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Biomedical subjects

J Nordmann

Publications and source records attributed to J Nordmann.

At least 37 records · Page 2Linked to original sources
PubMed1981

2-Mercaptoacetate administration depresses the beta-oxidation pathway through an inhibition of long-chain acyl-CoA dehydrogenase activity.

To elucidate the mechanisms through which 2-mercaptoacetate administration inhibits fatty acid oxidation in the liver, the respiration rates induced by different substrates were studied polarographically in rat hepatic mitochondria isolated 3 h after 2-mercaptoacetate administration. Palmitoyl-L-carnitine oxidation was almost completely inhibited in either the absence or presence of malonate. Octanoate oxidation was also inhibited, and the intramitochondrial acyl-CoA content was markedly increased. The oxidation rate of pyruvate and 2-oxoglutarate on the one hand and of 3-hydroxybutyrate, succinate and glutamate on the other was either normal or only slightly decreased. In the presence of 2,4-dinitrophenol, the extent of the inhibition of palmitoyl-L-carnitine oxidation was unchanged. All these results are consistent with the hypothesis that the 2-mercaptoacetate inhibition of fatty acid oxidation is due to an inhibition of the beta-oxidation pathway itself. Finally, the mitochondrial defect responsible for this inhibition was shown to be an inhibition of palmitoyl-CoA dehydrogenase activity (EC 1.3.99.3).

Acyl-CoA Dehydrogenase, Long-Chain↗
PubMed1981

Effect of glucagon on ethanol oxidation in isolated rat liver cells.

Addition of glucagon 5 min after ethanol was found to stimulate the rate of ethanol oxidation in hepatocytes isolated from starved rats. This stimulation is of the same order of magnitude as that mediated by asparagine. The glucagon effect is suppressed by antiproteolytic agents such as insulin or NH4Cl. The stimulating effect of glucagon on ethanol oxidation is probably linked to enhanced proteolysis and an elevated glutamate level in the hepatocytes.

Ammonium Chloride↗
PubMed1981

Liver lipid disposal following t-butanol administration to rats.

Oral administration of a single dose of t-butanol (25 mmol/kg body wt.) to female Wistar rats results in an accumulation of triacylglycerols (TAGs) in the liver. This administration induces an early increase in the rate of palmitate uptake by the liver and a delayed enhancement of the blood free fatty acid (FFA) level. Whereas hepatic lactate/pyruvate ratio and liver fatty acid oxidation appear unimpaired, a highly significant enhancement of palmitate incorporation into liver TAGs occurs after t-butanol administration. This administration impairs the biosynthesis and/or secretion of very low density lipoproteins (VLDLs) as shown by the decrease in both the serum TAG level and the palmitate incorporation into serum TAGs. These data suggest that the metabolic disturbances reported may be related to the stress induced by the administration of t-butanol which is very slowly metabolized, as shown by the sustained blood alcohol level found over a 20-h period. This study also provides evidence that metabolism through the alcohol dehydrogenase (ADH) pathway is not a prerequisite for the ability of an alcohol to induce a fatty liver when administered to rats.

Animals↗
PubMed1981

[Anything new concerning the human lens and senile cataract (author's transl)].

Many differences exist between human and animal lenses. Firstly, ATP concentrations in human lenses remain relatively unchanged during aging, despite slowing down of carbohydrate metabolism. Secondly, growth rate, expressed either by fresh weight or by volume, decreases with age, but this evolution is much less pronounced in human than in animal lenses and in the former never stops completely. This protein synthesis appears to be reduction in a very important pathogenic factor in senile cataract. This opinion is strengthened by the fact that ATP, which hardly decreases with age in human lenses, diminishes only in the last stages of senile cataract, whereas the deficiency in protein synthesis is an early phenomenon, and precedes the first opacities. Incorporation of amino acids into soluble lens protein in vitro can be stimulated by adding to the culture medium, 5 m M dibutyryl c AMP protected by 0,5 m M isobutylmethylxanthine. Topical application to the eye of a few drops confirmed penetration of the c AMP into the lens. The theoretical possibility, always denied, of a preventive or stabilizing medicinal treatment for senile cataract, does, therefore, exist.

Adenosine Triphosphate↗
PubMed1980

Evidence against the involvement of cyclic GMP in the insulin-stimulation of lipoprotein lipase activity in fat cells.

Under in vitro experimental conditions in which insulin increases adipose tissue lipoprotein lipase, cyclic GMP or dibutyryl cyclic GMP has no effect on this enzyme in rat adipose tissue fragments, or on either the intra- or extracellular forms of this enzyme in isolated fat cells. These results do not support the involvement of cyclic GMP in the insulin-stimulation of lipoprotein lipase in adipose tissue.

Adipose Tissue↗
PubMed1980

Comparative study of the effect of amino acids on ethanol oxidation in isolated hepatocytes from starved and fed rats.

The effects of the various naturally occurring amino acids on ethanol oxidation in hepatocytes from 18-hrs starved and fed rats were studied. In order to minimize the non-ADH pathways and to avoid interference with the liver amino acid uptake the ethanol concentration used was 4 mM, the amino acids being added at the same concentration. In hepatocytes from starved rats, asparagine, serine, ornithine, hydroxyproline, histidine, cysteine, alanine, glycine, glutamate, glutamine, aspartate and arginine significantly increase ethanol consumption. The stimulatory effect of glutamine being much less pronounced than the asparagine one and proline being devoid of action, the influence of ammonium chloride addition on ethanol consumption in the presence of these amino acids was studied. Ammonium chloride determines an enhancement of ethanol oxidation, the results showing, contrarily to previous data, no apparent correlation between intracellular glutamate concentration and ethanol oxidation rate but rather a relation with aspartate concentration. In hepatocytes from fed rats alanine, asparagine, cysteine, glycine, hydroxyproline, ornithine and serine still increase ethanol oxidation, although to a lesser extent than in cells from starved rats. It appears that only amino acids which are precursors of either pyruvate or aspartate or glutamate are able to activate the ethanol oxidation. Pyruvate, aspartate and glutamate supply malate-aspartate shuttle components especially in cells from starved rats, pyruvate allowing direct cytosolic reoxidation of NADH in cells from fed rats as well as from starved rats. The relative strengths of the stimulatory effect could be roughly dependent on energy demand for glucose synthesis in starved rats and for urea synthesis in fed rats.

