References of "Bettendorff, Lucien"
     in
Bookmark and Share    
Full Text
Peer Reviewed
See detailThiamine Deficiency--Induced Partial Necrosis and Mitochondrial Uncoupling in Neuroblastoma Cells Are Rapidly Reversed by Addition of Thiamine
Bettendorff, Lucien ULg; Sluse, Francis ULg; Goessens, Guy ULg et al

in Journal of Neurochemistry (1995), 65(5), 2178-2184

Culture of neuroblastoma cells in a medium of low-thiamine concentration (6 nM) and in the presence of the transport inhibitor amprolium leads to the appearance of overt signs of necrosis; i.e., the ... [more ▼]

Culture of neuroblastoma cells in a medium of low-thiamine concentration (6 nM) and in the presence of the transport inhibitor amprolium leads to the appearance of overt signs of necrosis; i.e., the chromatin condenses in dark patches, the oxygen consumption decreases, mitochondria are uncoupled, and their cristae are disorganized. Glutamate formed from glutamine is no longer oxidized and accumulates, suggesting that the thiamine diphosphate-dependent alpha-ketoglutarate dehydrogenase activity is impaired. When thiamine (10 microM) is added to the cells, the O2 consumption increases, respiratory control is restored, and normal cell and mitochondrial morphology is recovered within 1 h. Succinate, which is oxidized via the thiamine diphosphate-independent succinate dehydrogenase, is also able to restore a normal O2 consumption (with respiratory control) in digitonin-permeabilized thiamine-deficient cells. Our results therefore suggest that the slowing of the citric acid cycle is the main cause of the biochemical lesion induced by thiamine deficiency as observed in Wernicke's encephalopathy. [less ▲]

Detailed reference viewed: 42 (23 ULg)
Full Text
Peer Reviewed
See detailThiamine Deficiency in Cultured Neuroblastoma Cells: Effect on Mitochondrial Function and Peripheral Benzodiazepine Receptors
Bettendorff, Lucien ULg; Goessens, Guy ULg; Sluse, Francis ULg et al

in Journal of Neurochemistry (1995), 64(5), 2013-2021

When neuroblastoma cells were transferred to a medium of low (6 nM) thiamine concentration, a 16-fold decrease in total intracellular thiamine content occurred within 8 days. Respiration and ATP levels ... [more ▼]

When neuroblastoma cells were transferred to a medium of low (6 nM) thiamine concentration, a 16-fold decrease in total intracellular thiamine content occurred within 8 days. Respiration and ATP levels were only slightly affected, but addition of a thiamine transport inhibitor (amprolium) decreased ATP content and increased lactate production. Oxygen consumption became low and insensitive to oligomycin and uncouplers. At least 25% of mitochondria were swollen and electron translucent. Cell mortality increased to 75% within 5 days. [3H]PK 11195, a specific ligand of peripheral benzodiazepine receptors (located in the outer mitochondrial membrane) binds to the cells with high affinity (KD = 1.4 +/- 0.2 nM). Thiamine deficiency leads to an increase in both Bmax and KD. Changes in binding parameters for peripheral benzodiazepine receptors may be related to structural or permeability changes in mitochondrial outer membranes. In addition to the high-affinity (nanomolar range) binding site for peripheral benzodiazepine ligands, there is a low-affinity (micromolar range) saturable binding for PK 11195. At micromolar concentrations, peripheral benzodiazepines inhibit thiamine uptake by the cells. Altogether, our results suggest that impairment of oxidative metabolism, followed by mitochondrial swelling and disorganization of cristae, is the main cause of cell mortality in severely thiamine-deficient neuroblastoma cells. [less ▲]

Detailed reference viewed: 24 (9 ULg)
Full Text
Peer Reviewed
See detailThiamine Homeostasis in Neuroblastoma Cells
Bettendorff, Lucien ULg

in Neurochemistry International (1995), 26(3), 295-302

We recently showed that thiamine uptake by neuroblastoma cells is mediated by two saturable transport system: the first with high affinity for thiamine (Km = 35 nM) is blocked by veratridine; the other ... [more ▼]

