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Volumn 26, Issue 2, 2015, Pages 184-189

Skeletal muscle Sirt3 expression and mitochondrial respiration are regulated by a prenatal low-protein diet

Author keywords

Maternal low protein diet; Mitochondria; SDH; SIRT3; Skeletal muscle respiration

Indexed keywords

CYTOCHROME C OXIDASE; LYSINE; MESSENGER RNA; NUCLEAR RESPIRATORY FACTOR 1; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); SIRTUIN 3; SUCCINATE DEHYDROGENASE; UNCOUPLING PROTEIN 1; PROTEIN SUBUNIT;

EID: 84921044434     PISSN: 09552863     EISSN: 18734847     Source Type: Journal    
DOI: 10.1016/j.jnutbio.2014.10.003     Document Type: Article
Times cited : (29)

References (39)
  • 1
    • 84873853548 scopus 로고    scopus 로고
    • Maternal protein restriction in rats leads to reduced PGC-1alpha expression via altered DNA methylation in skeletal muscle
    • Zeng Y., Gu P., Liu K., Huang P. Maternal protein restriction in rats leads to reduced PGC-1alpha expression via altered DNA methylation in skeletal muscle. Mol Med Rep 2013, 7:306-312.
    • (2013) Mol Med Rep , vol.7 , pp. 306-312
    • Zeng, Y.1    Gu, P.2    Liu, K.3    Huang, P.4
  • 3
    • 2942530662 scopus 로고    scopus 로고
    • Prenatal stress induces intrauterine growth restriction and programmes glucose intolerance and feeding behaviour disturbances in the aged rat
    • Lesage J., Del-Favero F., Leonhardt M., Louvart H., Maccari S., Vieau D., et al. Prenatal stress induces intrauterine growth restriction and programmes glucose intolerance and feeding behaviour disturbances in the aged rat. J Endocrinol 2004, 181:291-296.
    • (2004) J Endocrinol , vol.181 , pp. 291-296
    • Lesage, J.1    Del-Favero, F.2    Leonhardt, M.3    Louvart, H.4    Maccari, S.5    Vieau, D.6
  • 4
    • 34247126988 scopus 로고    scopus 로고
    • Experimental IUGR and later diabetes
    • Martin-Gronert M.S., Ozanne S.E. Experimental IUGR and later diabetes. J Intern Med 2007, 261:437-452.
    • (2007) J Intern Med , vol.261 , pp. 437-452
    • Martin-Gronert, M.S.1    Ozanne, S.E.2
  • 5
    • 67349205865 scopus 로고    scopus 로고
    • Modeling intrauterine growth retardation in rodents: impact on pancreas development and glucose homeostasis
    • Schwitzgebel V.M., Somm E., Klee P. Modeling intrauterine growth retardation in rodents: impact on pancreas development and glucose homeostasis. Mol Cell Endocrinol 2009, 304:78-83.
    • (2009) Mol Cell Endocrinol , vol.304 , pp. 78-83
    • Schwitzgebel, V.M.1    Somm, E.2    Klee, P.3
  • 6
    • 84885747921 scopus 로고    scopus 로고
    • Prenatal low-protein and postnatal high-fat diets induce rapid adipose tissue growth by inducing Igf2 expression in Sprague Dawley rat offspring
    • Claycombe K.J., Uthus E.O., Roemmich J.N., Johnson L.K., Johnson W.T. Prenatal low-protein and postnatal high-fat diets induce rapid adipose tissue growth by inducing Igf2 expression in Sprague Dawley rat offspring. J Nutr 2013, 143:1533-1539.
    • (2013) J Nutr , vol.143 , pp. 1533-1539
    • Claycombe, K.J.1    Uthus, E.O.2    Roemmich, J.N.3    Johnson, L.K.4    Johnson, W.T.5
  • 7
    • 12344305124 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and type 2 diabetes
    • Lowell B.B., Shulman G.I. Mitochondrial dysfunction and type 2 diabetes. Science 2005, 307:384-387.
