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Volumn 416, Issue 1-2, 2016, Pages 11-22

Mitochondrial defects associated with β-alanine toxicity: relevance to hyper-beta-alaninemia

Author keywords

Apoptosis; Electron transport chain; Mitochondrial fragmentation; Oxidative stress; Respiration; Taurine

Indexed keywords

BETA ALANINE; CASPASE 3; CASPASE 9; GLUTAMIC ACID; MALIC ACID; OXYGEN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); SUPEROXIDE; TAURINE;

EID: 84962237703     PISSN: 03008177     EISSN: 15734919     Source Type: Journal    
DOI: 10.1007/s11010-016-2688-z     Document Type: Article
Times cited : (54)

References (29)
  • 1
    • 0027217863 scopus 로고
    • Dual activation of GABAA and glycine receptors by beta-alanine inverse modulation by progesterone and 5 alpha-pregnan-3 alpha-ol-20-one
    • COI: 1:CAS:528:DyaK3sXmsVWrsrk%3D, PID: 8223947
    • Wu FS, Gibbs TT, Farb DH (1993) Dual activation of GABAA and glycine receptors by beta-alanine inverse modulation by progesterone and 5 alpha-pregnan-3 alpha-ol-20-one. Eur J Pharmacol 246:239–246
    • (1993) Eur J Pharmacol , vol.246 , pp. 239-246
    • Wu, F.S.1    Gibbs, T.T.2    Farb, D.H.3
  • 2
    • 77955095029 scopus 로고    scopus 로고
    • β-alanine as a small molecule neurotransmitter
    • COI: 1:CAS:528:DC%2BC3cXptlWmt7k%3D, PID: 20540981
    • Tiedje KE, Stevens K, Barnes S, Weaver DF (2010) β-alanine as a small molecule neurotransmitter. Neurochem Int 57:177–188
    • (2010) Neurochem Int , vol.57 , pp. 177-188
    • Tiedje, K.E.1    Stevens, K.2    Barnes, S.3    Weaver, D.F.4
  • 3
    • 0001029250 scopus 로고
    • Enzymatic studies on the metabolism of β-alanine
    • COI: 1:CAS:528:DyaF3MXot1WgtA%3D%3D, PID: 13712439
    • Hayaishi O, Nishizuka Y, Tatibana M, Takeshita M, Kuno S (1961) Enzymatic studies on the metabolism of β-alanine. J Biol Chem 236:781–790
    • (1961) J Biol Chem , vol.236 , pp. 781-790
    • Hayaishi, O.1    Nishizuka, Y.2    Tatibana, M.3    Takeshita, M.4    Kuno, S.5
  • 4
    • 77749270811 scopus 로고    scopus 로고
    • Muscle carnosine metabolism and β-alanine supplementation in relation to exercise and training
    • PID: 20199122
    • Derave W, Everaert I, Beeckman S, Baguet A (2010) Muscle carnosine metabolism and β-alanine supplementation in relation to exercise and training. Sports Med 40:247–263
    • (2010) Sports Med , vol.40 , pp. 247-263
    • Derave, W.1    Everaert, I.2    Beeckman, S.3    Baguet, A.4
  • 5
    • 0003946372 scopus 로고
    • Aldehyde oxidation. V. Direct conversion of malonic semialdehyde to acetyl-coenzyme A
    • COI: 1:CAS:528:DyaF3cXotV2guw%3D%3D, PID: 13846369
    • Yamada EW, Jakoby WB (1960) Aldehyde oxidation. V. Direct conversion of malonic semialdehyde to acetyl-coenzyme A. J Biol Chem 235:589–594
    • (1960) J Biol Chem , vol.235 , pp. 589-594
    • Yamada, E.W.1    Jakoby, W.B.2
  • 6
    • 0002122628 scopus 로고    scopus 로고
    • Disorder of β- and γ-amino acids in free and peptide-linked forms
    • Scriver CR, Beaudet AL, Sly WS, Valle D, (eds), McGraw Hill, New York
    • Gibson MK, Jakobs C (2001) Disorder of β- and γ-amino acids in free and peptide-linked forms. In: Scriver CR, Beaudet AL, Sly WS, Valle D (eds) The metabolic and molecular basis of inherited disease. McGraw Hill, New York, pp 2079–2105
