Biomedical subjects

G van Hall

Publications and source records attributed to G van Hall.

26 records · Page 2Linked to original sources

PubMed1998

Effect of carbohydrate supplementation on plasma glutamine during prolonged exercise and recovery.

Muscle glycogen and glucose have been suggested to be carbon-chain precursors for glutamine synthesis in skeletal muscle. Therefore, the aim of the present study is to investigate whether carbohydrate supplementation affects plasma glutamine and other amino acids during exercise and 7 h of recovery. Eight well-trained subjects cycled at an alternating workload of 50 and 80% Wmax until exhaustion (59 to 140 min). During the exercise bout the subjects received either water (control) or a carbohydrate (CHO) drink (83 g CHO x l(-1), 2 ml x kg(-1) per kg body weight every 15 min). Plasma glutamine concentration appeared not to be affected by exercise, as a significant increase was only observed at some points in time during the control test. During recovery, however, plasma glutamine concentration decreased from 682+/-24 and 685+/-19 micromol x l(-1) at exhaustion to 552+/-19 and 534+/-12 micromol x l(-1) after 2 h of recovery for the control and CHO test, respectively. Plasma glutamine concentration returned to pre-exercise values after 7 h of recovery. Alanine concentration increased during exercise in both tests. During the recovery period the concentration of alanine (48%), and total amino acids (23%) decreased below the pre-exercise level. The plasma alanine and the total amino acid concentration was still suppressed after 7 h of recovery. In conclusion, carbohydrate supplementation had neither an effect during exercise nor during recovery on the concentration of plasma glutamine or other amino acids. Exercise, however, causes a substantial decrease in the plasma amino acid concentration during recovery.

Adult↗

PubMed1996

Mechanisms of activation of muscle branched-chain alpha-keto acid dehydrogenase during exercise in man.

1. Exercise leads to activation (dephosphorylation) of the branched-chain alpha-keto acid dehydrogenase (BCKADH). Here we investigate the effect of low pre-exercise muscle glycogen content and of branched-chain amino acid (BCAA) ingestion on the activity of BCKADH at rest and after 90 min of one-leg knee-extensor exercise at 65% maximal one-leg power output in five subjects. 2. Pre-exercise BCAA ingestion (308 mg BCAAs (kg body wt)-1) caused an increased muscle BCAA uptake, a higher intramuscular BCAA concentration and activation of BCKADH both at rest (9 +/- 1 versus 25 +/- 5% for the control and BCAA test, respectively) and after exercise (27 +/- 4 versus 54 +/- 7%). 3. At rest the percentage active BCKADH was not different, 6 +/- 2% versus 5 +/- 1%, in the normal and low glycogen content leg (392 +/- 21 and 147 +/- 34 mumol glycosyl units (g dry muscle)-1, respectively). The post-exercise BCKADH activity was higher in the low (46 +/- 2%) than in the normal glycogen content leg (26 +/- 2%). 4. It is concluded that: (1) the mechanism of activation by BCAA ingestion probably involves an increase of the muscle BCAA concentration; (2) BCKADH activation caused by exercise and BCAA ingestion are additive; (3) low pre-exercise muscle glycogen content augments the exercise-induced BCKADH activation without an increase in muscle BCAA concentration; and (4) the mechanism of BCKADH activation via BCAA ingestion and low muscle glycogen content are different.

3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)↗

PubMed1995

Deamination of amino acids as a source for ammonia production in human skeletal muscle during prolonged exercise.

