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PubMed1978

[Metabolic activity of adipose tissue in the goat during gestation and at the beginning of lactation].

In 5 French Alpine goats, omental adipose tissue acetyl-CoA carboxylase, glucose-6-phosphate deshydrogenase, malic enzyme and lipoprotein lipase activities significantly decreased during the third month of gestation, whereas plasma non-esterified fatty acid and triacyglycerol contents increased. This probably reflects an early decreasing rate of adipose tissue anabolism during gestation in the Goat. At the third week of lactation, anabolic activities relative to DNA content of adipose tissue were extremely low, and the tissue weight relative to DNA was lower than during gestation. Metabolic alterations of omental adipose tissue in early lactation do not seem to be related to milk production level. These results could contribute to a better control of the kinetic of body lipid stores during the reproductive cycle in high milk yielding ruminants.

Acetyl-CoA Carboxylase↗

PubMed1984

Effect of acetate and octanoate on tricarboxylic acid cycle metabolite disposal during propionate oxidation in the perfused rat heart.

Tricarboxylic acid cycle pool size is determined by anaplerosis and metabolite disposal. The regulation of the latter during propionate metabolism was studied in isolated perfused rat hearts in the light of the characteristics of NADP-linked malic enzyme, which is inhibited by acetyl-CoA. The acetyl-CoA concentration was varied by infusions of acetate and octanoate, and the rate of metabolite disposal was calculated from a metabolic balance sheet compiled from the relevant metabolic fluxes. Propionate addition increased the tricarboxylic acid cycle pool size 4-fold and co-infusion of acetate or octanoate did not change it further. Propionate caused a decrease in the CoA-SH concentration and a 10-fold increase in the propionyl-CoA concentration. A paradoxical increase in the CoA-SH concentration was observed upon co-infusion of acetate in the presence of propionate, an effect probably caused by competitive inhibition of propionate activation. A more pronounced decline in the propionyl-CoA concentration was observed upon the co-infusion of octanoate. In a metabolic steady state, acetate and octanoate reduced propionate disposal only slightly, but did not increase the tricarboxylic acid cycle pool size. The results are in accord with the notion that the tricarboxylic acid pool size is mainly regulated by the anaplerotic mechanisms.

Acetates↗

PubMed1993

Photosynthesis in Phosphoenolpyruvate carboxykinase-type C4 plants: mechanism and regulation of C4 acid decarboxylation in bundle sheath cells.

The mechanism and regulation of C4 acid decarboxylation in phosphoenolpyruvate (PEP) carboxykinase-type C4 plants was examined in isolated bundle sheath cell strands. These cells decarboxylated added oxaloacetate to PEP at rates exceeding 2.5 mumol min-1 mg-1 chlorophyll when ATP was added. This requirement for ATP could be replaced by malate plus ADP; under these conditions this cytosol-located decarboxylation of oxaloacetate via PEP carboxykinase was sustained by respiratory ATP. It was confirmed that respiratory ATP production was linked primarily to the oxidative decarboxylation of malate via NAD malic enzyme. This process, measured as pyruvate production, was highly dependent on Pi. Besides being required to generate ATP, Pi had a second role which was probably associated with the transport of malate into mitochondria. Maximum rates of malate decarboxylation via NAD malic enzyme substantially exceeded the minimum rates necessary for providing ATP for cytosolic oxaloacetate decarboxylation. When malate was added with oxaloacetate, ADP and Pi rates of malate decarboxylation of between 3 and 4 mumol min-1 mg-1 chlorophyll were recorded. About half of this activity was sustained by the reoxidation of NADH coupled to reduction of oxaloacetate via malate dehydrogenase. When malate was added without oxaloacetic acid, respiration by these bundle sheath cells was stoichiometrically linked with the oxidation of malate to pyruvate. This malate-dependent respiration was stimulated by adding ADP or phosphorylation uncouplers; it was not significantly inhibited by including oxaloacetate. Possible mechanisms of regulation of the partitioning of C4 acid decarboxylation between PEP carboxykinase in the cytosol and mitochondrial NAD malic enzyme are discussed.

