Metabolism of carnitine and coenzyme a esters of palmitic acid intermediates in liver mitochondria

Al-Arif, Adhid; Blecher, Melvin

doi:10.1016/0005-2760(71)90229-3

Cited by 19 publications

(15 citation statements)

References 18 publications

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“…The low free carnitine concentration with a high concentration of acylated carnitine in the plasma from the patient is probably secondary to impaired fatty acid oxidation (46). Both 3-hydroxyacyl-CoA esters and 3-hydroxyacylcarnitine esters are substrates for carnitine palmitoyltransferase (47). Further, rat liver mitochondria fractions oxidizing hexadecanoyl-carnitine in the presence of rotenone form 3-hydroxyhexadecanoyl-carnitine (19 (48).…”

Section: Resultsmentioning

confidence: 99%

Impaired mitochondrial beta-oxidation in a patient with an abnormality of the respiratory chain. Studies in skeletal muscle mitochondria.

Watmough

Bindoff²,

Birch‐Machin³

et al. 1990

J. Clin. Invest.

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Defects of complex I of the mitochondrial respiratory chain are important causes of neurological disease. We report studies that demonstrate a severe deficiency of complex I activity with less severe abnormalities of complexes III and IV (< 5, 63, and 30% of control values, respectively) in a skeletal muscle mitochondrial fraction from a 22-yr-old female with weakness, lactic acidemia, and the deposition of intramuscular neutral lipid. The observation that lipid accumulates in this and other patients with complex I deficiency suggests impaired mitochondrial fatty acid oxidation. To investigate this mechanism we have shown impaired flux through ft-oxidation ([U-"Cjhexadecanoate oxidation was 66% of control rate) and accumulation of specific acyl-CoA ester intermediates. The changes in fatty acid metabolism in complex I deficiency are secondary to the reduced state within the mitochondrial matrix with low NAD+/NADH ratios. (J. Clin. Invest. 1990. 85:177-184.) ,Boxidation -complex I * mitochondria

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Section: Resultsmentioning

confidence: 99%

Impaired mitochondrial beta-oxidation in a patient with an abnormality of the respiratory chain. Studies in skeletal muscle mitochondria.

Watmough

Bindoff²,

Birch‐Machin³

et al. 1990

J. Clin. Invest.

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“…The fatty acyl CoA's were prepared by the methods of Al-Arif and Blecher (17) and Kawanami (18), with modifications made to compensate for the fact that labeled fatty acids were involved and for the special needs of the less soluble, less reactive longer chain acids.…”

Section: Methodsmentioning

confidence: 99%

Enzymatic formation of hydroxy ceramides and comparison with enzymes forming nonhydroxy ceramides

Ullman¹,

Radin²

1972

Archives of Biochemistry and Biophysics

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Radioactive 2-hydroxystearic and cerebronic acids were converted to the coensyme A thio esters, then tested for reactivity with n-sphingosine. Microsomes from mouse brain were found to catalyze the formation of ceramides containing both hydroxy acids. Both the D-and L-forms of the hydroxy acids reacted. Comparisons of reactivity were made with stearoyl and lignoceroyl CoA, the analogous nonhydroxy acids, which also form ceramides. The ratios of activities of the substrates were found to vary with animal age, with various subcellular fractions, with different rat brain cell preparations, and with different mouse organs. Competition experiments with mixtures of thio ester substrates showed that stearate and lignocerate did not interfere with each other in the formation of ceramide, but hydroxystearoyl CoA inhibited the utilization of the two nonhydroxy substrates and cerebronoyl CoA inhibited the utilization of lignoceroyl CoA. The kinetics of the inhibitions indicated that the effects were noncompetitive. A similar type of inhibition was seen with stearoyl CoA against hydroxystearate incorporation, On the basis of these findings, we suggest that four different enzymes are involved in the acyl transfer reaction: for stearate, hydroxystearate, lignocerate, and cerebronate. Neuronal cell preparations were found to be relatively rich in stearate transferase, while glial cells were relatively rich in hydroxystearate and lignocerate transferases.Ceramides (the fatty acyl amides of sphingosine and related long chain bases) are the precursors of the sphingoglycolipids and, perhaps, of sphingomyelin (l-6). The NFA3 ceramides are converted to galactocerebroside (2) and glucocerebroside (2, 3) while the HFA ceramides are converted to galactocerebroside (1, 4). A curious feature becomes evident when the chain lengths of the fatty acids are examined: two clusters are seen, centering around the Cl8 acids and

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“…radioact. 177 mCi/mmol) was a product of The Radiochemical Centre, Amersham, U.K. Palmitoyl-CoA was synthesized according to the method of Al-Arif and Blecher [20]. Sephadex G-50 (fine) and Sepharose 4B were products from Pharmacia, Sweden.…”

Section: Methodsmentioning

confidence: 99%

Characterization of reconstituted partially purified glycerophosphate acyltransferase from Escherichia coli

Kessels

Bosch

1982

Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metaboli

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Metabolism of carnitine and coenzyme a esters of palmitic acid intermediates in liver mitochondria

Cited by 19 publications

References 18 publications

Impaired mitochondrial beta-oxidation in a patient with an abnormality of the respiratory chain. Studies in skeletal muscle mitochondria.

Impaired mitochondrial beta-oxidation in a patient with an abnormality of the respiratory chain. Studies in skeletal muscle mitochondria.

Enzymatic formation of hydroxy ceramides and comparison with enzymes forming nonhydroxy ceramides

Characterization of reconstituted partially purified glycerophosphate acyltransferase from Escherichia coli

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