We recently showed that thiamine uptake by neuroblastoma cells is mediated by two saturable transport system: the first with high affinity for thiamine (Km = 35 nM) is blocked by veratridine; the other, with low affinity is blocked by Ca2+. The driving force for thiamine uptake is its phosphorylation to thiamine diphosphate (TDP) by thiamine pyrophosphokinase and subsequent binding of this cofactor to apoenzymes. Our results suggest that cells of neuronal origin possess mechanisms regulating the intracellular concentration of thiamine. At low external thiamine, the vitamin is taken up by a high-affinity transporter and pyrophosphorylated in thiamine diphosphate (TDP): this is the TDP pool of slow turnover. An intraover extracellular concentration gradient of free thiamine is observed at low external concentration of the vitamin. At higher external thiamine concentration, TDP accumulation is limited by the binding capacity to the apoenzymes and unbound TDP (i.e. a small pool of fast turnover) is quickly hydrolyzed. Thiamine is slowly released by the cells by at least two different mechanisms. The first, accounting for a maximum of 50% of total thiamine release, is stimulated by external thiamine and is blocked by veratridine, suggesting that it is a self-exchange mechanism catalyzed by the high affinity thiamine transporter. The remaining thiamine efflux is neither sensitive to veratridine nor to Ca2+ and its mechanism is unknown. About 25% of intracellular thiamine is not released, even after treatment of the cells with digitonin, thus maintaining an apparent gradient. This suggests a binding or sequestration in intracellular compartments.(ABSTRACT TRUNCATED AT 250 WORDS) [less ▲]

Detailed reference viewed: 18 (1 ULg)
Peer Reviewed
See detailAn Atypical Anion Transporter Functioning at Acid pH in Neuroblastoma Cells
Bettendorff, Lucien ULg; Margineanu, Ilca; Wins, Pierre et al

in Biochemical and Biophysical Research Communications (1995), 207(1), 375-381

At pH 7.4, 36Cl- uptake by neuroblastoma cells was Na(+)-independent, saturable and blocked by submicromolar concentrations of DIDS. This suggests that at this pH, Cl- transport is mediated by an ... [more ▼]

At pH 7.4, 36Cl- uptake by neuroblastoma cells was Na(+)-independent, saturable and blocked by submicromolar concentrations of DIDS. This suggests that at this pH, Cl- transport is mediated by an exchanger analogous to erythroid band 3. At pH 6. [less ▲]

Detailed reference viewed: 13 (8 ULg)
See detailTransport and metabolism of thiamine
Bettendorff, Lucien ULg

Scientific conference (1994)

Detailed reference viewed: 2 (0 ULg)
Full Text
Peer Reviewed
See detailThiamine in Excitable Tissues: Reflections on a Non-Cofactor Role
Bettendorff, Lucien ULg

in Metabolic Brain Disease (1994), 9(3), 183-209

Detailed reference viewed: 11 (1 ULg)
Full Text
Peer Reviewed
See detailThe Compartmentation of Phosphorylated Thiamine Derivatives in Cultured Neuroblastoma Cells
Bettendorff, Lucien ULg

in Biochimica et Biophysica Acta (1994), 1222(1), 7-14

Thiamine transport in cultured neuroblastoma cells is mediated by a high-affinity carrier (KM = 40 nM). In contrast, the uptake of the more hydrophobic sulbutiamine (isobutyrylthiamine disulfide) is ... [more ▼]