    • (2005) Science , vol.307 , pp. 384-387
    • Lowell, B.B.1    Shulman, G.I.2
  • 8
    • 75549085755 scopus 로고    scopus 로고
    • Skeletal muscle insulin resistance is the primary defect in type 2 diabetes
    • DeFronzo R.A., Tripathy D. Skeletal muscle insulin resistance is the primary defect in type 2 diabetes. Diabetes Care 2009, 32(Suppl. 2):S157-S163.
    • (2009) Diabetes Care , vol.32 , pp. S157-S163
    • DeFronzo, R.A.1    Tripathy, D.2
  • 9
    • 84856415487 scopus 로고    scopus 로고
    • The role of mitochondria in insulin resistance and type 2 diabetes mellitus
    • Szendroedi J., Phielix E., Roden M. The role of mitochondria in insulin resistance and type 2 diabetes mellitus. Nat Rev Endocrinol 2012, 8:92-103.
    • (2012) Nat Rev Endocrinol , vol.8 , pp. 92-103
    • Szendroedi, J.1    Phielix, E.2    Roden, M.3
  • 10
    • 76149131004 scopus 로고    scopus 로고
    • The role of mitochondria in the pathophysiology of skeletal muscle insulin resistance
    • Pagel-Langenickel I., Bao J., Pang L., Sack M.N. The role of mitochondria in the pathophysiology of skeletal muscle insulin resistance. Endocr Rev 2010, 31:25-51.
    • (2010) Endocr Rev , vol.31 , pp. 25-51
    • Pagel-Langenickel, I.1    Bao, J.2    Pang, L.3    Sack, M.N.4
  • 12
    • 1642377274 scopus 로고    scopus 로고
    • Impaired mitochondrial activity in the insulin-resistant offspring of patients with type 2 diabetes
    • Petersen K.F., Dufour S., Befroy D., Garcia R., Shulman G.I. Impaired mitochondrial activity in the insulin-resistant offspring of patients with type 2 diabetes. N Engl J Med 2004, 350:664-671.
    • (2004) N Engl J Med , vol.350 , pp. 664-671
    • Petersen, K.F.1    Dufour, S.2    Befroy, D.3    Garcia, R.4    Shulman, G.I.5
  • 13
    • 84870352685 scopus 로고    scopus 로고
    • SIRT3 weighs heavily in the metabolic balance: a new role for SIRT3 in metabolic syndrome
    • Green M.F., Hirschey M.D. SIRT3 weighs heavily in the metabolic balance: a new role for SIRT3 in metabolic syndrome. J Gerontol A Biol Sci Med Sci 2013, 68:105-107.
    • (2013) J Gerontol A Biol Sci Med Sci , vol.68 , pp. 105-107
    • Green, M.F.1    Hirschey, M.D.2
  • 14
    • 82455212901 scopus 로고    scopus 로고
    • SIRT3 deficiency and mitochondrial protein hyperacetylation accelerate the development of the metabolic syndrome
    • Hirschey M.D., Shimazu T., Jing E., Grueter C.A., Collins A.M., Aouizerat B., et al. SIRT3 deficiency and mitochondrial protein hyperacetylation accelerate the development of the metabolic syndrome. Mol Cell 2011, 44:177-190.
    • (2011) Mol Cell , vol.44 , pp. 177-190
    • Hirschey, M.D.1    Shimazu, T.2    Jing, E.3    Grueter, C.A.4    Collins, A.M.5    Aouizerat, B.6
  • 15
    • 17144424946 scopus 로고    scopus 로고
    • SIRT3, a mitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes
    • Shi T., Wang F., Stieren E., Tong Q. SIRT3, a mitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes. J Biol Chem 2005, 280:13560-13567.
    • (2005) J Biol Chem , vol.280 , pp. 13560-13567
    • Shi, T.1    Wang, F.2    Stieren, E.3    Tong, Q.4
  • 16
    • 77951235122 scopus 로고    scopus 로고
    • NAD+-dependent deacetylase SIRT3 regulates mitochondrial protein synthesis by deacetylation of the ribosomal protein MRPL10
    • Yang Y., Cimen H., Han M.J., Shi T., Deng J.H., Koc H., et al. NAD+-dependent deacetylase SIRT3 regulates mitochondrial protein synthesis by deacetylation of the ribosomal protein MRPL10. J Biol Chem 2010, 285:7417-7429.
