메뉴 건너뛰기




Volumn 449, Issue 1, 2013, Pages 253-261

Metabolic inflexibility and protein lysine acetylation in heart mitochondria of a chronic model of Type 1 diabetes

Author keywords

Acetylation; Cardiac mitochondrion; Diabetes; Free radical

Indexed keywords

ACETIC ANHYDRIDE; FATTY ACID; LYSINE; PROTEIN; PYRUVATE DEHYDROGENASE; SUCCINATE DEHYDROGENASE (UBIQUINONE); SUPEROXIDE;

EID: 84870907221     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20121038     Document Type: Article
Times cited : (53)

References (42)
  • 1
    • 0035856980 scopus 로고    scopus 로고
    • Biochemistry and molecular cell biology of diabetic complications
    • Brownlee, M. (2001) Biochemistry and molecular cell biology of diabetic complications. Nature 414, 813-820
    • (2001) Nature , vol.414 , pp. 813-820
    • Brownlee, M.1
  • 3
    • 33644766038 scopus 로고    scopus 로고
    • Protection of cardiac mitochondria by overexpression of MnSOD reduces diabetic cardiomyopathy
    • DOI 10.1562/2005-10-20-RN-723
    • Shen, X., Zheng, S., Metreveli, N. S. and Epstein, P. N. (2006) Protection of cardiac mitochondria by overexpression of MnSOD reduces diabetic cardiomyopathy. Diabetes 55, 798-805 (Pubitemid 43343239)
    • (2006) Diabetes , vol.55 , Issue.3 , pp. 798-805
    • Shen, X.1    Zheng, S.2    Metreveli, N.S.3    Epstein, P.N.4
  • 4
    • 77956572071 scopus 로고    scopus 로고
    • Mitochondria in the diabetic heart
    • Bugger, H. and Abel, E. D. (2010) Mitochondria in the diabetic heart. Cardiovasc. Res. 88, 229-240
    • (2010) Cardiovasc. Res. , vol.88 , pp. 229-240
    • Bugger, H.1    Abel, E.D.2
  • 5
    • 77953440109 scopus 로고    scopus 로고
    • Diabetic cardiomyopathy, causes and effects
    • Boudina, S. and Abel, E. D. (2010) Diabetic cardiomyopathy, causes and effects. Rev. Endocr. Metab. Disord. 11, 31-39
    • (2010) Rev. Endocr. Metab. Disord. , vol.11 , pp. 31-39
    • Boudina, S.1    Abel, E.D.2
  • 6
    • 58149330628 scopus 로고    scopus 로고
    • Type 1 diabetic Akita mouse hearts are insulin sensitive but manifest structurally abnormal mitochondria that remain coupled despite increased uncoupling protein 3
    • Bugger, H., Boudina, S., Hu, X. X., Tuinei, J., Zaha, V. G., Theobald, H. A., Yun, U. J., McQueen, A. P., Wayment, B., Litwin, S. E. and Abel, E. D. (2008) Type 1 diabetic Akita mouse hearts are insulin sensitive but manifest structurally abnormal mitochondria that remain coupled despite increased uncoupling protein 3. Diabetes 57, 2924-2932
    • (2008) Diabetes , vol.57 , pp. 2924-2932
    • Bugger, H.1    Boudina, S.2    Hu, X.X.3    Tuinei, J.4    Zaha, V.G.5    Theobald, H.A.6    Yun, U.J.7    McQueen, A.P.8    Wayment, B.9    Litwin, S.E.10    Abel, E.D.11
  • 7
    • 79957969004 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in diabetic cardiomyopathy
    • Duncan, J. G. (2011) Mitochondrial dysfunction in diabetic cardiomyopathy. Biochim. Biophys. Acta 1813, 1351-1359
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 1351-1359
    • Duncan, J.G.1
  • 10
    • 29244477536 scopus 로고    scopus 로고
    • Shotgun lipidomics identifies cardiolipin depletion in diabetic myocardium linking altered substrate utilization with mitochondrial dysfunction
    • DOI 10.1021/bi051908a
    • Han, X., Yang, J., Cheng, H., Yang, K., Abendschein, D. R. and Gross, R. W. (2005) Shotgun lipidomics identifies cardiolipin depletion in diabetic myocardium linking altered substrate utilization with mitochondrial dysfunction. Biochemistry 44, 16684-16694 (Pubitemid 41832048)
