Stimulation of oxidation of mitochondrial fatty acids and of acetate by acetylcarnitine

Siliprandi, N.; Siliprandi, D.; Ciman, M.

doi:10.1042/bj0960777

Cited by 69 publications

(28 citation statements)

References 11 publications

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“…Finally, ALC is in equilibrium with L-carnitine, which is an essential cofactor for the transport of long chain acyl groups from the cytosol to the mitochondrion (Bahl and Bressler, 1955;Bremer etal., 1983). From the preceding information it appears possible that ALC may protect from MPP + damage within the mitochondrion by (1) supplying energy at a downstream level, i.e., bypassing the NAD/NADH chain and shunting the oxidative metabolism of acylated high energy compounds (Fritz, 1963;Siliprandi et al, 1965), or (2) producing high energy compounds and NADH as a result of a degradation step in an overloaded carnitine-ALC system.…”

Section: Discussionmentioning

confidence: 97%

Acetyl-levo-carnitine protects against MPTP-induced parkinsonism in primates

Bódis-Wollner

Chung

Ghilardi

et al. 1991

J Neural Transm Gen Sect

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Acetyl-levo-carnitine (ALC) protects against 1-methyl, 4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)-induced toxicity in the nonhuman primate. ALC pretreated monkeys do not show signs of parkinsonism or electroretinographic changes typical of dopaminergic deficiency when given MPTP. In addition, pilot neurochemical and morphological data confirm a partial protection effect. While MAO-B inhibitors, like L-Deprenyl, are thought to protect dopaminergic neurons from MPTP-induced cell death by preventing the conversion of MPTP to its toxic metabolite MPP+, ALC is not known to have MAO-B affinity. Converging evidence suggests that ALC may affect directly mitochondrial respiration, which is known to be the target of MPP+ and affected in human neurodegenerative diseases, including Parkinson's disease. The results of this study point to new therapeutic avenues for the treatment of these nosologic entities.

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Section: Discussionmentioning

confidence: 97%

Acetyl-levo-carnitine protects against MPTP-induced parkinsonism in primates

Bódis-Wollner

Chung

Ghilardi

et al. 1991

J Neural Transm Gen Sect

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“…Samples of the enzyme containing 0.05 -0.5 nmol thiamine-P2 were applied to cellulose thin-layer chromatographic plates (Eastman) and chromatographed at room temperature with propan-1 -01/0.1 M sodium phosphate pH 4.9/H20 (6 : 2 : 2, v/v/v) [18]. Thiamine-Pz was oxidized to the fluorescent thiochrome-Pz with hexacyanoferrate(II1) in basic solution [19]. The fluorescent spot was scratched from the plate and extracted with 2.5 ml 0.01 M NaOH.…”

Section: Methodsmentioning

confidence: 99%

Irreversible Inactivation of Pyruvate Decarboxylase in the Presence of Substrate and an Oxidant. An Example of Paracatalytic Enzyme Inactivation

1979

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Pyruvate decarboxylase from yeast isoprogressively inactivated in the presence of pyruvate and an extrinsic oxidant such as 2,6-dichloroindophenol or hexacyanoferrate(II1). The inactivation is linked to the oxidation of the hydroxyethylthiamine diphosphate intermediate to acetate. Removal of low-molecular compounds by gel filtration does not reactivate the enzyme. The rate of inactivation obeys saturation kinetics with respect to substrate concentration and is independent of enzyme concentration. In analogy to the paracatalytic inactivation of other enzymes forming oxidizable carbanion intermediates Methods Enzymol.46, 48 -541, the oxidation of enzymebound hydroxyethylthiamine diphosphate is thought to generate a transiently reactive intermediate which, without being released from the enzyme, covalently modifies a group at or near the active site. Reconstitution experiments indicate that the protein rather than the coenzyme moiety is modified.

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“…Acetyl-L-carni tine (x-trimethyl-ß-acetylbutyrrobetaine, ALC) is the ace tyl ester of carnitine [6]. The reversible formation of ALC modulates, through the carnitine acetyltransferase en zymes, the intracellular concentrations of free coenzyme A (CoA) and acetyl-CoA [7], ALC can be freely exchanged across subcellular membranes and can serve as a pool of acetyl groups from which to regenerate acetyl-CoA [8], ALC.…”

Section: Introductionmentioning

confidence: 99%

Protection from Oxygen Radical Damage in Human Diploid Fibroblasts by Acetyl-<i>L</i>-Carnitine

Tesco¹,

Latorraca²,

Piersanti³

et al. 1992

Dement Geriatr Cogn Disord

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Oxygen radical production is suspected of being a major cause of aging. We have studied the effect of acetyl-L-carnitine (ALC) on oxygen metabolites toxicity in fibroblast cell lines derived from skin biopsies taken from apparently normal subjects. Fibroblast damage was produced by the generation of oxygen metabolites during the enzymatic oxidation of acetaldehyde with 50 mU of xanthine oxidase (XO). We measured lactate dehydrogenase (LDH) activity in the culture medium and cell viability in fibroblast cultures, both 4 days preincubated with 50 µg/ml ALC and not treated, after a 2-hour XO incubation in order to quantify the cell damage. We found a significant increase of LDH activity in cells without ALC exposed to free radical formation. No significant increase of the LDH activity was observed in the same cell lines, in the same experimental conditions after 4 days’ preincubation with 50 µg/ml ALC.

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Stimulation of oxidation of mitochondrial fatty acids and of acetate by acetylcarnitine

Cited by 69 publications

References 11 publications

Acetyl-levo-carnitine protects against MPTP-induced parkinsonism in primates

Acetyl-levo-carnitine protects against MPTP-induced parkinsonism in primates

Irreversible Inactivation of Pyruvate Decarboxylase in the Presence of Substrate and an Oxidant. An Example of Paracatalytic Enzyme Inactivation

Protection from Oxygen Radical Damage in Human Diploid Fibroblasts by Acetyl-<i>L</i>-Carnitine

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