Perspectives In Cell Physiology Human NADH:ubiquinone oxidoreductase deficiency: radical changes in mitochondrial morphology?
نویسندگان
چکیده
Werner J. H. Koopman, Sjoerd Verkaart, Henk Jan Visch, Sjenet van Emst-de Vries, Leo G. J. Nijtmans, Jan A. M. Smeitink, and Peter H. G. M. Willems Department of Membrane Biochemistry, Nijmegen Centre for Molecular Life Sciences, Department of Paediatrics, Nijmegen Centre for Mitochondrial Disorders, and Microscopical Imaging Centre of the Nijmegen Centre for Molecular Life Sciences, Radboud University Nijmegen Medical Centre, Nijmegen, The Netherlands
منابع مشابه
Human NADH:ubiquinone oxidoreductase deficiency: radical changes in mitochondrial morphology?
Malfunction of NADH:ubiquinone oxidoreductase or complex I (CI), the first and largest complex of the mitochondrial oxidative phosphorylation system, has been implicated in a wide variety of human disorders. To demonstrate a quantitative relationship between CI amount and activity and mitochondrial shape and cellular reactive oxygen species (ROS) levels, we recently combined native electrophore...
متن کاملMitochondrial network complexity and pathological decrease in complex I activity are tightly correlated in isolated human complex I deficiency.
Complex I (NADH:ubiquinone oxidoreductase) is the largest multisubunit assembly of the oxidative phosphorylation system, and its malfunction is associated with a wide variety of clinical syndromes ranging from highly progressive, often early lethal, encephalopathies to neurodegenerative disorders in adult life. The changes in mitochondrial structure and function that are at the basis of the cli...
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Alternative NADH:ubiquinone oxidoreductases are single subunit enzymes capable of transferring electrons from NADH to ubiquinone without contributing to the proton gradient across the respiratory membrane. The obligately aerobic yeast Yarrowia lipolytica has only one such enzyme, encoded by the NDH2 gene and located on the external face of the mitochondrial inner membrane. In sharp contrast to ...
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Complex I (NADH:ubiquinone oxidoreductase) is central to cellular NAD(+) recycling and accounts for approximately 40% of mitochondrial ATP production. To understand how complex I function impacts respiration and plant development, we isolated Arabidopsis (Arabidopsis thaliana) lines that lack complex I activity due to the absence of the catalytic subunit NDUFV1 (for NADH:ubiquinone oxidoreducta...
متن کاملMitochondrial fluidity matters. Focus on "Inherited complex I deficiency is associated with faster protein diffusion in the matrix of moving mitochondria".
Mitochondria continuously change shape, position, and matrix configuration for optimal metabolite exchange. It is well established that changes in mitochondrial metabolism influence mitochondrial shape and matrix configuration. We demonstrated previously that inhibition of mitochondrial complex I (CI or NADH:ubiquinone oxidoreductase) by rotenone accelerated matrix protein diffusion and decreas...
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