    • (2005) Biochemistry , vol.44 , Issue.50 , pp. 16684-16694
    • Han, X.1    Yang, J.2    Cheng, H.3    Yang, K.4    Abendschein, D.R.5    Gross, R.W.6
  • 11
    • 21244492310 scopus 로고    scopus 로고
    • Myocardial substrate metabolism in the normal and failing heart
    • DOI 10.1152/physrev.00006.2004
    • Stanley, W. C., Recchia, F. A. and Lopaschuk, G. D. (2005) Myocardial substrate metabolism in the normal and failing heart. Physiol. Rev. 85, 1093-1129 (Pubitemid 40894649)
    • (2005) Physiological Reviews , vol.85 , Issue.3 , pp. 1093-1129
    • Stanley, W.C.1    Recchia, F.A.2    Lopaschuk, G.D.3
  • 12
    • 0342506484 scopus 로고    scopus 로고
    • Regulation of energy substrate metabolism in the diabetic heart
    • DOI 10.1016/S0008-6363(97)00047-3, PII S9998636397000473
    • Stanley, W. C., Lopaschuk, G. D. and McCormack, J. G. (1997) Regulation of energy substrate metabolism in the diabetic heart. Cardiovasc. Res. 34, 25-33 (Pubitemid 27261909)
    • (1997) Cardiovascular Research , vol.34 , Issue.1 , pp. 25-33
    • Stanley, W.C.1    Lopaschuk, G.D.2    McCormack, J.G.3
  • 14
    • 71549149354 scopus 로고    scopus 로고
    • Role of fatty acid uptake and fatty acid beta-oxidation in mediating insulin resistance in heart and skeletal muscle
    • Zhang, L., Keung, W., Samokhvalov, V., Wang, W. and Lopaschuk, G. D. (2010) Role of fatty acid uptake and fatty acid beta-oxidation in mediating insulin resistance in heart and skeletal muscle. Biochim. Biophys. Acta 1801, 1-22
    • (2010) Biochim. Biophys. Acta , vol.1801 , pp. 1-22
    • Zhang, L.1    Keung, W.2    Samokhvalov, V.3    Wang, W.4    Lopaschuk, G.D.5
  • 15
    • 0037160091 scopus 로고    scopus 로고
    • Topology of superoxide production from different sites in the mitochondrial electron transport chain
    • DOI 10.1074/jbc.M207217200
    • St-Pierre, J., Buckingham, J. A., Roebuck, S. J. and Brand, M. D. (2002) Topology of superoxide production from different sites in the mitochondrial electron transport chain. J. Biol. Chem. 277, 44784-44790 (Pubitemid 36159072)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.47 , pp. 44784-44790
    • St-Pierre, J.1    Buckingham, J.A.2    Roebuck, S.J.3    Brand, M.D.4
  • 22
    • 84859951790 scopus 로고    scopus 로고
    • SIRT3 deacetylates isocitrate dehydrogenase 2 (IDH2) and regulates mitochondrial redox status
    • Yu, W., Dittenhafer-Reed, K. E. and Denu, J. M. (2012) SIRT3 deacetylates isocitrate dehydrogenase 2 (IDH2) and regulates mitochondrial redox status. J. Biol. Chem. 287, 14078-14086
    • (2012) J. Biol. Chem. , vol.287 , pp. 14078-14086
    • Yu, W.1    Dittenhafer-Reed, K.E.2    Denu, J.M.3
  • 23
    • 77957003282 scopus 로고
    • Mitochondrial respiratory control and the polarographic measurement of ADP:O ratios
    • Estabrook, R. W. (1967) Mitochondrial respiratory control and the polarographic measurement of ADP:O ratios. Methods Enzymol. 10, 41-47
    • (1967) Methods Enzymol. , vol.10 , pp. 41-47
    • Estabrook, R.W.1
  • 24
    • 67651121563 scopus 로고    scopus 로고
    • Inhibition of succinate-linked respiration and complex II activity by hydrogen peroxide
    • Moser, M. D., Matsuzaki, S. and Humphries, K. M. (2009) Inhibition of succinate-linked respiration and complex II activity by hydrogen peroxide. Arch. Biochem. Biophys. 488, 69-75
