메뉴 건너뛰기




Volumn 177, Issue 5, 2010, Pages 2541-2548

Unexpected vascular enrichment of SCO1 over SCO2 in mammalian tissues: Implications for human mitochondrial disease

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; COPPER BINDING PROTEIN; CYTOCHROME C OXIDASE; MITOCHONDRIAL PROTEIN; PROTEIN SCO1; PROTEIN SCO2; UNCLASSIFIED DRUG;

EID: 78149352179     PISSN: 00029440     EISSN: 15252191     Source Type: Journal    
DOI: 10.2353/ajpath.2010.100229     Document Type: Article
Times cited : (13)

References (35)
  • 2
    • 23644456143 scopus 로고    scopus 로고
    • Biogenesis of cytochrome oxidase-sophisticated assembly lines in the mitochondrial inner membrane
    • Herrmann JM, Funes S: Biogenesis of cytochrome oxidase-sophisticated assembly lines in the mitochondrial inner membrane. Gene 2005, 354:43-52
    • (2005) Gene , vol.354 , pp. 43-52
    • Herrmann, J.M.1    Funes, S.2
  • 3
    • 33845298268 scopus 로고    scopus 로고
    • Assembly of mitochondrial cytochrome c-oxidase, a complicated and highly regulated cellular process
    • Fontanesi F, Soto IC, Horn D, Barrientos A: Assembly of mitochondrial cytochrome c-oxidase, a complicated and highly regulated cellular process. Am J Physiol Cell Physiol 2006, 291:C1129-C1147
    • (2006) Am J Physiol Cell Physiol , vol.291
    • Fontanesi, F.1    Soto, I.C.2    Horn, D.3    Barrientos, A.4
  • 4
    • 56349099660 scopus 로고    scopus 로고
    • Suppression mechanisms of COX assembly defects in yeast and human: Insights into the COX assembly process
    • Barrientos A, Gouget K, Horn D, Soto IC, Fontanesi F: Suppression mechanisms of COX assembly defects in yeast and human: insights into the COX assembly process. Biochim Biophys Acta 2009, 1793:97-107
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 97-107
    • Barrientos, A.1    Gouget, K.2    Horn, D.3    Soto, I.C.4    Fontanesi, F.5
  • 6
    • 9444296498 scopus 로고    scopus 로고
    • SCO1 and SCO2 act as high copy suppressors of a mitochondrial copper recruitment defect in Saccharomyces cerevisiae
    • Glerum DM, Shtanko A, Tzagoloff A: SCO1 and SCO2 act as high copy suppressors of a mitochondrial copper recruitment defect in Saccharomyces cerevisiae. J Biol Chem 1996, 271:20531-20535
    • (1996) J Biol Chem , vol.271 , pp. 20531-20535
    • Glerum, D.M.1    Shtanko, A.2    Tzagoloff, A.3
  • 7
    • 0034680823 scopus 로고    scopus 로고
    • Mitochondrial copper metabolism in yeast: Interaction between Sco1p and Cox2p
    • Lode A, Kuschel M, Paret C, Rodel G: Mitochondrial copper metabolism in yeast: interaction between Sco1p and Cox2p. FEBS Lett 2000, 485:19-24
    • (2000) FEBS Lett , vol.485 , pp. 19-24
    • Lode, A.1    Kuschel, M.2    Paret, C.3    Rodel, G.4
  • 8
    • 17644415027 scopus 로고    scopus 로고
    • Crystal structure of human SCO1: Implications for redox signaling by a mitochondrial cytochrome c oxidase "assembly" protein
    • Williams JC, Sue C, Banting GS, Yang H, Glerum DM, Hendrickson WA, Schon EA: Crystal structure of human SCO1: implications for redox signaling by a mitochondrial cytochrome c oxidase "assembly" protein. J Biol Chem 2005, 280:15202-15211
    • (2005) J Biol Chem , vol.280 , pp. 15202-15211