    • (2010) J Biol Chem , vol.285 , pp. 7417-7429
    • Yang, Y.1    Cimen, H.2    Han, M.J.3    Shi, T.4    Deng, J.H.5    Koc, H.6
  • 17
    • 77951705893 scopus 로고    scopus 로고
    • Characterization of the murine SIRT3 mitochondrial localization sequence and comparison of mitochondrial enrichment and deacetylase activity of long and short SIRT3 isoforms
    • Bao J., Lu Z., Joseph J.J., Carabenciov D., Dimond C.C., Pang L., et al. Characterization of the murine SIRT3 mitochondrial localization sequence and comparison of mitochondrial enrichment and deacetylase activity of long and short SIRT3 isoforms. J Cell Biochem 2010, 110:238-247.
    • (2010) J Cell Biochem , vol.110 , pp. 238-247
    • Bao, J.1    Lu, Z.2    Joseph, J.J.3    Carabenciov, D.4    Dimond, C.C.5    Pang, L.6
  • 18
    • 84857883360 scopus 로고    scopus 로고
    • Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice
    • Fritz K.S., Galligan J.J., Hirschey M.D., Verdin E., Petersen D.R. Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice. J Proteome Res 2012, 11:1633-1643.
    • (2012) J Proteome Res , vol.11 , pp. 1633-1643
    • Fritz, K.S.1    Galligan, J.J.2    Hirschey, M.D.3    Verdin, E.4    Petersen, D.R.5
  • 19
    • 75349111140 scopus 로고    scopus 로고
    • Regulation of succinate dehydrogenase activity by SIRT3 in mammalian mitochondria
    • Cimen H., Han M.J., Yang Y., Tong Q., Koc H., Koc E.C. Regulation of succinate dehydrogenase activity by SIRT3 in mammalian mitochondria. Biochemistry 2010, 49:304-311.
    • (2010) Biochemistry , vol.49 , pp. 304-311
    • Cimen, H.1    Han, M.J.2    Yang, Y.3    Tong, Q.4    Koc, H.5    Koc, E.C.6
  • 20
    • 33746992118 scopus 로고    scopus 로고
    • Substrate and functional diversity of lysine acetylation revealed by a proteomics survey
    • Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., et al. Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell 2006, 23:607-618.
    • (2006) Mol Cell , vol.23 , pp. 607-618
    • Kim, S.C.1    Sprung, R.2    Chen, Y.3    Xu, Y.4    Ball, H.5    Pei, J.6
  • 21
    • 0027487229 scopus 로고
    • AIN-93 purified diets for laboratory rodents: final report of the American Institute of Nutrition ad hoc writing committee on the reformulation of the AIN-76A rodent diet
    • Reeves P.G., Nielsen F.H., Fahey G.C. AIN-93 purified diets for laboratory rodents: final report of the American Institute of Nutrition ad hoc writing committee on the reformulation of the AIN-76A rodent diet. J Nutr 1993, 123:1939-1951.
    • (1993) J Nutr , vol.123 , pp. 1939-1951
    • Reeves, P.G.1    Nielsen, F.H.2    Fahey, G.C.3
  • 22
    • 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 1976, 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 23
    • 7444263525 scopus 로고    scopus 로고
    • Development of a quantitative PCR (TaqMan) assay for relative mitochondrial DNA copy number and the common mitochondrial DNA deletion in the rat
    • Nicklas J.A., Brooks E.M., Hunter T.C., Single R., Branda R.F. Development of a quantitative PCR (TaqMan) assay for relative mitochondrial DNA copy number and the common mitochondrial DNA deletion in the rat. Environ Mol Mutagen 2004, 44:313-320.