    • (2009) Arch. Biochem. Biophys. , vol.488 , pp. 69-75
    • Moser, M.D.1    Matsuzaki, S.2    Humphries, K.M.3
  • 25
    • 0032898050 scopus 로고    scopus 로고
    • Triton X-100 as a specific inhibitor of the mammalian NADH-ubiquinone oxidoreductase (Complex I)
    • DOI 10.1016/S0005-2728(98)00156-X, PII S000527289800156X
    • Ushakova, A. V., Grivennikova, V. G., Ohnishi, T. and Vinogradov, A. D. (1999) Triton X-100 as a specific inhibitor of the mammalian NADH-ubiquinone oxidoreductase (Complex I). Biochim. Biophys. Acta 1409, 143-153 (Pubitemid 29044063)
    • (1999) Biochimica et Biophysica Acta - Bioenergetics , vol.1409 , Issue.3 , pp. 143-153
    • Ushakova, A.V.1    Grivennikova, V.G.2    Ohnishi, T.3    Vinogradov, A.D.4
  • 27
    • 0032506040 scopus 로고    scopus 로고
    • Selective inactivation of α-ketoglutarate dehydrogenase and pyruvate dehydrogenase: Reaction of lipoic acid with 4-hydroxy-2-nonenal
    • DOI 10.1021/bi981512h
    • Humphries, K. M. and Szweda, L. I. (1998) Selective inactivation of α-ketoglutarate dehydrogenase and pyruvate dehydrogenase: reaction of lipoic acid with 4-hydroxy-2-nonenal. Biochemistry 37, 15835-15841 (Pubitemid 28524755)
    • (1998) Biochemistry , vol.37 , Issue.45 , pp. 15835-15841
    • Humphries, K.M.1    Szweda, L.I.2
  • 28
    • 0038368985 scopus 로고    scopus 로고
    • Superoxide reacts with hydroethidine but forms a fluorescent product that is distinctly different from ethidium: Potential implications in intracellular fluorescence detection of superoxide
    • DOI 10.1016/S0891-5849(03)00142-4
    • Zhao, H., Kalivendi, S., Zhang, H., Joseph, J., Nithipatikom, K., Vasquez-Vivar, J. and Kalyanaraman, B. (2003) Superoxide reacts with hydroethidine but forms a fluorescent product that is distinctly different from ethidium: potential implications in intracellular fluorescence detection of superoxide. Free Radical Biol. Med. 34, 1359-1368 (Pubitemid 36570409)
    • (2003) Free Radical Biology and Medicine , vol.34 , Issue.11 , pp. 1359-1368
    • Zhao, H.1    Kalivendi, S.2    Zhang, H.3    Joseph, J.4    Nithipatikom, K.5    Vasquez-Vivar, J.6    Kalyanaraman, B.7
  • 30
    • 0024459130 scopus 로고
    • Calmodulin-induced early-onset diabetes in transgenic mice
    • DOI 10.1016/0092-8674(89)90505-9
    • Epstein, P. N., Overbeek, P. A. and Means, A. R. (1989) Calmodulin-induced early-onset diabetes in transgenic mice. Cell 58, 1067-1073 (Pubitemid 19238184)
    • (1989) Cell , vol.58 , Issue.6 , pp. 1067-1073
    • Epstein, P.N.1    Overbeek, P.A.2    Means, A.R.3
  • 31
    • 37849053352 scopus 로고    scopus 로고
    • Diabetic cardiomyopathy in OVE26 mice shows mitochondrial ros production and divergence between in vivo and in vitro contractility
    • Song, Y., Du, Y., Prabhu, S. D. and Epstein, P. N. (2007) Diabetic cardiomyopathy in OVE26 mice shows mitochondrial ros production and divergence between in vivo and in vitro contractility. Rev. Diabet. Stud. 4, 159-168
    • (2007) Rev. Diabet. Stud. , vol.4 , pp. 159-168
    • Song, Y.1    Du, Y.2    Prabhu, S.D.3    Epstein, P.N.4
  • 32
    • 0016343539 scopus 로고
    • Regulation of heart muscle pyruvate dehydrogenase kinase
    • Cooper, R. H., Randle, P. J. and Denton, R. M. (1974) Regulation of heart muscle pyruvate dehydrogenase kinase. Biochem. J. 143, 625-641
    • (1974) Biochem. J. , vol.143 , pp. 625-641
