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Titolo:
Immunocytochemical characterization of the mitochondrially encoded ND1 subunit of complex I (NADH : ubiquinone oxidoreductase) in rat brain
Autore:
Pettus, EH; Betarbet, R; Cottrell, B; Wallace, DC; Madyastha, V; Greenamyre, JT;
Indirizzi:
Emory Univ, Dept Neurol, Atlanta, GA 30322 USA Emory Univ Atlanta GA USA 30322 Univ, Dept Neurol, Atlanta, GA 30322 USA Emory Univ, Dept Pharmacol, Atlanta, GA 30322 USA Emory Univ Atlanta GA USA 30322 iv, Dept Pharmacol, Atlanta, GA 30322 USA Emory Univ, Ctr Mol Med, Atlanta, GA 30322 USA Emory Univ Atlanta GA USA 30322 Univ, Ctr Mol Med, Atlanta, GA 30322 USA Emory Univ, Yerkes Reg Primate Res Ctr, Atlanta, GA 30322 USA Emory Univ Atlanta GA USA 30322 eg Primate Res Ctr, Atlanta, GA 30322 USA
Titolo Testata:
JOURNAL OF NEUROCHEMISTRY
fascicolo: 1, volume: 75, anno: 2000,
pagine: 383 - 392
SICI:
0022-3042(200007)75:1<383:ICOTME>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
HEREDITARY OPTIC NEUROPATHY; TOXIN 3-NITROPROPIONIC ACID; NADH-UBIQUINONE REDUCTASE; ELECTRON-TRANSPORT CHAIN; PARKINSONS-DISEASE; DIHYDROROTENONE BINDING; HUNTINGTONS-DISEASE; GLUTAMATE RECEPTORS; NEUROSPORA-CRASSA; DEHYDROGENASE;
Keywords:
mitochondria; complex I; mitochondrially encoded subunit I of NADH dehydrogenase (complex I); immunocytochemistry; complex IV;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
45
Recensione:
Indirizzi per estratti:
Indirizzo: Greenamyre, JT Emory Univ, Dept Neurol, WMRB 6000,1639 Pierce Dr, Atlanta,GA 30322 USA Emory Univ WMRB 6000,1639 Pierce Dr Atlanta GA USA 30322 SA
Citazione:
E.H. Pettus et al., "Immunocytochemical characterization of the mitochondrially encoded ND1 subunit of complex I (NADH : ubiquinone oxidoreductase) in rat brain", J NEUROCHEM, 75(1), 2000, pp. 383-392

Abstract

In Parkinson's disease, there is a selective defect in complex I of the electron transfer chain. To better understand complex I and its involvement in neurodegenerative disease, we raised an antibody against a conserved epitope of the human mitochondrially encoded subunit 1 of complex I (ND1). Antibodies were affinity purified and assessed by ELISA, immunoblotting, and immunocytochemistry. Immunoblots of brain homogenates from mouse, rat, and monkey brain showed a single 33-kDa band consistent with the predicted molecular mass of the protein. Subcellular fractionation showed the protein to beenriched in mitochondria, Immunocytochemistry in rat brain revealed punctate labeling in cell bodies and processes of neurons. Immunoreactivity generally co-localized with subunit IV of complex IV. In striatum, ND1 immunoreactivity was greatly enriched in large cholinergic neurons and neurons containing nitric oxide synthase, two cell populations that are resistant to excitotoxic and metabolic insults. In substantia nigra, many dopaminergic neurons had little ND1 immunoreactivity, which may help to explain their sensitivity to complex I inhibitors. In spinal cord, ND1 immunoreactivity was enriched in motor neurons. We conclude that complex I is differentially distributed across brain regions, between neurons and glia, and between types of neurons. This antibody should provide a valuable tool for assessing complexI in normal and pathological conditions.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/01/20 alle ore 08:58:37