    • (2001) The metabolic and molecular basis of inherited disease , pp. 2079-2105
    • Gibson, M.K.1    Jakobs, C.2
  • 7
    • 0021024797 scopus 로고
    • 6-azauridine triacetate induced hyper beta-alaninemia and its decrease by administration of pyridoxine
    • COI: 1:CAS:528:DyaL2cXivFeqtQ%3D%3D, PID: 6198500
    • Slavik M, Blanc O, Smith KJ, Slavik J (1983) 6-azauridine triacetate induced hyper beta-alaninemia and its decrease by administration of pyridoxine. J Nutr Sci Vitaminol (Tokyo) 29:631–635
    • (1983) J Nutr Sci Vitaminol (Tokyo) , vol.29 , pp. 631-635
    • Slavik, M.1    Blanc, O.2    Smith, K.J.3    Slavik, J.4
  • 8
    • 0033073142 scopus 로고    scopus 로고
    • Experimental beta-alaninuria induced by (aminooxy)acetate
    • COI: 1:CAS:528:DyaK1MXhvVGgtrk%3D, PID: 10096733
    • Kurozumi Y, Abe T, Yao WB, Ubuka T (1999) Experimental beta-alaninuria induced by (aminooxy)acetate. Acta Med Okayama 53:13–18
    • (1999) Acta Med Okayama , vol.53 , pp. 13-18
    • Kurozumi, Y.1    Abe, T.2    Yao, W.B.3    Ubuka, T.4
  • 11
    • 0344872685 scopus 로고    scopus 로고
    • Apoptotic cascade initiated by angiotensin II in neonatal cardiomyocytes: role of DNA damage
    • COI: 1:CAS:528:DC%2BD2cXhsVSj
    • Grishko V, Pastukh V, Solodushko V, Gillespie M, Azuma J, Schaffer S (2003) Apoptotic cascade initiated by angiotensin II in neonatal cardiomyocytes: role of DNA damage. Am J Physiol 285:H2364–H2372
    • (2003) Am J Physiol , vol.285 , pp. H2364-H2372
    • Grishko, V.1    Pastukh, V.2    Solodushko, V.3    Gillespie, M.4    Azuma, J.5    Schaffer, S.6
  • 12
    • 33646716659 scopus 로고    scopus 로고
    • The mechanism of superoxide production by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria
    • COI: 1:CAS:528:DC%2BD28XlsVGlurs%3D, PID: 16682634
    • Kussmaul L, Hirst J (2006) The mechanism of superoxide production by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria. Proc Natl Acad Sci USA 103(20):7607–7612
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.20 , pp. 7607-7612
    • Kussmaul, L.1    Hirst, J.2
  • 13
    • 10344221083 scopus 로고    scopus 로고
    • Complex III releases superoxide to both sides of the inner mitochondrial membrane
    • COI: 1:CAS:528:DC%2BD2cXpslKjt7k%3D, PID: 15317809
    • Muller FL, Liu Y, van Remmen H (2004) Complex III releases superoxide to both sides of the inner mitochondrial membrane. J Biol Chem 279(47):49064–49073
    • (2004) J Biol Chem , vol.279 , Issue.47 , pp. 49064-49073
    • Muller, F.L.1    Liu, Y.2    van Remmen, H.3
  • 15
    • 6344274848 scopus 로고    scopus 로고
    • Roles of the mammalian mitochondrial fission and fusion mediators fis1, drp1 and opa1 in apoptosis
    • COI: 1:CAS:528:DC%2BD2cXpslKns7c%3D, PID: 15356267
    • Lee YJ, Jeong SY, Karbowski M, Smith CL, Youle RJ (2004) Roles of the mammalian mitochondrial fission and fusion mediators fis1, drp1 and opa1 in apoptosis. Mol Biol Cell 15:5001–5011
    • (2004) Mol Biol Cell , vol.15 , pp. 5001-5011
    • Lee, Y.J.1    Jeong, S.Y.2    Karbowski, M.3    Smith, C.L.4    Youle, R.J.5
  • 16
    • 84864343417 scopus 로고    scopus 로고