    • Cooper, R.H.1    Randle, P.J.2    Denton, R.M.3
  • 33
    • 0017640466 scopus 로고
    • Diabetes and the control of pyruvate dehydrogenase in rat heart mitochondria by concentration ratios of adenosine triphosphate/adenosine diphosphate, of reduced/oxidized nicotinamide-adenine dinucleotide and of acetyl-coenzyme A/coenzymeA
    • Kerbey, A. L., Radcliffe, P. M. and Randle, P. J. (1977) Diabetes and the control of pyruvate dehydrogenase in rat heart mitochondria by concentration ratios of adenosine triphosphate/adenosine diphosphate, of reduced/oxidized nicotinamide-adenine dinucleotide and of acetyl-coenzyme A/coenzyme A. Biochem. J. 164, 509-519 (Pubitemid 8132903)
    • (1977) Biochemical Journal , vol.164 , Issue.3 , pp. 509-519
    • Kerbey, A.L.1    Radcliffe, P.M.2    Randle, P.J.3
  • 34
    • 84870907842 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted
  • 36
    • 53549105529 scopus 로고    scopus 로고
    • SIRT3 is a stress-responsive deacetylase in cardiomyocytes that protects cells from stress-mediated cell death by deacetylation of Ku70
    • Sundaresan, N. R., Samant, S. A., Pillai, V. B., Rajamohan, S. B. and Gupta, M. P. (2008) SIRT3 is a stress-responsive deacetylase in cardiomyocytes that protects cells from stress-mediated cell death by deacetylation of Ku70. Mol. Cell. Biol. 28, 6384-6401
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 6384-6401
    • Sundaresan, N.R.1    Samant, S.A.2    Pillai, V.B.3    Rajamohan, S.B.4    Gupta, M.P.5
  • 37
    • 0024564749 scopus 로고
    • Differential labeling of the catalytic subunit of cAMP-dependent protein kinase with acetic anhydride: Substrate-induced conformational changes
    • DOI 10.1021/bi00433a042
    • Buechler, J. A., Vedvick, T. A. and Taylor, S. S. (1989) Differential labeling of the catalytic subunit of cAMP-dependent protein kinase with acetic anhydride: substrate-induced conformational changes. Biochemistry 28, 3018-3024 (Pubitemid 19099485)
    • (1989) Biochemistry , vol.28 , Issue.7 , pp. 3018-3024
    • Buechler, J.A.1    Vedvick, T.A.2    Taylor, S.S.3
  • 39
    • 33644637265 scopus 로고    scopus 로고
    • Decreased complex II respiration and HNE-modified SDH subunit in diabetic heart
    • DOI 10.1016/j.freeradbiomed.2005.10.040, PII S0891584905006350
    • Lashin, O. M., Szweda, P. A., Szweda, L. I. and Romani, A. M. (2006) Decreased complex II respiration and HNE-modified SDH subunit in diabetic heart. Free Radical Biol. Med. 40, 886-896 (Pubitemid 43327322)
    • (2006) Free Radical Biology and Medicine , vol.40 , Issue.5 , pp. 886-896
    • Lashin, O.M.1    Szweda, P.A.2    Szweda, L.I.3    Romani, A.M.P.4
  • 40
    • 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. and Koc, E. C. (2010) Regulation of succinate dehydrogenase activity by SIRT3 in mammalian mitochondria. Biochemistry 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
  • 42
    • 0036097650 scopus 로고    scopus 로고
    • Overexpression of metallothionein reduces diabetic cardiomyopathy
    • Liang, Q., Carlson, E. C., Donthi, R. V., Kralik, P. M., Shen, X. and Epstein, P. N. (2002) Overexpression of metallothionein reduces diabetic cardiomyopathy. Diabetes 51, 174-181 (Pubitemid 34517995)
    • (2002) Diabetes , vol.51 , Issue.1 , pp. 174-181
    • Liang, Q.1    Carlson, E.C.2    Donthi, R.V.3    Kralik, P.M.4    Shen, X.5    Epstein, P.N.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.