA1: absence of structural mutations in five patients with Brody disease Genomics 45 3 1997 541 553
    • (1997) Genomics , vol.45 , Issue.3 , pp. 541-553
    • Odermatt, A.1
  • 39
    • 0014182854 scopus 로고
    • Contribution of skeletal muscle to nonshivering thermogenesis in the dog
    • T.R. Davis Contribution of skeletal muscle to nonshivering thermogenesis in the dog Am. J. Physiol. 213 6 1967 1423 1426
    • (1967) Am. J. Physiol. , vol.213 , Issue.6 , pp. 1423-1426
    • Davis, T.R.1
  • 40
    • 0025280990 scopus 로고
    • Increase in cytochrome oxidase capacity of BAT and other tissues in cold-acclimated gerbils
    • M. Bourhim, and et al. Increase in cytochrome oxidase capacity of BAT and other tissues in cold-acclimated gerbils Am. J. Physiol. 258 Pt 2 1990 R1291 R1298
    • (1990) Am. J. Physiol. , vol.258 , pp. R1291-R1298
    • Bourhim, M.1
  • 41
    • 0006382707 scopus 로고    scopus 로고
    • Potential for non-shivering thermogenesis in perfused chicken (Gallus domesticus) muscle
    • T.P. Eldershaw, and et al. Potential for non-shivering thermogenesis in perfused chicken (Gallus domesticus) muscle Comp. Biochem. Physiol. A Physiol. 117 4 1997 545 554
    • (1997) Comp. Biochem. Physiol. A Physiol. , vol.117 , Issue.4 , pp. 545-554
    • Eldershaw, T.P.1
  • 42
    • 0028314350 scopus 로고
    • Thermogenesis in muscle
    • B.A. Block Thermogenesis in muscle Annu. Rev. Physiol. 56 1994 535 577
    • (1994) Annu. Rev. Physiol. , vol.56 , pp. 535-577
    • Block, B.A.1
  • 43
    • 0024074964 scopus 로고
    • The structure of the membrane systems in a novel muscle cell modified for heat production
    • B.A. Block, and C. Franzini-Armstrong The structure of the membrane systems in a novel muscle cell modified for heat production J. Cell Biol. 107 3 1988 1099 1112
    • (1988) J. Cell Biol. , vol.107 , Issue.3 , pp. 1099-1112
    • Block, B.A.1    Franzini-Armstrong, C.2
  • 44
    • 0028089697 scopus 로고
    • Characterization of the sarcoplasmic reticulum proteins in the thermogenic muscles of fish
    • B.A. Block, J. O'Brien, and G. Meissner Characterization of the sarcoplasmic reticulum proteins in the thermogenic muscles of fish J. Cell Biol. 127 5 1994 1275 1287
    • (1994) J. Cell Biol. , vol.127 , Issue.5 , pp. 1275-1287
    • Block, B.A.1    O'Brien, J.2    Meissner, G.3
  • 45
    • 0037338934 scopus 로고    scopus 로고
    • 2+-ATPase isoforms in the thermogenic heater organ of blue marlin (Makaira nigricans)
    • 2+-ATPase isoforms in the thermogenic heater organ of blue marlin (Makaira nigricans) J. Exp. Biol. 206 Pt 5 2003 805 812
    • (2003) J. Exp. Biol. , vol.206 , pp. 805-812
    • Morrissette, J.M.1    Franck, J.P.2    Block, B.A.3
  • 46
    • 2342561101 scopus 로고    scopus 로고
    • 2+ on oxidative phosphorylation in mitochondria from the thermogenic organ of marlin
    • 2+ on oxidative phosphorylation in mitochondria from the thermogenic organ of marlin J. Exp. Biol. 199 Pt 12 1996 2679 2687
    • (1996) J. Exp. Biol. , vol.199 , pp. 2679-2687
    • O'Brien, J.1    Block, B.A.2
  • 47
    • 84925506798 scopus 로고    scopus 로고
    • The disorders of the calcium release unit of skeletal muscles: What have we learned from mouse models?