Carbonyl Cyanide m-Chlorophenyl Hydrazone↗

PubMed1987

Effect of long-term clofibric acid treatment on serum and tissue lipid and cholesterol levels in obese Zucker rats.

The long-term effects of clofibric acid (200 mg/kg body weight) injected subcutaneously from 6-36 weeks of age were assessed in obese, hyperlipemic Zucker rats. At 18 and 36 weeks of age, treated rats had significantly lower fasted serum cholesterol levels but triacylglycerol levels were not affected. Rats were killed at 36 weeks of age at which time there were no differences in body and kidney weights between control and clofibric acid-treated rats. Liver, spleen and heart weights were lowered by clofibric acid treatment. In liver there was an elevation of lipid/g due to treatment but there were no effects on cholesterol/g or on either total liver lipid or cholesterol levels. In the epididymal fat pad of clofibric acid-treated rats, there was a 21% elevation of cholesterol level on a per pad basis. In the other organs, there were no effects of treatment on lipid or cholesterol levels except for lowered total cholesterol in kidney. Several liver lipogenic enzymes were lowered by treatment but malic enzyme was two times higher.

Adipose Tissue↗

PubMed2000

Cerebral metabolism of lactate in vivo: evidence for neuronal pyruvate carboxylation.

The cerebral metabolism of lactate was investigated. Awake mice received [3-13C]lactate or [1-13C]glucose intravenously, and brain and blood extracts were analyzed by 13C nuclear magnetic resonance spectroscopy. The cerebral uptake and metabolism of [3-13C]lactate was 50% that of [1-13C]glucose. [3-13C]Lactate was almost exclusively metabolized by neurons and hardly at all by glia, as revealed by the 13C labeling of glutamate, gamma-aminobutyric acid and glutamine. Injection of [3-13C]lactate led to extensive formation of [2-13C]lactate, which was not seen with [1-13C]glucose, nor has it been seen in previous studies with [2-13C]acetate. This formation probably reflected reversible carboxylation of [3-13C]pyruvate to malate and equilibration with fumarate, because inhibition of succinate dehydrogenase with nitropropionic acid did not block it. Of the [3-13C]lactate that reached the brain, 20% underwent this reaction, which probably involved neuronal mitochondrial malic enzyme. The activities of mitochondrial malic enzyme, fumarase, and lactate dehydrogenase were high enough to account for the formation of [2-13C]lactate in neurons. Neuronal pyruvate carboxylation was confirmed by the higher specific activity of glutamate than of glutamine after intrastriatal injection of [1-14C]pyruvate into anesthetized mice. This procedure also demonstrated equilibration of malate, formed through pyruvate carboxylation, with fumarate. The demonstration of neuronal pyruvate carboxylation demands reconsideration of the metabolic interrelationship between neurons and glia.

Animals↗

PubMed1997

[U-13C]glutamate metabolism in rat brain mitochondria reveals malic enzyme activity.

13C nuclear magnetic resonance spectroscopy was used to study the activity of malic enzyme in isolated brain mitochondria from rat in the presence of unlabelled malate and [U-13C]glutamate. ADP, inorganic phosphate, malate and [U-13C]glutamate were added to a suspension of oxygenated mitochondria. Typical tricarboxylic acid (TCA) cycle constituents (malate, 2-oxoglutarate and succinate) were labelled from [U-13C]glutamate and detected in the superfusion medium. The labelling patterns in the different atom positions of glutamate revealed entry of both unlabelled and labelled acetyl-CoA into the TCA cycle. Unlabelled acetyl-CoA was derived via pyruvate from exogenously applied malate by the action of mitochondrial malic enzyme, while labelled acetyl-CoA was derived from TCA cycle intermediates, most likely by the action of mitochondrial malic enzyme on malate produced from [U-13C]glutamate. The results demonstrate malic enzyme activity and pyruvate recycling in isolated rat brain mitochondria.

Animals↗

PubMed1995

NADPH diaphorase is not inhibited by ethylenediaminetetraacetic acid and is not specific for nitric oxide synthase in the choroid plexus of rat and mouse.