    • Williams, J.C.1    Sue, C.2    Banting, G.S.3    Yang, H.4    Glerum, D.M.5    Hendrickson, W.A.6    Schon, E.A.7
  • 11
    • 0033930194 scopus 로고    scopus 로고
    • Cytochrome c oxidase assembly factors with a thioredoxin fold are conserved among prokaryotes and eukaryotes
    • Chinenov YV: Cytochrome c oxidase assembly factors with a thioredoxin fold are conserved among prokaryotes and eukaryotes. J Mol Med 2000, 78:239-242
    • (2000) J Mol Med , vol.78 , pp. 239-242
    • Chinenov, Y.V.1
  • 12
    • 66149139796 scopus 로고    scopus 로고
    • Human SCO2 is required for the synthesis of CO II and as a thiol-disulphide oxidoreductase for SCO1
    • Leary SC, Sasarman F, Nishimura T, Shoubridge EA: Human SCO2 is required for the synthesis of CO II and as a thiol-disulphide oxidoreductase for SCO1. Hum Mol Genet 2009, 18:2230-2240
    • (2009) Hum Mol Genet , vol.18 , pp. 2230-2240
    • Leary, S.C.1    Sasarman, F.2    Nishimura, T.3    Shoubridge, E.A.4
  • 13
    • 33645052707 scopus 로고    scopus 로고
    • Mutational analysis of the Saccharomyces cerevisiae cytochrome c oxidase assembly protein Cox11p
    • Banting GS, Glerum DM: Mutational analysis of the Saccharomyces cerevisiae cytochrome c oxidase assembly protein Cox11p. Eukaryot Cell 2006, 5:568-578
    • (2006) Eukaryot Cell , vol.5 , pp. 568-578
    • Banting, G.S.1    Glerum, D.M.2
  • 18
    • 0032534869 scopus 로고    scopus 로고
    • Identification and characterization of human cDNAs specific to BCS1. PET112, SCO1, COX15, and COX11, five genes involved in the formation and function of the mitochondrial respiratory chain
    • Petruzzella V, Tiranti V, Fernandez P, Ianna P, Carrozzo R, Zeviani M: Identification and characterization of human cDNAs specific to BCS1. PET112, SCO1, COX15, and COX11, five genes involved in the formation and function of the mitochondrial respiratory chain Genomics 1998, 54:494-504
    • (1998) Genomics , vol.54 , pp. 494-504
    • Petruzzella, V.1    Tiranti, V.2    Fernandez, P.3    Ianna, P.4    Carrozzo, R.5    Zeviani, M.6
  • 19
    • 0034881326 scopus 로고    scopus 로고
    • Inter-mitochondrial complementation: Mitochondria-specific system preventing mice from expression of disease phenotypes by mutant mtDNA
    • Nakada K, Inoue K, Ono T, Isobe K, Ogura A, Goto YI, Nonaka I, Hayashi JI: Inter-mitochondrial complementation: mitochondria-specific system preventing mice from expression of disease phenotypes by mutant mtDNA. Nat Med 2001, 7:934-940
    • (2001) Nat Med , vol.7 , pp. 934-940
    • Nakada, K.1    Inoue, K.2    Ono, T.3    Isobe, K.4    Ogura, A.5    Goto, Y.I.6    Nonaka, I.7    Hayashi, J.I.8
  • 20
    • 34250339727 scopus 로고    scopus 로고
    • Contribution of the endothelium to the glomerular permselectivity barrier in health and disease
    • Ballermann BJ: Contribution of the endothelium to the glomerular permselectivity barrier in health and disease. Nephron Physiol 2007, 106:19-25
    • (2007) Nephron Physiol , vol.106 , pp. 19-25
    • Ballermann, B.J.1
  • 23
    • 35448995703 scopus 로고    scopus 로고
    • Transcription of mammalian cytochrome c oxidase subunit IV-2 is controlled by a novel conserved oxygen responsive element