    • M. Canato, P. Capitanio, C. Reggiani, and L. Cancellara The disorders of the calcium release unit of skeletal muscles: what have we learned from mouse models? J. Muscle Res. Cell Motil. 36 1 2015 61 69
    • (2015) J. Muscle Res. Cell Motil. , vol.36 , Issue.1 , pp. 61-69
    • Canato, M.1    Capitanio, P.2    Reggiani, C.3    Cancellara, L.4
  • 48
  • 49
    • 0027296683 scopus 로고
    • 2+-ATPase and ryanodine receptor in cold-acclimated ducklings and thermogenesis
    • 2+-ATPase and ryanodine receptor in cold-acclimated ducklings and thermogenesis Am. J. Physiol. 265 Pt 1 1993 C507 C513
    • (1993) Am. J. Physiol. , vol.265 , pp. C507-C513
    • Dumonteil, E.1    Barre, H.2    Meissner, G.3
  • 53
    • 57349198716 scopus 로고    scopus 로고
    • 2+ ATPase isoform 1 heat production
    • 2+ ATPase isoform 1 heat production Endocrinology 149 12 2008 6262 6271
    • (2008) Endocrinology , vol.149 , Issue.12 , pp. 6262-6271
    • Arruda, A.P.1
  • 55
    • 84930226879 scopus 로고    scopus 로고
    • 2+ transport
    • 2+ transport J. Biol. Chem. 290 22 2015 14057 14067
    • (2015) J. Biol. Chem. , vol.290 , Issue.22 , pp. 14057-14067
    • Sahoo, S.K.1
  • 56
    • 84874994481 scopus 로고    scopus 로고
    • The sarcolipin-bound calcium pump stabilizes calcium sites exposed to the cytoplasm
    • A.M. Winther, and et al. The sarcolipin-bound calcium pump stabilizes calcium sites exposed to the cytoplasm Nature 495 7440 2013 265 269
    • (2013) Nature , vol.495 , Issue.7440 , pp. 265-269
    • Winther, A.M.1
  • 57
    • 84874957001 scopus 로고    scopus 로고
    • 2+-bound E1 state
    • 2+-bound E1 state Nature 495 7440 2013 260 264
    • (2013) Nature , vol.495 , Issue.7440 , pp. 260-264
    • Toyoshima, C.1
  • 58
    • 84875448440 scopus 로고    scopus 로고
    • Sarco(endo) plasmic reticulum calcium ATPase (SERCA) inhibition by sarcolipin is encoded in its luminal tail
    • P.A. Gorski, J.P. Glaves, P. Vangheluwe, and H.S. Young Sarco(endo) plasmic reticulum calcium ATPase (SERCA) inhibition by sarcolipin is encoded in its luminal tail J. Biol. Chem. 288 12 2013 8456 8467
    • (2013) J. Biol. Chem. , vol.288 , Issue.12 , pp. 8456-8467
    • Gorski, P.A.1    Glaves, J.P.2    Vangheluwe, P.3    Young, H.S.4
  • 59
    • 84878215698 scopus 로고    scopus 로고
    • 2+-ATPases in resting skeletal muscle
    • 2+-ATPases in resting skeletal muscle FEBS Lett. 587 11 2013 1687 1692
    • (2013) FEBS Lett. , vol.587 , Issue.11 , pp. 1687-1692
    • Bombardier, E.1
  • 61
    • 36749060047 scopus 로고    scopus 로고
    • Ablation of sarcolipin enhances sarcoplasmic reticulum calcium transport and atrial contractility
    • G.J. Babu, and et al. Ablation of sarcolipin enhances sarcoplasmic reticulum calcium transport and atrial contractility Proc. Natl. Acad. Sci. U. S. A. 104 45 2007 17867 17872
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , Issue.45 , pp. 17867-17872
    • Babu, G.J.1
  • 62
    • 84870270479 scopus 로고    scopus 로고
    • Heat from calcium cycling melts fat
    • L.P. Kozak, and M.E. Young Heat from calcium cycling melts fat Nat. Med. 18 10 2012 1458 1459
    • (2012) Nat. Med. , vol.18 , Issue.10 , pp. 1458-1459
    • Kozak, L.P.1    Young, M.E.2
  • 63
    • 0030044236 scopus 로고    scopus 로고
    • Calcium activation of mitochondrial glycerol phosphate dehydrogenase restudied
    • M.J. MacDonald, and L.J. Brown Calcium activation of mitochondrial glycerol phosphate dehydrogenase restudied Arch. Biochem. Biophys. 326 1 1996 79 84
    • (1996) Arch. Biochem. Biophys. , vol.326 , Issue.1 , pp. 79-84
    • MacDonald, M.J.1    Brown, L.J.2
  • 64