Thiamine transport in cultured neuroblastoma cells is mediated by a high-affinity carrier (KM = 40 nM). In contrast, the uptake of the more hydrophobic sulbutiamine (isobutyrylthiamine disulfide) is unsaturable and its initial transport rate is 20-times faster than for thiamine. In the cytoplasm, sulbutiamine is rapidly hydrolyzed and reduced to free thiamine, the overall process resulting in a rapid and concentrative thiamine accumulation. Incorporation of radioactivity from [14C]thiamine or [14C]sulbutiamine into intracellular thiamine diphosphate is slow in both cases. Despite the fact that the diphosphate is probably the direct precursor for both thiamine monophosphate and triphosphate, the specific radioactivity increased much faster for the latter two compounds than for thiamine diphosphate. This suggests the existence of two pools of thiamine diphosphate, the larger one having a very slow turnover (about 17 h); a much smaller, rapidly turning over pool would be the precursor of thiamine mono- and triphosphate. The turnover time for thiamine triphosphate could be estimated to be 1-2 h. When preloading the cells with [14C]sulbutiamine was followed by a chase with the same concentration of the unlabeled compound, the specific radioactivities of thiamine and thiamine monophosphate decreased exponentially as expected, but labeling of the diphosphate continued to increase slowly. Specific radioactivity of thiamine triphosphate increased first, but after 30 min it began to slowly decrease. These results show for the first time the existence of distinct thiamine diphosphate pools in the same homogeneous cell population. They also suggest a complex compartmentation of thiamine metabolism. [less ▲]

Detailed reference viewed: 12 (1 ULg)
Full Text
Peer Reviewed
See detailMechanism of Thiamine Transport in Neuroblastoma Cells. Inhibition of a High Affinity Carrier by Sodium Channel Activators and Dependence of Thiamine Uptake on Membrane Potential and Intracellular Atp
Bettendorff, Lucien ULg; Wins, Pierre

in Journal of Biological Chemistry (1994), 269(20), 14379-14385

Nerve cells are particularly sensitive to thiamine deficiency. We studied thiamine transport in mouse neuroblastoma (Neuro 2a) cells. At low external concentration, [14C]thiamine was taken up through a ... [more ▼]

Nerve cells are particularly sensitive to thiamine deficiency. We studied thiamine transport in mouse neuroblastoma (Neuro 2a) cells. At low external concentration, [14C]thiamine was taken up through a saturable high affinity mechanism (Km = 35 nM). This was blocked by low concentrations of the Na+ channel activators veratridine (IC50 = 7 +/- 4 microM) and batrachotoxin (IC50 = 0.9 microM). These effects were not antagonized by tetrodotoxin and were also observed in cell lines devoid of Na+ channels, suggesting that these channels are not involved in the mechanism of inhibition. At high extracellular concentrations, thiamine uptake proceeds essentially via a low affinity carrier (Km = 0.8 mM), insensitive to veratridine but blocked by divalent cations. In both cases, the uptake was independent on external sodium, partially inhibited (10-35%) by depolarization and sensitive to metabolic inhibitors. A linear relationship between the rate of thiamine transport and intracellular ATP concentration was found. When cells grown in a medium of low thiamine concentration (6 nM) were exposed to 100 nM extracellular thiamine, a 3-fold increase in intracellular thiamine diphosphate was observed after 2 h while the concomitant increase in intracellular free thiamine was barely significant. These data suggest a secondary active transport of thiamine, the main driving force being thiamine phosphorylation rather than the sodium gradient. [less ▲]

Detailed reference viewed: 16 (1 ULg)
Peer Reviewed
See detailChloride Permeability of Rat Brain Membrane Vesicles Correlates with Thiamine Triphosphate Content
Bettendorff, Lucien ULg; Hennuy, Benoît ULg; De Clerck, Anne et al

in Brain Research (1994), 652(1), 157-160

Incubation of rat brain homogenates with thiamine or thiamine diphosphate (TDP) leads to a synthesis of thiamine triphosphate (TTP). In membrane vesicles subsequently prepared from the homogenates ... [more ▼]