    • Hüttemann M, Lee I, Liu J, Grossman LI: Transcription of mammalian cytochrome c oxidase subunit IV-2 is controlled by a novel conserved oxygen responsive element. FEBS J 2007, 274:5737-5748
    • (2007) FEBS J , vol.274 , pp. 5737-5748
    • Hüttemann, M.1    Lee, I.2    Liu, J.3    Grossman, L.I.4
  • 24
  • 25
    • 0042768716 scopus 로고    scopus 로고
    • Cytochrome c oxidase of mammals contains a testes-specific isoform of subunit VIb - The counterpart to testes-specific cytochrome c?
    • Hüttemann M, Jaradat S, Grossman LI: Cytochrome c oxidase of mammals contains a testes-specific isoform of subunit VIb - the counterpart to testes-specific cytochrome c? Mol Reprod Dev 2003, 66:8-16
    • (2003) Mol Reprod Dev , vol.66 , pp. 8-16
    • Hüttemann, M.1    Jaradat, S.2    Grossman, L.I.3
  • 26
    • 0035804655 scopus 로고    scopus 로고
    • Mammalian subunit IV isoforms of cytochrome c oxidase
    • Hüttemann M, Kadenbach B, Grossman LI: Mammalian subunit IV isoforms of cytochrome c oxidase. Gene 2001, 267:111-123
    • (2001) Gene , vol.267 , pp. 111-123
    • Hüttemann, M.1    Kadenbach, B.2    Grossman, L.I.3
  • 30
    • 33746929896 scopus 로고    scopus 로고
    • Copper trafficking to the mitochondrion and assembly of copper metalloenzymes
    • Cobine PA, Pierrel F, Winge DR: Copper trafficking to the mitochondrion and assembly of copper metalloenzymes. Biochim Biophys Acta 2006, 1763:759-772
    • (2006) Biochim Biophys Acta , vol.1763 , pp. 759-772
    • Cobine, P.A.1    Pierrel, F.2    Winge, D.R.3
  • 32
    • 0037090630 scopus 로고    scopus 로고
    • Copper supplementation restores cytochrome c oxidase activity in cultured cells from patients with SCO2 mutations
    • Salviati L, Hernandez-Rosa E, Walker WF, Sacconi S, DiMauro S, Schon EA, Davidson MM: Copper supplementation restores cytochrome c oxidase activity in cultured cells from patients with SCO2 mutations. Biochem J 2002, 363:321-327
    • (2002) Biochem J , vol.363 , pp. 321-327
    • Salviati, L.1    Hernandez-Rosa, E.2    Walker, W.F.3    Sacconi, S.4    DiMauro, S.5    Schon, E.A.6    Davidson, M.M.7
  • 33
    • 1842433755 scopus 로고    scopus 로고
    • Reversion of hypertrophic cardiomyopathy in a patient with deficiency of the mitochondrial copper binding protein Sco2: Is there a potential effect of copper?
    • Freisinger P, Horvath R, Macmillan C, Peters J, Jaksch M: Reversion of hypertrophic cardiomyopathy in a patient with deficiency of the mitochondrial copper binding protein Sco2: is there a potential effect of copper? J Inher Metab Dis 2004, 27:67-79
    • (2004) J Inher Metab Dis , vol.27 , pp. 67-79
    • Freisinger, P.1    Horvath, R.2    Macmillan, C.3    Peters, J.4    Jaksch, M.5
  • 35
    • 0034728367 scopus 로고    scopus 로고
    • From redox flow to gene regulation: Role of the PrrC protein of Rhodobacter sphaeroides 2.4.1
    • Eraso JM, Kaplan S: From redox flow to gene regulation: role of the PrrC protein of Rhodobacter sphaeroides 2.4.1. Biochemistry 2000, 39:2052-2062
    • (2000) Biochemistry , vol.39 , pp. 2052-2062
    • Eraso, J.M.1    Kaplan, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.