NADPH diaphorase is a histochemical activity which, in formaldehyde-fixed tissue, is rather specific for nitric oxide synthase. Recently, it was shown that NADPH diaphorase activity is inhibited by ethylenediaminetetraacetic acid (EDTA) in neurons but not in the choroid plexus epithelium. The present study, while confirming these results, demonstrates that the apparent sensitivity of NADPH diaphorase for EDTA reflects only the dependence of malic enzyme, which is used as the source of reduced cofactor, on Mg2+ or Mn2+ ions. Furthermore, evidence is provided that the apparent EDTA-insensitive NADPH diaphorase activity in the choroid plexus reflects the activity of alkaline phosphatase in conjunction with NADH diaphorase. Apart from these pitfalls, the use of the indirect, malic enzyme based method for NADPH diaphorase was found to cause much higher background staining compared to the direct method using NADPH, and is therefore proposed to be abandoned.

Animals↗

PubMedDate not supplied

Relationship between enzymatic activity loss and post-translational protein modification in aging.

During aging, there is a decrease in the activity of many enzymes. The mechanism causing the loss of activity is still not well understood in most cases. We have studied the decrease in the activities of the malic, 6-phosphogluconate dehydrogenase and superoxide dismutase enzymes. The old malic enzyme is about 36% less active than the young enzyme and the old 6-phosphogluconic dehydrogenase enzyme is about 26% less active than the young enzyme. In this paper, some chemical properties of these enzymes are studied. Diethyl pyrocarbonate measurements indicate that the old malic enzyme has 1 histidine residue less than the young malic enzyme. Moreover, the treatment of the young malic enzyme with ascorbate for 15 min produces the loss of 36% of enzymatic activity and the loss of 1.2 histidine residues. 2,4,6-trinitrobenzenesulfonic acid measurements indicate that the old 6-phosphogluconate dehydrogenase enzyme has 11 lysine residues less than the young 6-phosphogluconate dehydrogenase enzyme. The proteolysis with trypsin produces more peptides in the young 6-phosphogluconate dehydrogenase enzyme than in the old one. However, similar numbers of peptides were produced when endoproteinase Arg-C was used in both enzymes, young and old 6-phosphogluconate dehydrogenase. Moreover, the treatment of young 6-phosphogluconate dehydrogenase enzyme with ascorbate for 15 min produces the loss of 8 lysine residues. These results suggest that during aging the modification of histidine residue could be involved in the loss of malic enzyme activity, and the modification of lysine residues could be involved in the loss of 6-phosphogluconate dehydrogenase activity. These results could also suggest that the modification of histidine and lysine residues during aging could be produced by oxidation. This could be a general process in aging, with an increase in the oxidation of many proteins. The relevance of this process in the aging effects must be related to the kind of proteins that are susceptible of oxidation and that this oxidation affects their enzymatic or biological function. We have also studied other enzymes one of which is the superoxide dismutase enzyme involved in the protection against oxidative damage. Our results are similar to those described for malic enzyme. In the latter case, the failure to measure one of the histidines in the Cu/Zn SOD is due to a chemical modification, probably caused by oxidation of the residue.

Journal Article↗

PubMed1984

Intermediary carbon metabolism of Azospirillum brasilense.

Azospirillum brasilense Sp 7 grew rapidly in AZO medium containing reduced nitrogen and succinate as an energy source, with a doubling time of 43 min. No growth was measured with glucose as the sole carbon source. In contrast, Azospirillum lipoferum Sp 59b could grow in media containing either succinate or glucose with a doubling time of 69 min and 223 min, respectively. Warburg-Barcroft respirometry showed that the rate of oxygen consumption by A. brasilense Sp 7 on glucose medium (0.034 mumol of O2 min-1 mg-1 of cell protein) was only one-quarter of that on succinate medium (0.14 mumol of O2 min-1 mg-1). Radioisotopic labeling showed that very little glucose was assimilated by A. brasilense Sp 7 as compared to succinate. High respiration rates were measured on A. lipoferum Sp 59b with either succinate (0.15 mumol of O2 min-1 mg-1) or glucose (0.13 mumol of O2 min-1 mg-1) as the sole carbon source. The pattern of CO2 evolution from differentially labeled succinate indicated that A. brasilense Sp 7 had a complete tricarboxylic acid cycle. Assimilation of most of the radioactivity from labeled succinate, pyruvate, and acetate into lipids suggested a strong anabolic metabolism and the presence of an active malic enzyme of phosphoenolpyruvate carboxykinase. The distribution of radioactivity from differentially labeled pyruvate showed that gluconeogenesis competed with pyruvate dehydrogenase. Uptake and incorporation of labeled acetate also indicated the presence of a glyoxylate cycle in A. brasilense Sp 7.