    • (2004) Environ Mol Mutagen , vol.44 , pp. 313-320
    • Nicklas, J.A.1    Brooks, E.M.2    Hunter, T.C.3    Single, R.4    Branda, R.F.5
  • 24
    • 0026906885 scopus 로고
    • Mutation in mitochondrial tRNA(Leu)(UUR) gene in a large pedigree with maternally transmitted type II diabetes mellitus and deafness
    • van den Ouweland J.M., Lemkes H.H., Ruitenbeek W., Sandkuijl L.A., de Vijlder M.F., Struyvenberg P.A., et al. Mutation in mitochondrial tRNA(Leu)(UUR) gene in a large pedigree with maternally transmitted type II diabetes mellitus and deafness. Nat Genet 1992, 1:368-371.
    • (1992) Nat Genet , vol.1 , pp. 368-371
    • van den Ouweland, J.M.1    Lemkes, H.H.2    Ruitenbeek, W.3    Sandkuijl, L.A.4    de Vijlder, M.F.5    Struyvenberg, P.A.6
  • 25
    • 0036788293 scopus 로고    scopus 로고
    • Dysfunction of mitochondria in human skeletal muscle in type 2 diabetes
    • Kelley D.E., He J., Menshikova E.V., Ritov V.B. Dysfunction of mitochondria in human skeletal muscle in type 2 diabetes. Diabetes 2002, 51:2944-2950.
    • (2002) Diabetes , vol.51 , pp. 2944-2950
    • Kelley, D.E.1    He, J.2    Menshikova, E.V.3    Ritov, V.B.4
  • 26
    • 33745769040 scopus 로고    scopus 로고
    • Mitochondrial dysfunction induces aberrant insulin signalling and glucose utilisation in murine C2C12 myotube cells
    • Lim J.H., Lee J.I., Suh Y.H., Kim W., Song J.H., Jung M.H. Mitochondrial dysfunction induces aberrant insulin signalling and glucose utilisation in murine C2C12 myotube cells. Diabetologia 2006, 49:1924-1936.
    • (2006) Diabetologia , vol.49 , pp. 1924-1936
    • Lim, J.H.1    Lee, J.I.2    Suh, Y.H.3    Kim, W.4    Song, J.H.5    Jung, M.H.6
  • 27
    • 77956367951 scopus 로고    scopus 로고
    • Prolonged fasting identifies skeletal muscle mitochondrial dysfunction as consequence rather than cause of human insulin resistance
    • Hoeks J., van Herpen N.A., Mensink M., Moonen-Kornips E., van Beurden D., Hesselink M.K., et al. Prolonged fasting identifies skeletal muscle mitochondrial dysfunction as consequence rather than cause of human insulin resistance. Diabetes 2010, 59:2117-2125.
    • (2010) Diabetes , vol.59 , pp. 2117-2125
    • Hoeks, J.1    van Herpen, N.A.2    Mensink, M.3    Moonen-Kornips, E.4    van Beurden, D.5    Hesselink, M.K.6
  • 28
    • 0036300538 scopus 로고    scopus 로고
    • Lipid-induced insulin resistance in human muscle is associated with changes in diacylglycerol, protein kinase C, and IkappaB-alpha
    • Itani S.I., Ruderman N.B., Schmieder F., Boden G. Lipid-induced insulin resistance in human muscle is associated with changes in diacylglycerol, protein kinase C, and IkappaB-alpha. Diabetes 2002, 51:2005-2011.
    • (2002) Diabetes , vol.51 , pp. 2005-2011
    • Itani, S.I.1    Ruderman, N.B.2    Schmieder, F.3    Boden, G.4
  • 29
    • 0037184925 scopus 로고    scopus 로고
    • Mechanism by which fatty acids inhibit insulin activation of insulin receptor substrate-1 (IRS-1)-associated phosphatidylinositol 3-kinase activity in muscle
    • Yu C., Chen Y., Cline G.W., Zhang D., Zong H., Wang Y., et al. Mechanism by which fatty acids inhibit insulin activation of insulin receptor substrate-1 (IRS-1)-associated phosphatidylinositol 3-kinase activity in muscle. J Biol Chem 2002, 277:50230-50236.
    • (2002) J Biol Chem , vol.277 , pp. 50230-50236
    • Yu, C.1    Chen, Y.2    Cline, G.W.3    Zhang, D.4    Zong, H.5    Wang, Y.6
  • 30
    • 45749088032 scopus 로고    scopus 로고
    • Intermuscular lipid: a marker of disordered fat partitioning or the consequence of obesity?
