Extensive Defects of Mitochondrial Electron-Transfer Chain in Muscular Cytochrome c Oxidase Deficiency

Tanaka, Masashi; Miyabayashi, Shigeaki; Nishikimi, Morimitsu; Suzuki, Hiroshi; Shimomura, Yoshiharu; Ito, Ken; Narisawa, Kuniaki; Tada, Keiya; Ozawa, Takayuki

doi:10.1203/00006450-198810000-00006

Cited by 35 publications

(10 citation statements)

References 23 publications

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“…The antibodies against mitochondrial complex I, III and IV were prepared and characterized as reported (Tanaka et al, 1988).…”

Section: Methodsmentioning

confidence: 99%

“…The presence of 3-NT-immunoreactive protein bands was examined in polypeptide composition of mitochondrial complex I-IV, using antibodies against mitochondria complexes (Tanaka et al, 1988), by Western blot analyses after sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) or two-dimensional electrophoresis. The effects of ONOO Ϫ on the protein nitration and the viability of SH-SY5Y cells were studied by use of an ONOO Ϫ -generating agent, Nmorpholinosydonimine (SIN-1).…”

Section: Introductionmentioning

confidence: 99%

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Selective nitration of mitochondrial complex I by peroxynitrite: involvement in mitochondria dysfunction and cell death of dopaminergic SH-SY5Y cells

Yamamoto

Maruyama

Kato

et al. 2002

Journal of Neural Transmission

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3-Nitrotyrosine (3-NT) is a specific marker of protein nitration by peroxynitrite (ONOO-) produced from nitric oxide and superoxide. Increase in 3-NT containing protein (3-NT protein) was reported in brains from patients with some neurodegenerative disorders and aging. In this paper, intracellular localization of 3-NT protein was examined in dopaminergic SH-SY5Y cells using the selective antibody against protein-bound 3-NT. 3-NT protein was detected in plasma membrane/nucleus and mitochondria fractions, and interestingly in polypeptide composition of mitochondrial complex I. ONOO--generating SIN-1 induced apoptotic cell death with concomitant increase in 3-NT protein and reduction in mitochondrial ATP synthesis. In addition, an inhibitor of proteasomes, carbobenzoxy-L-isoleucyl-gamma-t-butyl-L-glutamyl-L-alanyl-L-leucinal, enhanced the effects of ONOO-. These results suggest that ONOO- may induce mitochondrial dysfunction and cell death in neurons through nitration of mitochondrial complex I subunits.

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“…The antibodies against mitochondrial complex I, III and IV were prepared and characterized as reported (Tanaka et al, 1988).…”

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Selective nitration of mitochondrial complex I by peroxynitrite: involvement in mitochondria dysfunction and cell death of dopaminergic SH-SY5Y cells

Yamamoto

Maruyama

Kato

et al. 2002

Journal of Neural Transmission

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“…Mitochondria1 proteins separated in the gel were electrophoretically transferred to a Durapore GVHP filter (Millipore Continental Water Systems, Bedford, MA) essentially according to the method of Towbin et al (26) with addition of 0.1% SDS to the electrode buffer. The binding of antibodies to the subunits of the mitochondrial enzymes on the filter was detected by the peroxidase-antiperoxidase method, as described previously (27,28). The immunoblot strips were analyzed densitometrically using a CS-930 chromatoscanner (Shimazu Corporation, Kyoto, Japan).…”

Section: Methodsmentioning

confidence: 99%

Disproportionate Deficiency of Iron-Sulfur Clusters and Subunits of Complex I in Mitochondrial Encephalomyopathy

Ichiki¹,

Tanaka

Kobayashi³

et al. 1989

Pediatr Res

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ABSTRACT. To investigate the molecular abnormality in the mitochondria from various tissues of an autopsied patient exhibiting mitochondrial myopathy, encephalopathy, lactic acidosis, and stroke-like episodes, we have examined the enzymatic activity, iron-sulfur cluster, and subunit composition of the NADH-ubiquinone oxidoreductase (complex I). Rotenone-sensitive NADH-cytochrome c reductase activity was found to be decreased in all the tissues examined. A detailed study of the liver mitochondria has shown that NADH-ubiquinone oxidoreductase activity was greatly diminished. Analysis of the electron paramagnetic resonance spectra of the liver submitochondrial particles revealed a disproportionate deficiency of iron-sulfur clusters in the complex I segment of the respiratory chain. Signals from the clusters N-2 and N-3 diminished more drastically than those from clusters N-lb and N-4. Immunoblotting analysis showed that the 75-kD, 51-kD, and several other subunits were markedly diminished among multiple subunit polypeptides of complex I. These findings suggest that the underlying bases for mitochondrial myopathy, encephalopathy, lactic acidosis, and stroke-like episodes are defects, at least, in the complex I subunits containing a flavin and/or iron-sulfur cluster(s), which resulted in deficiencies of some iron-sulfur clusters.

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“…To examine the reversibility of glutathionylation, parts of the samples were treated with the SDS sample buffer containing 5% b-mercaptoethanol and subjected to SDS-PAGE. To identify PrS-SG in mitochondrial complex I and III, the polyclonal antibodies against complex I and III were used (Tanaka et al 1988).…”

Section: Assay For Activities Of Caspasementioning

confidence: 99%

Neuromelanin selectively induces apoptosis in dopaminergic SH‐SY5Y cells by deglutathionylation in mitochondria: involvement of the protein and melanin component

Naoi¹,

Maruyama

Yi³

et al. 2008

Journal of Neurochemistry

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Parkinson’s disease (PD) is characterized by selective depletion of nigral dopamine (DA) neurons containing neuromelanin (NM), suggesting the involvement of NM in the pathogenesis. This study reports induction of apoptosis by NM in SH‐SY5Y cells, whereas protease‐K‐treated NM, synthesized DA‐ and cysteinyl dopamine melanin showed much less cytotoxicity. Cell death was mediated by mitochondria‐mediated apoptotic pathway, namely collapse of mitochondrial membrane potential, release of cytochrome c, and activation of caspase 3, but Bcl‐2 over‐expression did not suppress apoptosis. NM increased sulfhydryl content in mitochondria, and a major part of it was identified as GSH, whereas dopamine melanin significantly reduced sulfhydryl levels. Western blot analysis for protein‐bound GSH demonstrated that only NM reduced S‐glutathionylated proteins in mitochondria and dissociated macromolecular structure of complex I. Reactive oxygen and nitrogen species were required for the deglutathionylation by NM, which antioxidants reduced significantly with prevention of apoptosis. These results suggest that NM may be related to cell death of DA neurons in PD and aging through regulation of mitochondrial redox state and S‐glutathionylation, for which NM‐associated protein is absolutely required. The novel function of NM is discussed in relation to the pathogenesis of PD.

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Extensive Defects of Mitochondrial Electron-Transfer Chain in Muscular Cytochrome c Oxidase Deficiency

Cited by 35 publications

References 23 publications

Selective nitration of mitochondrial complex I by peroxynitrite: involvement in mitochondria dysfunction and cell death of dopaminergic SH-SY5Y cells

Selective nitration of mitochondrial complex I by peroxynitrite: involvement in mitochondria dysfunction and cell death of dopaminergic SH-SY5Y cells

Disproportionate Deficiency of Iron-Sulfur Clusters and Subunits of Complex I in Mitochondrial Encephalomyopathy

Neuromelanin selectively induces apoptosis in dopaminergic SH‐SY5Y cells by deglutathionylation in mitochondria: involvement of the protein and melanin component

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