Adenosine Triphosphate↗
PubMed1980

Acute ethanol effects on rat liver tryptophan oxygenase and tyrosine aminotransferase.

In starved rats, ethanol administered acutely enhances tryptophan oxygenase (TO) and tyrosine aminotransferase (TAT) activities. Ethanol also inhibits the early phase of the cortisol-mediated TO and TAT induction. Ethanol administered at the same time as tryptophan does not modify the tryptophan-mediated TO and TAT induction. In cortisol-pretreated rats, ethanol enhances the subsequent TO and TAT induction whereas no additive effects are observed when ethanol is injected together with tryptophan. These results suggest that ethanol mimics the effects of tryptophan on TO and TAT activities. In fed animals, ethanol alone does not result in increased TO and TAT activities, but inhibits their cortisol induction. It increases TO activities when given together with a tryptophan dose which, when given alone, does not enhance these activities. It is suggested that the observed inhibitory effects of ethanol on cortisol-mediated TO and TAT induction in starved and fed animals are related to a defective cortisol transport in the liver cells.

Alcoholic Intoxication↗
PubMed1979

Comparative effects of ethanol, n-propranol and isopropanol on lipid disposal by rat liver.

Besides ethanol, other aliphatic alcohols such as n-propanol and isopropanol induce a triacylglycerol (TAG) accumulation in the liver. To determine whether a common mechanism is responsible for the effects of these three alcohols on hepatic lipid metabolism, each was administered by gastric tube to female Wistar rats at the dose of 50 mmol/kg body wt. Whichever alcohol was administered, the hepatic triacylglycerol accumulation was found to be related to the duration of elevated blood alcohol concentration. After administration of n-propanol or isopropanol, the liver [14C]palmitate uptake was increased whereas hepatic palmitate oxidation to 14CO2 was impaired and palmitate esterification into TAG enhanced; these perturbations were however more discrete than after ethanol administration. In contrast to ethanol and n-propanol which, at the dose presently used, increase precursor incorporation into blood TAG, isopropanol inhibits this incorporation. Interference with the process of very low density lipoprotein (VLDL) synthesis and/or secretion, which appears only at a late stage of isopropanol intoxication, is probably responsible for the intensity and duration of the fatty liver observed after administration of this alcohol.

1-Propanol↗
PubMed1979

[Effect of natural amino acids on ethanol oxidation in isolated rat hepatocytes].

The effects of the various naturally occurring amino acids on ethanol oxidation in hepatocytes from starved rats was systematically studied. In order to minimize the non ADH pathways, the ethanol concentration used was 4 mmol/litre, the amino acids being added at the same concentration. In hepatocytes from fasted rats, alanine, arginine, asparagine, aspartate, citrulline, cysteine, glutamate, glutamine, glycine, histidine, hydroxyproline, ornithine and serine increase significantly ethanol consumption. The stimulatory effect of glutamine being much less pronounced than the asparagine one and proline being devoid of action, the influence of ammonium chloride addition on ethanol consumption in the presence of these amino acids was studied. Ammonium chloride determines an enhancement of ethanol oxidation in these conditions, the results showing no apparent correlation between intracellular glutamate concentration and ethanol oxidation rate, contrarily to previous data. In hepatocytes from fed rats, only alanine, asparagine, cysteine, glycine, hydroxyproline, ornithine and serine increase ethanol oxidation, although to a lesser extent than in cells from starved rats.

Amino Acids↗
PubMed1978

Loss of the lipoprotein lipase activating ability of rat serum after administration of some fatty liver inducing drugs.

The effects of the administration of different fatty liver inducing drugs on the serum lipoprotein lipase activating ability was investigated in rats. Addition of serum from 2-mercaptoethanol-, 2-mercaptoacetate-, ethionine- or D-galactosamine- treated rats failed to activate heart and adipose tissue lipoprotein lipase from control rats. The activating effect of serum was only slightly reduced in isopropanol-treated rats, whereas it was found unaffected in ethanol-treated ones. Electrophoresis of the lipoproteins and of the very low density lipoproteins (VLDL) fraction of sera from 2-mercaptoethanol-, 2-mercaptoacetate-, isopropanol-, ethionine- and D-galactosamine-treated rats suggest that the lack of lipoprotein lipase activation ability of these sera is most probably related to the impairing effects of these drugs upon VLDL metabolism, i.e. reduction of VLDL secretion in the case of 2-mercaptoethanol, 2-mercaptoacetate and isopropanol, production of abnormal VLDL in the case of D-galactosamine and both decreased VLDL secretion and production of abnormal VLDL in the case of ethionine.

1-Propanol↗
PubMed1977

Role and mechanism of peripheral fatty acid mobilization in 2-mercaptoethanol-induced fatty liver.

2-Mercaptoethanol-induced fatty liver involves an increased free fatty acid mobilization which is primarily due to an inhibition of free fatty acid reesterification in adipose tissue. Furthermore, increased free fatty acid mobilization as well as fatty liver induction are not induced by 2-mercaptoethanol per se but result most probably from 2-mercaptoacetate through oxidation of 2-mercaptoethanol.

Adenosine Triphosphate↗