Acetates↗

PubMed1998

Expression of retinoic acid, triiodothyronine, and glucocorticoid hormone nuclear receptors is decreased in the liver of rats fed a hypercholesterolemia-inducing diet.

Several studies have shown that dietary factors modulate cell signaling pathways. The aim of this study was to determine whether a hypercholesterolemia-inducing diet rich in saturated fat and cholesterol modifies rat liver expression of the nuclear receptors of retinoic acid (RAR), triiodothyronine (TR), and glucocorticoid hormone (GR), which are transcriptional factors. The experimental diet contained coconut oil 25 g/100 g as a source of lipids, cholesterol 1 g/100 g, and cholic acid 0.5 g/100 g, and the control diet contained olive oil 5 g/100 g. After 26 days of feeding the hypercholesterolemia-inducing diet, a lower binding capacity of the nuclear receptors and a smaller amount of their mRNA were observed. Moreover, the activities of malic enzyme (ME) and tyrosine aminotransferase (TAT), whose gene promotors contain a response element to TR and GR, respectively, were significantly decreased. These changes occurred in a cellular environment characterized by a high level of cholesterol and free fatty acids (FFAs). Thus, two nonexclusive hypotheses can be proposed to explain this decreased expression of nuclear receptors, one emphasizing the effect of lipidic components on the cellular amount of receptor ligands (retinoic acid [RA] and triiodothyronine [T3]), the other emphasizing a modification of the balance between nuclear receptors that could impede the upregulation of TR and RAR.

Animals↗

PubMed2006

Malic enzyme 1 genotype is associated with backfat thickness and meat quality traits in pigs.

Malic enzyme 1 (ME1) is a part of the tricarboxylate shuttle that provides NADPH and acetyl-CoA required in fatty acid biosynthesis. The pig ME1 locus maps on the proximal end of chromosome 1, where a quantitative trait loci (QTL) affecting fat deposition has been previously described. We amplified fragments of 1457 and 1459 bp that corresponded to the complete coding region and the 3'-untranslated region (UTR), respectively, of the pig ME1 gene. The sequences of these two fragments in pigs from three breeds (Landrace, Large White and Piétrain) contained five single nucleotide polymorphisms (SNP) in the 3'-UTR: C1706T, G1762T, A1807C, C1857A and T1880A. Three haplotypes were found in two generations of a selected Landrace population: H1 (C1706 G1762 A1807 C1857 A1880), H2 (C1706 G1762 A1807 C1857 T1880) and H3 (T1706 T1762 C1807 A1857 T1880). Using Bayesian association analyses, significant associations (highest posterior density at 95%) between ME1 genotype and backfat (BF) thickness at 171 days and muscular pH were found in a Landrace population.

Animals↗

PubMed1983

Malolactic enzyme of Lactobacillus plantarum. Purification, properties, and distribution among bacteria.

The malolactic enzyme of Lactobacillus plantarum was purified from 5.5 units/mg to a specific activity of 265 units/mg of protein. The enzyme has an isoelectric point of pH 4.4. The molecular weight is Mr = 140,000 as determined by gradient gel electrophoresis. The enzyme consists of two probably identical subunits (Mr = 70,000) that were observed after treatment with sodium dodecyl sulfate. Malolactic enzyme catalyzes the NAD- and manganese-dependent reaction L-malate leads to CO2 + L-lactate. Therefore, this enzyme can be distinguished from the well known malic enzymes (L-malate: NAD+ oxidoreductase, oxalacetate-decarboxylating EC 1.1.1.38 or 1.1.1.39). Malolactic enzyme is found in most lactic acid bacteria (Lactobacteriaceae); it has not been detected in other bacteria.