1. The influence of pre-exercise muscle glycogen content on ammonia production, adenine nucleotide breakdown and amino acid metabolism was investigated during prolonged exercise in six subjects having one leg with a normal and one leg with a low muscle glycogen content. One-leg knee-extensor exercise was performed for 90 min, at a workload of 60-65% of the maximal power output, first with one leg and then with the other. 2. During exercise ammonia was released in gradually increasing amounts and plateaued after 1 h exercise at a rate of approximately 80 mumol min-1. The total ammonia production was 9.1 +/- 0.4 and 9.5 +/- 1.4 mmol (kg dry muscle)-1 in the normal and low glycogen content leg, respectively. 3. Levels of muscle phosphocreatine (PC), total adenine nucleotides and inosine monophosphate (IMP) were similar at rest and after 90 min of exercise. 4. Only minor differences were observed between rest and exercise and between legs for the muscle concentrations of glutamine, alanine and the branched-chain amino acids. Muscle glutamate concentration decreased by 60-70% within the first 10 min of exercise. Glutamate consumption over 90 min quantitatively equalled ammonia production. Most of the glutamate was consumed within the first 10 min of exercise, while ammonia production gradually increased during exercise. Therefore deamination of glutamate cannot be the main source of ammonia production during the later stage of exercise. 5. It is concluded that during prolonged one-leg exercise at moderate intensity: (a) ammonia production is not affected by pre-exercise muscle glycogen content, (b) ammonia production exceeds by far the breakdown of adenine nucleotides to IMP and therefore has to be derived from alternative sources, and (c) deamination of amino acids is a likely source of ammonia production during prolonged exercise.

Adult↗

PubMed1995

Ingestion of branched-chain amino acids and tryptophan during sustained exercise in man: failure to affect performance.

1. An increased uptake of tryptophan in the brain may increase serotoninergic activity and recently has been suggested to be a cause of fatigue during prolonged exercise. The present study, therefore, investigates whether ingestion of tryptophan or the competing branched-chain amino acids (BCAAs) affect performance. Ten endurance-trained male athletes were studied during cycle exercise at 70-75% maximal power output, while ingesting, ad random and double-blind, drinks that contained 6% sucrose (control) or 6% sucrose supplemented with (1) tryptophan (3 g l-1), (2) a low dose of BCAA (6 g l-1) or (3) a high dose of BCAA (18 g l-1). 2. These treatments greatly increased the plasma concentration of the respective amino acids. Using the kinetic parameters of transport of human brain capillaries, BCAA supplements were estimated to reduce brain tryptophan uptake at exhaustion by 8-12%, while tryptophan ingestion caused a 7- to 20-fold increase. Exercise time to exhaustion was not different between treatments (122 +/- 3 min). 3. The data suggest that manipulation of tryptophan supply to the brain either has no additional effect upon serotoninergic activity during prolonged exhaustive exercise or that manipulation of serotoninergic activity functionally does not contribute to mechanisms of fatigue.

Adult↗

PubMed1995

Chronic oral lactate supplementation does not affect lactate disappearance from blood after exercise.

This study tested the hypothesis that a 3-week oral lactate supplementation affects postexercise blood lactate disappearance in untrained male subjects. Fifteen men were randomly assigned to either a lactate supplementation (n = 8) or a placebo (n = 7) treatment. During the treatment period they drank an oral lactate or a maltodextrin (placebo) supplement twice a day. The lactate drink contained 10 g of lactate as calcium, sodium, and potassium salts. Blood lactate concentrations were studied before, during, and immediately after three exercise tests, both pre- and posttreatment. Peak lactate values for placebo (PL) or lactate (L) treatment groups during different tests were as follows: Test 1 PL, 13.49 +/- 3.71; L, 13.70 +/- 1.90; Test 2 PL, 12.64 +/- 2.32; L, 12.00 +/- 2.23; Test 3 PL, 12.29 +/- 2.92; L, 11.35 +/- 1.38 and were reached 3 min postexercise. The decrease in blood lactate during the long (30- to 45-min) recovery periods amounted to / 10 mmol/L. Blood lactate changes were highly reproducible. However, a 3-week oral lactate supplementation did not result in differences in lactate disappearance. This study does not support the hypothesis that regular oral lactate intake at rest enhances the removal of lactate during and following exercise, that is, not with the given lactate load and supplementation period.