    • 33644546383 scopus 로고    scopus 로고
    • Mitochondrial matrix phosphoproteome: Effect of extra mitochondrial calcium
    • R.K. Hopper, and et al. Mitochondrial matrix phosphoproteome: effect of extra mitochondrial calcium Biochemistry 45 8 2006 2524 2536
    • (2006) Biochemistry , vol.45 , Issue.8 , pp. 2524-2536
    • Hopper, R.K.1
  • 65
    • 0030581291 scopus 로고    scopus 로고
    • Mitochondrial ATP synthase F1-beta-subunit is a calcium-binding protein
    • M.J. Hubbard, and N.J. McHugh Mitochondrial ATP synthase F1-beta-subunit is a calcium-binding protein FEBS Lett. 391 3 1996 323 329
    • (1996) FEBS Lett. , vol.391 , Issue.3 , pp. 323-329
    • Hubbard, M.J.1    McHugh, N.J.2
  • 66
    • 34250201078 scopus 로고    scopus 로고
    • 2+-dependent interaction of S100A1 with F1-ATPase leads to an increased ATP content in cardiomyocytes
    • 2+-dependent interaction of S100A1 with F1-ATPase leads to an increased ATP content in cardiomyocytes Mol. Cell. Biol. 27 12 2007 4365 4373
    • (2007) Mol. Cell. Biol. , vol.27 , Issue.12 , pp. 4365-4373
    • Boerries, M.1
  • 68
    • 0032169351 scopus 로고    scopus 로고
    • Integrating cytosolic calcium signals into mitochondrial metabolic responses
    • L.D. Robb-Gaspers, and et al. Integrating cytosolic calcium signals into mitochondrial metabolic responses EMBO J. 17 17 1998 4987 5000
    • (1998) EMBO J. , vol.17 , Issue.17 , pp. 4987-5000
    • Robb-Gaspers, L.D.1
  • 69
    • 0033598828 scopus 로고    scopus 로고
    • Regulation of mitochondrial ATP synthesis by calcium: Evidence for a long-term metabolic priming
    • L.S. Jouaville, and et al. Regulation of mitochondrial ATP synthesis by calcium: evidence for a long-term metabolic priming Proc. Natl. Acad. Sci. U. S. A. 96 24 1999 13807 13812
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , Issue.24 , pp. 13807-13812
    • Jouaville, L.S.1
  • 71
    • 80054995362 scopus 로고    scopus 로고
    • 2+-calmodulin-dependent proteins for skeletal muscle plasticity
    • 2+-calmodulin-dependent proteins for skeletal muscle plasticity J. Physiol. 589 Pt 21 2011 5021 5031
    • (2011) J. Physiol. , vol.589 , pp. 5021-5031
    • Tavi, P.1    Westerblad, H.2
  • 72
    • 0037102256 scopus 로고    scopus 로고
    • Transcriptional co-activator PGC-1 alpha drives the formation of slow-twitch muscle fibres
    • J. Lin, and et al. Transcriptional co-activator PGC-1 alpha drives the formation of slow-twitch muscle fibres Nature 418 6899 2002 797 801
    • (2002) Nature , vol.418 , Issue.6899 , pp. 797-801
    • Lin, J.1
  • 73
    • 0037322888 scopus 로고    scopus 로고
    • Exercise induces transient transcriptional activation of the PGC-1alpha gene in human skeletal muscle
    • H. Pilegaard, B. Saltin, and P.D. Neufer Exercise induces transient transcriptional activation of the PGC-1alpha gene in human skeletal muscle J. Physiol. 546 Pt 3 2003 851 858
    • (2003) J. Physiol. , vol.546 , pp. 851-858
    • Pilegaard, H.1    Saltin, B.2    Neufer, P.D.3
  • 75
    • 4544355935 scopus 로고    scopus 로고
    • Calcineurin and calcium/calmodulin-dependent protein kinase activate distinct metabolic gene regulatory programs in cardiac muscle
    • P.J. Schaeffer, and et al. Calcineurin and calcium/calmodulin-dependent protein kinase activate distinct metabolic gene regulatory programs in cardiac muscle J. Biol. Chem. 279 38 2004 39593 39603
    • (2004) J. Biol. Chem. , vol.279 , Issue.38 , pp. 39593-39603
    • Schaeffer, P.J.1
  • 76
    • 0033372915 scopus 로고    scopus 로고
    • Uncoupling protein - a useful energy dissipator