    • Ergogenic effects of β-alanine and carnosine: proposed future research to quantify their efficacy
    • Caruso J, Charles J, Unruh K, Giebel R, Learmonth L, Potter W (2012) Ergogenic effects of β-alanine and carnosine: proposed future research to quantify their efficacy. Nutrients 4:586–601
    • (2012) Nutrients , vol.4 , pp. 586-601
    • Caruso, J.1    Charles, J.2    Unruh, K.3    Giebel, R.4    Learmonth, L.5    Potter, W.6
  • 17
    • 77956052517 scopus 로고    scopus 로고
    • Effects of β-alanine treatment on mitochondrial taurine level and 5-taurinomethyluridine content
    • Jong CJ, Ito T, Mozaffari M, Azuma J, Schaffer S (2010) Effects of β-alanine treatment on mitochondrial taurine level and 5-taurinomethyluridine content. J Biomed Sci 17(S1):525–532
    • (2010) J Biomed Sci , vol.17 , Issue.S1 , pp. 525-532
    • Jong, C.J.1    Ito, T.2    Mozaffari, M.3    Azuma, J.4    Schaffer, S.5
  • 18
    • 84862264118 scopus 로고    scopus 로고
    • Mechanism underlying the antioxidant activity of taurine: prevention of mitochondrial oxidant production
    • COI: 1:CAS:528:DC%2BC38XmvFGlu7k%3D, PID: 21691752
    • Jong CJ, Azuma J, Schaffer S (2012) Mechanism underlying the antioxidant activity of taurine: prevention of mitochondrial oxidant production. Amino Acids 42(6):2223–2232
    • (2012) Amino Acids , vol.42 , Issue.6 , pp. 2223-2232
    • Jong, C.J.1    Azuma, J.2    Schaffer, S.3
  • 19
    • 84895909083 scopus 로고    scopus 로고
    • Role of taurine in the pathologies of MELAS and MERRF
    • COI: 1:CAS:528:DC%2BC2cXptFKhtg%3D%3D, PID: 23179085
    • Schaffer SW, Jong CJ, Ito T, Azuma J (2014) Role of taurine in the pathologies of MELAS and MERRF. Amino Acids 46(1):47–56
    • (2014) Amino Acids , vol.46 , Issue.1 , pp. 47-56
    • Schaffer, S.W.1    Jong, C.J.2    Ito, T.3    Azuma, J.4
  • 20
    • 18844430007 scopus 로고    scopus 로고
    • Specific correlation between the wobble modification deficiency in mutant tRNAs and the clinical features of a human mitochondrial disease
    • COI: 1:CAS:528:DC%2BD2MXks12gu7c%3D, PID: 15870203
    • Kirino Y, Goto Y, Campos Y, Arenas J, Suzuki T (2005) Specific correlation between the wobble modification deficiency in mutant tRNAs and the clinical features of a human mitochondrial disease. Proc Natl Acad Sci USA 102:7127–7132
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 7127-7132
    • Kirino, Y.1    Goto, Y.2    Campos, Y.3    Arenas, J.4    Suzuki, T.5
  • 21
    • 0019083215 scopus 로고
    • Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
    • COI: 1:CAS:528:DyaL3MXlvF2mtg%3D%3D, PID: 6263247
    • Turrens J, Boveris A (1980) Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria. Biochem J 191:421–427
    • (1980) Biochem J , vol.191 , pp. 421-427
    • Turrens, J.1    Boveris, A.2
  • 22
    • 84880659584 scopus 로고    scopus 로고
    • Regulation of the intrinsic apoptosis pathway by reactive oxygen species
    • COI: 1:CAS:528:DC%2BC3sXhtFanu7vP, PID: 22978471
    • Wu CC, Bratton SB (2013) Regulation of the intrinsic apoptosis pathway by reactive oxygen species. Antioxid Redox Signal 19(6):546–558
    • (2013) Antioxid Redox Signal , vol.19 , Issue.6 , pp. 546-558
    • Wu, C.C.1    Bratton, S.B.2
