Antimitochondrial effect of saturated medium chain length (C8-C13) dicarboxylic acids

Siro Passi; Mauro Picardo; Marcella Nazzaro-Porro; Aodan Breathnach; Anna Maria Confaloni; Giovanni Serlupi-Crescenzi

doi:10.1016/0006-2952(84)90376-9

Antimitochondrial effect of saturated medium chain length (C8-C13) dicarboxylic acids

Siro Passi, Mauro Picardo, Marcella Nazzaro-Porro, Aodan Breathnach, Anna Maria Confaloni, Giovanni Serlupi-Crescenzi

Istituto S. Maria e S. Gallicano

Research output: Contribution to journal › Article › peer-review

Abstract

In isolated rat liver mitochondria, respiration was competitively inhibited by medium chain length (C₈ to C₁₃) dicarboxylic acids to different extents: the higher the number of carbon atoms up to C₁₂, the greater the inhibition. In particular, experiments on submitochondrial particles showed that the competitive inhibition concerned the following enzymes: NADH dehydrogenase, succinic dehydrogenase and reduced ubiquinone: cytochrome c oxido-reductase. These results tend to confirm the suggestion that the melanocytotoxic effect of dicarboxylic acids, which are also competitive inhibitors of tyrosinase, may be primarily due to an antimitochondrial effect rather than being tyrosinase-dependent.

Original language	English
Pages (from-to)	103-108
Number of pages	6
Journal	Biochemical Pharmacology
Volume	33
Issue number	1
DOIs	https://doi.org/10.1016/0006-2952(84)90376-9
Publication status	Published - Jan 1 1984

ASJC Scopus subject areas

Pharmacology

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title = "Antimitochondrial effect of saturated medium chain length (C8-C13) dicarboxylic acids",

abstract = "In isolated rat liver mitochondria, respiration was competitively inhibited by medium chain length (C8 to C13) dicarboxylic acids to different extents: the higher the number of carbon atoms up to C12, the greater the inhibition. In particular, experiments on submitochondrial particles showed that the competitive inhibition concerned the following enzymes: NADH dehydrogenase, succinic dehydrogenase and reduced ubiquinone: cytochrome c oxido-reductase. These results tend to confirm the suggestion that the melanocytotoxic effect of dicarboxylic acids, which are also competitive inhibitors of tyrosinase, may be primarily due to an antimitochondrial effect rather than being tyrosinase-dependent.",

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AU - Passi, Siro

AU - Picardo, Mauro

AU - Nazzaro-Porro, Marcella

AU - Breathnach, Aodan

AU - Confaloni, Anna Maria

AU - Serlupi-Crescenzi, Giovanni

PY - 1984/1/1

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AB - In isolated rat liver mitochondria, respiration was competitively inhibited by medium chain length (C8 to C13) dicarboxylic acids to different extents: the higher the number of carbon atoms up to C12, the greater the inhibition. In particular, experiments on submitochondrial particles showed that the competitive inhibition concerned the following enzymes: NADH dehydrogenase, succinic dehydrogenase and reduced ubiquinone: cytochrome c oxido-reductase. These results tend to confirm the suggestion that the melanocytotoxic effect of dicarboxylic acids, which are also competitive inhibitors of tyrosinase, may be primarily due to an antimitochondrial effect rather than being tyrosinase-dependent.

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