    • Elbein S.C., Rasouli N. Intermuscular lipid: a marker of disordered fat partitioning or the consequence of obesity?. Am J Clin Nutr 2008, 87:1585-1586.
    • (2008) Am J Clin Nutr , vol.87 , pp. 1585-1586
    • Elbein, S.C.1    Rasouli, N.2
  • 31
    • 45749114064 scopus 로고    scopus 로고
    • Adipose tissue infiltration in skeletal muscle: age patterns and association with diabetes among men of African ancestry
    • Miljkovic-Gacic I., Gordon C.L., Goodpaster B.H., Bunker C.H., Patrick A.L., Kuller L.H., et al. Adipose tissue infiltration in skeletal muscle: age patterns and association with diabetes among men of African ancestry. Am J Clin Nutr 2008, 87:1590-1595.
    • (2008) Am J Clin Nutr , vol.87 , pp. 1590-1595
    • Miljkovic-Gacic, I.1    Gordon, C.L.2    Goodpaster, B.H.3    Bunker, C.H.4    Patrick, A.L.5    Kuller, L.H.6
  • 33
    • 80052291180 scopus 로고    scopus 로고
    • Sirtuin-3 (Sirt3) regulates skeletal muscle metabolism and insulin signaling via altered mitochondrial oxidation and reactive oxygen species production
    • Jing E., Emanuelli B., Hirschey M.D., Boucher J., Lee K.Y., Lombard D., et al. Sirtuin-3 (Sirt3) regulates skeletal muscle metabolism and insulin signaling via altered mitochondrial oxidation and reactive oxygen species production. Proc Natl Acad Sci U S A 2011, 108:14608-14613.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 14608-14613
    • Jing, E.1    Emanuelli, B.2    Hirschey, M.D.3    Boucher, J.4    Lee, K.Y.5    Lombard, D.6
  • 36
    • 84885194042 scopus 로고    scopus 로고
    • Skeletal muscle MnSOD, mitochondrial complex II, and SIRT3 enzyme activities are decreased in maternal obesity during human pregnancy and gestational diabetes mellitus
    • Boyle K.E., Newsom S.A., Janssen R.C., Lappas M., Friedman J.E. Skeletal muscle MnSOD, mitochondrial complex II, and SIRT3 enzyme activities are decreased in maternal obesity during human pregnancy and gestational diabetes mellitus. J Clin Endocrinol Metab 2013, 98:E1601-E1609.
    • (2013) J Clin Endocrinol Metab , vol.98 , pp. E1601-E1609
    • Boyle, K.E.1    Newsom, S.A.2    Janssen, R.C.3    Lappas, M.4    Friedman, J.E.5
  • 37
    • 84891506172 scopus 로고    scopus 로고
    • Sirt3 regulates metabolic flexibility of skeletal muscle through reversible enzymatic deacetylation
    • Jing E., O'Neill B.T., Rardin M.J., Kleinridders A., Ilkeyeva O.R., Ussar S., et al. Sirt3 regulates metabolic flexibility of skeletal muscle through reversible enzymatic deacetylation. Diabetes 2013, 62:3404-3417.
    • (2013) Diabetes , vol.62 , pp. 3404-3417
    • Jing, E.1    O'Neill, B.T.2    Rardin, M.J.3    Kleinridders, A.4    Ilkeyeva, O.R.5    Ussar, S.6
  • 38
    • 0037404976 scopus 로고    scopus 로고
    • Recent advances in mechanisms regulating glucose oxidation at the level of the pyruvate dehydrogenase complex by PDKs
    • Sugden M.C., Holness M.J. Recent advances in mechanisms regulating glucose oxidation at the level of the pyruvate dehydrogenase complex by PDKs. Am J Physiol Endocrinol Metab 2003, 284:E855-E862.
    • (2003) Am J Physiol Endocrinol Metab , vol.284 , pp. E855-E862
    • Sugden, M.C.1    Holness, M.J.2


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