Incubation of rat brain homogenates with thiamine or thiamine diphosphate (TDP) leads to a synthesis of thiamine triphosphate (TTP). In membrane vesicles subsequently prepared from the homogenates, increased TTP content correlates with increased 36Cl- uptake. A hyperbolic relationship was obtained with a K0.5 of 0.27 nmol TTP/mg protein. In crude mitochondrial fractions from the brains of animals previously treated with thiamine or sulbutiamine, a positive correlation between 36Cl- uptake and TTP content was found. These results, together with other results previously obtained with the patch-clamp technique, suggest that TTP is an activator of chloride channels having a large unit conductance. [less ▲]

Detailed reference viewed: 15 (3 ULg)
Full Text
Peer Reviewed
See detailSubcellular Localization and Compartmentation of Thiamine Derivatives in Rat Brain
Bettendorff, Lucien ULg; Wins, Pierre; Lesourd, Monique

in Biochimica et Biophysica Acta (1994), 1222(1), 1-6

The subcellular distribution of thiamine derivatives in rat brain was studied. Thiamine diphosphate content was highest in the mitochondrial and synaptosomal fractions, and lowest in microsomal, myelin ... [more ▼]

The subcellular distribution of thiamine derivatives in rat brain was studied. Thiamine diphosphate content was highest in the mitochondrial and synaptosomal fractions, and lowest in microsomal, myelin and cytosolic fractions. Only 3-5% of total thiamine diphosphate was bound to transketolase, a cytosolic enzyme. Thiamine triphosphate was barely detectable in the microsomal and cytosolic fraction, but synaptosomes were slightly enriched in this compound compared to the crude homogenate. Both myelin and mitochondrial fractions contained significant amounts of thiamine triphosphate. In order to estimate the relative turnover rates of these compounds, the animals received an intraperitoneal injection of either [14C]thiamine or [14C]sulbutiamine (isobutyrylthiamine disulfide) 1 h before decapitation. The specific radioactivities of thiamine compounds found in the brain decreased in the order: thiamine > thiamine triphosphate > thiamine monophosphate > thiamine diphosphate. Incorporation of radioactivity into thiamine triphosphate was more marked with [14C]sulbutiamine than with [14C]thiamine. The highest specific radioactivity of thiamine diphosphate was found in the cytosolic fraction of the brain, though this pool represents less than 10% of total thiamine diphosphate. Cytosolic thiamine diphosphate had a twice higher specific radioactivity when [14C]sulbutiamine was used as precursor compared with thiamine though no significant differences were found in the other cellular compartments. Our results suggest the existence of two thiamine diphosphate pools: the bound cofactor pool is essentially mitochondrial and has a low turnover; a much smaller cytosolic pool (6-7% of total TDP) of high turnover is the likely precursor of thiamine triphosphate. [less ▲]

Detailed reference viewed: 15 (2 ULg)
Full Text
Peer Reviewed
See detailMetabolism of Thiamine Triphosphate in Rat Brain: Correlation with Chloride Permeability
Bettendorff, Lucien ULg; Peeters, Maryline; Wins, Pierre et al

in Journal of Neurochemistry (1993), 60(2), 423-434

Our results show that a net synthesis of thiamine triphosphate (TTP) can be demonstrated in vitro using rat brain extracts. The total homogenate was preincubated with thiamine or its diphosphate ... [more ▼]