Administration, Oral↗

PubMed1995

Adaptation of Xanthobacter autotrophicus GJ10 to bromoacetate due to activation and mobilization of the haloacetate dehalogenase gene by insertion element IS1247.

Monobromoacetate (MBA) is toxic for the 1,2-dichloroethane-degrading bacterium Xanthobacter autotrophicus GJ10 at concentrations higher than 5 mM. Mutants which are able to grow on higher concentrations of MBA were isolated and found to overexpress haloacid dehalogenase, which is encoded by the dhlB gene. In mutant GJ10M50, a DNA fragment (designated IS1247) had copied itself from a position on the chromosome that was not linked to the dhlB region to a site immediately upstream of dhlB, resulting in a 1,672-bp insertion. IS1247 was found to encode an open reading frame corresponding to 464 amino acids which showed similarity to putative transposases from two other insertion elements. In most of the other MBA-resistant mutants of GJ10, IS1247 was also present in one more copy than in the wild type, which had two copies located within 20 kb. After insertion to a site proximal to dhlB, IS1247 was able to transpose itself together with the dhlB gene to a plasmid, without the requirement of a second insertion element being present downstream of dhlB. The results show that IS1247 causes bromoacetate resistance by overexpression and mobilization of the haloacid dehalogenase gene, which mimics steps during the evolution of a catabolic transposon and plasmid during adaptation to a toxic growth substrate.

Acetates↗

PubMed1991

Characterization of the haloacid dehalogenase from Xanthobacter autotrophicus GJ10 and sequencing of the dhlB gene.

The haloacid dehalogenase of the 1,2-dichloroethane-utilizing bacterium Xanthobacter autotrophicus GJ10 was purified from a mutant with an eightfold increase in expression of the enzyme. The mutant was obtained by selecting for enhanced resistance to monobromoacetate. The enzyme was purified through (NH4)2SO4 fractionation, DEAE-cellulose chromatography, and hydroxylapatite chromatography. The molecular mass of the protein was 28 kDa as determined with sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 36 kDa as determined with gel filtration on Superose 12 fast protein liquid chromatography. The enzyme was active with 2-halogenated carboxylic acids and converted only the L-isomer of 2-chloropropionic acid with inversion of configuration to produce D-lactate. The activity of the enzyme was not readily influenced by thiol reagents. The gene encoding the haloacid dehalogenase (dhlB) was cloned and could be allocated to a 6.5-kb EcoRI-BglII fragment. Part of this fragment was sequenced, and the dhlB open reading frame was identified by comparison with the N-terminal amino acid sequence of the protein. The gene was found to encode a protein of 27,433 Da that showed considerable homology (60.5 and 61.0% similarity) with the two other haloacid dehalogenases sequenced to date but not with the haloalkane dehalogenase from X. autotrophicus GJ10.

Amino Acid Sequence↗

PubMed1989

Identification of Na+/K+-ATPase inhibitors in bovine plasma as fatty acids and hydrocarbons.

A preparative purification of endogenous inhibitors of the Na+/K+-ATPase has been carried out from bovine blood. Dried plasma was deproteinized, hexane-extracted and desalted, followed by further purification through a series of reverse-phase HPLC fractionations. Fractions active in inhibiting Na+/K+-ATPase activity and displacing ouabain were collected and purified further. By comparison with ouabain, the final extract was found to have a steeper concentration-effect curve in the inhibition of Na+/K+-ATPase. In displacement of [3H]ouabain, the extract had again a steeper concentration-effect curve than does ouabain, and in addition it enhanced ouabain binding at high dilutions. These properties are indicative of nonspecific interactions with the Na+/K+-ATPase. The active fraction was identified by TLC, HPLC, NMR, GLC and GC-MS, to be a mixture of three unesterified fatty acids, mainly oleic acid (72% of the total) and three saturated hydrocarbons. The assignment of structures was corroborated by comparison with authentic samples.

Animals↗