Electrophoresis, Polyacrylamide Gel↗

PubMed1996

Regulation of gene expression for lipogenic enzymes in the liver and adipose tissue of hereditary hypertriglyceridemic, insulin-resistant rats: effect of dietary sucrose and marine fish oil.

Hypertriglyceridemia is closely linked to insulin resistance. Increased dietary intake of n-3 polyunsaturated fatty acids reverses both hypertriglyceridemia and insulin resistance. To evaluate molecular mechanisms responsible for the hypotriglyceridemic effects of n-3 polyunsaturated fatty acids, the expression of genes for lipogenic enzymes in liver and white and brown adipose tissue was estimated in hereditary hypertriglyceridemic rats which underwent an euglycemic hyperinsulinemic clamp. Before the clamp, animals were fed a basal or a high (63%) sucrose diet with or without fish oil for two weeks. Results were compared to data obtained from control animals subjected to the identical protocol. In hereditary hypertriglyceridemic rats, gene expression for malic enzyme was increased in liver and in brown adipose tissue but not in white adipose tissue. The high sucrose diet raised malic enzyme mRNA levels in liver of both hereditary hypertriglyceridemic and control rats, and this effect was more pronounced in brown adipose tissue. Supplementing the high sucrose diet with fish oil led to a suppression of malic enzyme gene expression in liver and brown adipose tissue of control rats. However, this inhibitory effect was not as pronounced in the hereditary hypertriglyceridemic rats. Raised levels of fatty acid synthase mRNA in liver and brown adipose tissue of control rats fed high sucrose diet were suppressed by consumption of diet high in n-3 fatty acids. On the other hand, in hereditary hypertriglyceridemic rats fed high sucrose diet, fish oil supplementation failed to suppress increased levels of fatty acid synthase mRNA in liver and in brown adipose tissue. It appears that hereditary hypertriglyceridemic rats have elevated levels of mRNA for lipogenic enzymes in liver and brown adipose tissue and dietary control leading to an alteration of hypertriglyceridemia influences gene expression of lipogenic enzymes only under special dietary circumstances.

Adipose Tissue↗

PubMed1987

Conversion of urea or ammonia into essential amino acids (L-leucine, L-valine, and L-isoleucine) using multienzyme systems and NADH-dextran immobilised in artificial cells.

Artificial cells containing leucine dehydrogenase (EC 1.4.1.9), alcohol dehydrogenase (EC 1.1.1.1; or glucose dehydrogenase, EC 1.1.1.47; or lactic dehydrogenase, EC 1.1.1.27; or malic dehydrogenase, EC 1.1.1.37), urease (EC 3.5.1.5) and dextran-NAD+ were prepared. Ammonia or urea could be converted into L-leucine, L-valine and L-isoleucine using artificial cells with four different multienzyme systems.

Amino Acids, Essential↗

PubMed1995

Quantification of compartmented metabolic fluxes in maize root tips using isotope distribution from 13C- or 14C-labeled glucose.

Metabolic pathways of the intermediate metabolism of maize root tips were identified and quantified after labeling to isotopic and metabolic steady state using glucose labeled on carbon-1, -2, or -6 with 14C or 13C. The specific radioactivity of amino acids and the 13C-specific enrichment of specific carbons of free glucose, sucrose, alanine and glutamate were measured and used to calculate metabolic fluxes. The non-triose pathways, including synthesis of polysaccharides, accumulation of free hexoses, and to a lesser extent starch synthesis, were found to consume 75% of the glucose entering the root tips. The cycle of synthesis and hydrolysis of sucrose was found to consume about 70% of the ATP produced by respiration. The comparison of the specific radioactivities of amino acids and phospholipid glycerol phosphate after labeling with [1-(14)C] or [6-(14)C]glucose revealed the operation of the pentose phosphate pathway. The transfer of label from [2-(14)C]glucose to carbon-1 of starch glucosyl units confirmed the operation of this pathway and indicated that it is located in plastids. It was found to consume 32% of the hexose phosphates entering the triose pathways. The remaining 68% were consumed by glycolysis. The determination of the specific enrichment of carbohydrate carbons -1 and -6 after labeling with [1-(13)C]glucose indicated that both the conversion of triose phosphates back to hexose phosphates and the transaldolase exchange contributed to this randomization. Of the triose phosphates produced by glycolysis and the pentose phosphate pathway, about 60% were found to be recycled to hexose phosphates, and 28% were directed to the tricarboxylic acid cycle. Of this 28%, two-thirds were found to be directed through the pyruvate kinase branch and one-third through the phosphoenolpyruvate branch. The latter essentially has an anaplerotic function since little malate was found to be converted to pyruvate (malic enzyme reaction).