Our results show that a net synthesis of thiamine triphosphate (TTP) can be demonstrated in vitro using rat brain extracts. The total homogenate was preincubated with thiamine or its diphosphate derivative (TDP), centrifuged, and washed twice. With TDP (1 mM) as substrate, a 10-fold increase in TTP content was observed in this fraction (nuclear fraction, membrane vesicles). A smaller, but significant, increase was observed in the P2 fraction (mitochondrial/synaptosomal fraction). In view of the low TTP content of our fractions, it was carefully assessed that authentic TTP was being formed. Incorporation of radioactivity from [beta-32P]TDP and [gamma-32P]ATP in TTP suggests that these two compounds are its precursors. Furthermore, TTP synthesis was inhibited by ADP and relatively low concentrations of Zn2+. These results suggest that TTP synthesis is catalyzed by an ATP:TDP transphosphorylase rather than by the cytoplasmic adenylate kinase that may be present in the vesicles. After osmotic lysis of the vesicles at alkaline pH, TTP was recovered in protein-bound form. Concomitantly, a soluble thiamine triphosphatase, with alkaline pH optimum, was also released from the vesicles. No net synthesis could be obtained in the cytosolic fraction or in detergent-solubilized systems. Like TTP synthesis, chloride permeability of the vesicles was increased when the homogenate had been incubated with thiamine and particularly with TDP. Our results suggest a regulatory role of TTP on chloride permeability, but the target remains to be characterized. [less ▲]

Detailed reference viewed: 21 (1 ULg)
Peer Reviewed
See detailThiamine Triphosphate Activates an Anion Channel of Large Unit Conductance in Neuroblastoma Cells
Bettendorff, Lucien ULg; Kolb, Hans-Albert; Schoffeniels, E.

in Journal of Membrane Biology (1993), 136(3), 281-8

In neuroblastoma cells, the intracellular thiamine triphosphate (TTP) concentration was found to be about 0.5 microM, which is several times above the amount of cultured neurons or glial cells. In inside ... [more ▼]

In neuroblastoma cells, the intracellular thiamine triphosphate (TTP) concentration was found to be about 0.5 microM, which is several times above the amount of cultured neurons or glial cells. In inside-out patches, addition of TTP (1 or 10 microM) to the bath activated an anion channel of large unit conductance (350-400 pS) in symmetrical 150 mM NaCl solution. The activation occurred after a delay of about 4 min and was not reversed when TTP was washed out. A possible explanation is that the channel has been irreversibly phosphorylated by TTP. The channel open probability (Po) shows a bell-shaped behavior as a function of pipette potential (Vp). Po is maximal for -25 mV < Vp < 10 mV and steeply decreases outside this potential range. From reversal potentials, permeability ratios of PCl/PNa = 20 and PCl/Pgluconate = 3 were estimated. ATP (5 mM) at the cytoplasmic side of the channel decreased the mean single channel conductance by about 50%, but thiamine derivatives did not affect unit conductance; 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid (0.1 mM) increased the flickering of the channel between the open and closed state, finally leading to its closure. Addition of oxythiamine (1 mM), a thiamine antimetabolite, to the pipette filling solution potentiates the time-dependent inactivation of the channel at Vp = -20 mV but had the opposite effect at +30 mV. This finding corresponds to a shift of Po towards more negative resting membrane potentials. These observations agree with our previous results showing a modulation of chloride permeability by thiamine derivatives in membrane vesicles from rat brain. [less ▲]

Detailed reference viewed: 11 (3 ULg)
Peer Reviewed
See detailThiamin and Derivatives as Modulators of Rat Brain Chloride Channels
Bettendorff, Lucien ULg; Hennuy, Benoît ULg; Wins, Pierre et al

in Neuroscience (1993), 52(4), 1009-1017

Several membrane fractions were prepared from rat brain by differential and sucrose density gradient centrifugation. Most fractions took up 36Cl- rapidly at a rate linear with time during the first 30-60 ... [more ▼]

