Premium
Mitochondrial Complex I Deficiency in Parkinson's Disease
Author(s) -
Schapira A. H. V.,
Cooper J. M.,
Dexter D.,
Clark J. B.,
Jenner P.,
Marsden C. D.
Publication year - 1990
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1990.tb02325.x
Subject(s) - substantia nigra , mptp , parkinsonism , parkinson's disease , respiratory chain , mitochondrial respiratory chain , cytochrome c oxidase , mitochondrion , reductase , neurotoxin , biochemistry , biology , chemistry , enzyme , medicine , disease
The structure and function of mitochondrial respiratory‐chain enzyme proteins were studied postmortem in the substantia nigra of nine patients with Parkinson's disease and nine matched controls. Total protein and mitochondrial mass were similar in the two groups. NADH‐ubiquinone reductase (Complex I) and NADH cytochrome c reductase activities were significantly reduced, whereas succinate cytochrome c reductase activity was normal. These results indicated a specific defect of Complex I activity in the substantia nigra of patients with Parkinson's disease. This biochemical defect is the same as that produced in animal models of parkinsonism by 1‐methyl‐4‐phenyl‐1,2,3,6‐tetrahydropyridine (MPTP) and adds further support to the proposition that Parkinson's disease may be due to an environmental toxin with action(s) similar to those of MPTP.