    • M. Klingenberg Uncoupling protein - a useful energy dissipator J. Bioenerg. Biomembr. 31 5 1999 419 430
    • (1999) J. Bioenerg. Biomembr. , vol.31 , Issue.5 , pp. 419-430
    • Klingenberg, M.1
  • 77
    • 0018964918 scopus 로고
    • Increased proton conductance pathway in brown adipose tissue mitochondria of rats exhibiting diet-induced thermogenesis
    • S.L. Brooks, and et al. Increased proton conductance pathway in brown adipose tissue mitochondria of rats exhibiting diet-induced thermogenesis Nature 286 5770 1980 274 276
    • (1980) Nature , vol.286 , Issue.5770 , pp. 274-276
    • Brooks, S.L.1
  • 78
    • 0020682957 scopus 로고
    • Effect of sucrose overfeeding on brown adipose tissue lipogenesis and lipoprotein lipase activity in rats
    • J.G. Granneman, and G.N. Wade Effect of sucrose overfeeding on brown adipose tissue lipogenesis and lipoprotein lipase activity in rats Metabolism 32 2 1983 202 207
    • (1983) Metabolism , vol.32 , Issue.2 , pp. 202-207
    • Granneman, J.G.1    Wade, G.N.2
  • 79
    • 0034668852 scopus 로고    scopus 로고
    • Mitochondrial uncoupling proteins: from mitochondria to the regulation of energy balance
    • D. Ricquier, and F. Bouillaud Mitochondrial uncoupling proteins: from mitochondria to the regulation of energy balance J. Physiol. 529 Pt 1 2000 3 10
    • (2000) J. Physiol. , vol.529 , pp. 3-10
    • Ricquier, D.1    Bouillaud, F.2
  • 80
    • 0020619526 scopus 로고
    • Effects of dietary essential fatty acids on active thermogenin content in rat brown adipose tissue
    • J. Nedergaard, W. Becker, and B. Cannon Effects of dietary essential fatty acids on active thermogenin content in rat brown adipose tissue J. Nutr. 113 9 1983 1717 1724
    • (1983) J. Nutr. , vol.113 , Issue.9 , pp. 1717-1724
    • Nedergaard, J.1    Becker, W.2    Cannon, B.3
  • 81
    • 84856529575 scopus 로고    scopus 로고
    • Brown adipose tissue oxidative metabolism contributes to energy expenditure during acute cold exposure in humans
    • V. Ouellet, and et al. Brown adipose tissue oxidative metabolism contributes to energy expenditure during acute cold exposure in humans J. Clin. Invest. 122 2 2012 545 552
    • (2012) J. Clin. Invest. , vol.122 , Issue.2 , pp. 545-552
    • Ouellet, V.1
  • 82
    • 0018646453 scopus 로고
    • A role for brown adipose tissue in diet-induced thermogenesis
    • N.J. Rothwell, and M.J. Stock A role for brown adipose tissue in diet-induced thermogenesis Nature 281 5726 1979 31 35
    • (1979) Nature , vol.281 , Issue.5726 , pp. 31-35
    • Rothwell, N.J.1    Stock, M.J.2
  • 83
    • 84962076500 scopus 로고    scopus 로고
    • Brown and Beige fat: Molecular parts of a thermogenic machine
    • P. Cohen, and B.M. Spiegelman Brown and Beige fat: molecular parts of a thermogenic machine Diabetes 64 7 2015 2346 2351
    • (2015) Diabetes , vol.64 , Issue.7 , pp. 2346-2351
    • Cohen, P.1    Spiegelman, B.M.2
  • 84
    • 84864287504 scopus 로고    scopus 로고
    • Beige adipocytes are a distinct type of thermogenic fat cell in mouse and human
    • J. Wu, and et al. Beige adipocytes are a distinct type of thermogenic fat cell in mouse and human Cell 150 2 2012 366 376
    • (2012) Cell , vol.150 , Issue.2 , pp. 366-376
    • Wu, J.1
  • 85
    • 84873518501 scopus 로고    scopus 로고
    • Adaptive thermogenesis in adipocytes: Is beige the new brown?
    • J. Wu, P. Cohen, and B.M. Spiegelman Adaptive thermogenesis in adipocytes: is beige the new brown? Genes Dev. 27 3 2013 234 250
    • (2013) Genes Dev. , vol.27 , Issue.3 , pp. 234-250
    • Wu, J.1    Cohen, P.2    Spiegelman, B.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.