  • 23
    • 77956095537 scopus 로고    scopus 로고
    • Mitochondria and cell death: outer membrane permeabilization and beyond
    • COI: 1:CAS:528:DC%2BC3cXps1egt7w%3D, PID: 20683470
    • Tait SW, Green DR (2010) Mitochondria and cell death: outer membrane permeabilization and beyond. Nat Rev Mol Cell Biol 11(9):621–632
    • (2010) Nat Rev Mol Cell Biol , vol.11 , Issue.9 , pp. 621-632
    • Tait, S.W.1    Green, D.R.2
  • 25
    • 49349083531 scopus 로고    scopus 로고
    • Redox control of cell fate by MAP kinase: physiological roles of ASK1-MAP kinase pathway in stress signaling
    • COI: 1:CAS:528:DC%2BD1cXhtVarsbfF, PID: 18206122
    • Matsuzawa A, Ichijo H (2008) Redox control of cell fate by MAP kinase: physiological roles of ASK1-MAP kinase pathway in stress signaling. Biochim Biophys Acta 1780(11):1325–1336
    • (2008) Biochim Biophys Acta , vol.1780 , Issue.11 , pp. 1325-1336
    • Matsuzawa, A.1    Ichijo, H.2
  • 26
    • 84865395988 scopus 로고    scopus 로고
    • Stress-induced phosphorylation and proteasomal degradation of mitofusin 2 facilitates mitochondrial fragmentation and apoptoSsis
    • COI: 1:CAS:528:DC%2BC38XpsVOks74%3D, PID: 22748923
    • Leboucher GP, Tsai YC, Yang M, Shaw KC, Zhou M, Veenstra TD, Glickman MH, Weissman AM (2012) Stress-induced phosphorylation and proteasomal degradation of mitofusin 2 facilitates mitochondrial fragmentation and apoptoSsis. Mol Cell 47(4):547–557
    • (2012) Mol Cell , vol.47 , Issue.4 , pp. 547-557
    • Leboucher, G.P.1    Tsai, Y.C.2    Yang, M.3    Shaw, K.C.4    Zhou, M.5    Veenstra, T.D.6    Glickman, M.H.7    Weissman, A.M.8
  • 27
    • 0037408271 scopus 로고    scopus 로고
    • Possible cause of taurine deficient cardiomyopathy: potentiation of angiotensin II action
    • COI: 1:CAS:528:DC%2BD3sXjt1Shtrg%3D, PID: 12717106
    • Schaffer S, Solodushko V, Pastukh V, Ricci C, Azuma J (2003) Possible cause of taurine deficient cardiomyopathy: potentiation of angiotensin II action. J Cardiovasc Pharmacol 41(5):751–759
    • (2003) J Cardiovasc Pharmacol , vol.41 , Issue.5 , pp. 751-759
    • Schaffer, S.1    Solodushko, V.2    Pastukh, V.3    Ricci, C.4    Azuma, J.5
  • 28
    • 84943590091 scopus 로고    scopus 로고
    • Role of protein phosphorylation in excitation-contraction coupling in taurine deficient hearts
    • COI: 1:CAS:528:DC%2BC2MXjsVKmtbc%3D
    • Ramila KC, Jong CJ, Pastukh V, Ito T, Azuma J, Schaffer SW (2015) Role of protein phosphorylation in excitation-contraction coupling in taurine deficient hearts. Am J Physiol 308(3):H232–H239
    • (2015) Am J Physiol , vol.308 , Issue.3 , pp. H232-H239
    • Ramila, K.C.1    Jong, C.J.2    Pastukh, V.3    Ito, T.4    Azuma, J.5    Schaffer, S.W.6
  • 29
    • 84883562084 scopus 로고    scopus 로고
    • Heart failure compendium: cardiac metabolism and heart failure: implications beyond ATP production
    • COI: 1:CAS:528:DC%2BC3sXhtlChs7bJ, PID: 23989714
    • Doenst T, Nguyen TD, Abel ED (2013) Heart failure compendium: cardiac metabolism and heart failure: implications beyond ATP production. Circ Res 113:709–724
    • (2013) Circ Res , vol.113 , pp. 709-724
    • Doenst, T.1    Nguyen, T.D.2    Abel, E.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.