Biological Transport↗

PubMed1993

Glutamate and glutamine metabolism and compartmentation in astrocytes.

Metabolism of glutamate and glutamine in cultured mouse cerebral cortical astrocytes has been investigated using either radioactively labelled (14C) amino acids or 13C-labelled amino acids combined with NMR spectroscopy of cell extracts and lyophilyzed incubation media. Using [U-13C]glutamate it has been shown that in astrocytes exogenously supplied glutamate is primarily (70%) metabolized oxidatively through the tricarboxylic acid (TCA) cycle and to a lesser extent (30%) directly to glutamine. Glutamate metabolized in the TCA cycle is to a large extent recovered as lactate showing that the astrocyte-specific enzyme, malic enzyme is functionally active. Incubation with [U-14C]glutamine led to a higher specific radioactivity in glutamate than in glutamine. It could also be shown that glutamate and glutamine were metabolized differently to aspartate and alanine. These results taken together strongly suggest that glutamate/glutamine metabolism in astrocytes is compartmentalized and a model with multiple cytoplasmic and mitochondrial compartments of these amino acids is proposed.

Animals↗

PubMedDate not supplied

Accelerated hepatic lipid synthesis in fasted septic rats.

We examined changes in the enzyme activities and metabolites related to hepatic fatty acid synthesis in fasted rats with sepsis produced by cecal ligation and puncture. Sepsis stimulated the in vivo incorporation of tritiated water into hepatic fatty acids and nonsaponifiable lipids. The activities of acetyl-CoA carboxylase, ATP-citrate lyase, and NADPH-generating enzymes (glucose-6-phosphate dehydrogenase and malic enzyme), the tissue levels of citrate and malonyl-CoA, and the dephosphorylation of carboxylase were increased in the livers of fasted septic rats compared with fasted sham-operated control rats. These results indicate that sepsis stimulated hepatic lipogenesis and sterologenesis in fasting rats. Furthermore, sepsis reduced the specific activity of hepatic mitochondrial carnitine palmitoyltransferase and raised that of glycerophosphate acyltransferase, suggesting an increased diversion of cytosolic acyl-CoA towards esterification. These intrahepatic metabolic changes strongly suggest that sepsis causes anabolic action on hepatic lipid metabolism.

Acetyl-CoA Carboxylase↗

PubMed1985

Recovery from energy deficit in golden hamsters.

Hamsters feeding at greater than 2-h intermeal intervals (IMI) lose weight but recover from weight losses without hyperphagia if they are allowed to feed at 2-h IMIs (Am. J. Physiol. 236 (Endocrinol. Metab. Gastrointest. Physiol. 5): E105-E112, 1979). To determine the relative importance of changes in energy expenditure and fat synthesis in their energy regulation, measurements were made of resting metabolic rate, respiration by brown adipose tissue (BAT), locomotion, fecal energy content, and insulin and hepatic lipogenic enzyme responses to feeding in underweight hamsters allowed to feed at 2- or 5-h IMIs. Energy deficit suppressed the resting metabolic rate and general locomotor activity and increased the activity of fatty acid synthetase (FAS). Heat production by BAT increased in underweight hamsters. Increase in IMIs blocked the postprandial insulin release, reduced plasma insulin concentration and FAS activity, and increased malic enzyme activity. Thus ad libitum feeding hamsters recover from energy deficit by reducing energy expenditure, whereas failure to add additional meals and impaired insulin and changed lipogenic responses to feeding produce energy deficits in infrequently feeding hamsters.

Adipose Tissue, Brown↗