Several membrane fractions were prepared from rat brain by differential and sucrose density gradient centrifugation. Most fractions took up 36Cl- rapidly at a rate linear with time during the first 30-60 s, then the rate progressively slowed down. The lowest rate of uptake was found in the mitochondrial fraction. Oxythiamin partially inhibited 36Cl- uptake in all fractions. In P2 (crude synaptosomal fraction), oxythiamin decreased the initial rate of uptake by 32%, the apparent Ki being 1.5 mM. Thiamin and amprolium were less effective as inhibitors. 4,4'-Diisothiocyanostilbene-2,2'-disulfonic acid (0.1-1 mM) inhibited 36Cl- uptake by 40-50%. In the presence of this compound at a concentration > or = 5 x 10(-4) M, oxythiamin became ineffective. 36Cl- uptake was increased by GABA (0.1 mM) and this effect was antagonized by picrotoxin as expected, but not by oxythiamin. The rate of 36Cl- uptake did not appreciably depend on the external chloride concentration and was unaffected by bumetanide or by replacement of external Na+ by choline. Taken together, these data suggest that the oxythiamin-sensitive 36Cl- influx is essentially diffusional and is not related to the GABA receptor or the Na:K:2Cl co-transport. Partial replacement of external Na+ by K+ or treatment with 0.1 mM veratridine (which should both result in membrane depolarization) increased 36Cl- uptake by 50 and 30% respectively; the inhibitory effect of oxythiamin was enhanced to the same proportion.(ABSTRACT TRUNCATED AT 250 WORDS) [less ▲]

Detailed reference viewed: 10 (4 ULg)
Peer Reviewed
See detailApplication of High-Performance Liquid Chromatography to the Study of Thiamine Metabolism and in Particular Thiamine Triphosphatase
Bettendorff, Lucien ULg

in Journal of Chromatography. A (1991), 566(2), 397-408

Thiamine triphosphate can be found in most tissues at very low levels, but its role is unknown. Organs and muscles that generate electrical impulses are particularly rich in this compound. This paper ... [more ▼]

Thiamine triphosphate can be found in most tissues at very low levels, but its role is unknown. Organs and muscles that generate electrical impulses are particularly rich in this compound. This paper describes a thiamine triphosphatase from the electrical organ of Electrophorus electricus. The activity of this enzyme, as measured by a high-performance liquid chromatographic method, is closely anion-regulated. Furthermore, thiamine triphosphate increases chloride uptake in membrane vesicles prepared from rat brain. Our results suggest that this compound could play an important role in the regulation of chloride permeability. [less ▲]

Detailed reference viewed: 28 (3 ULg)
Peer Reviewed
See detailSolubilization of Thiamine Triphosphatase from the Electric Organ of Electrophorus Electricus
Bettendorff, Lucien ULg; Longree, Isabelle; Wins, Pierre et al

in Biochimica et Biophysica Acta - General Subjects (1991), 1073(1), 69-76

The membrane-associated, anion-regulated thiamine triphosphatase from Electrophorus electricus electric organ can be solubilized by various neutral detergents. Polyoxyethylene ethers are the most ... [more ▼]

The membrane-associated, anion-regulated thiamine triphosphatase from Electrophorus electricus electric organ can be solubilized by various neutral detergents. Polyoxyethylene ethers are the most effective. Anionic detergents readily inactivate the enzyme. A 6.4-fold increase in specific activity is obtained by successive treatment of crude membranes with octanoyl-N-methylglucamide, which solubilized other proteins, and Lubrol-PX with releases 60% of the thiamine triphosphatase (TTPase) activity. Solubilization by Lubrol-PX rapidly modifies kinetic parameters. The Km, Vmax and pH optimum are decreased. However, the solubilized TTPase may be kept at 0 degrees C for many hours without further change in specific activity. At 35 degrees C, the half-life is still 83 min at pH 5.0, but denaturation becomes rapid at pH greater than or equal to 7. Solubilization modifies anion effects on TTPase activity. The activating effect of nitrate is nearly lost, while inhibition by sulfate is no longer time-dependent. [less ▲]

Detailed reference viewed: 11 (3 ULg)
Full Text
Peer Reviewed
See detailDetermination of Thiamin and Its Phosphate Esters in Cultured Neurons and Astrocytes Using an Ion-Pair Reversed-Phase High-Performance Liquid Chromatographic Method
Bettendorff, Lucien ULg; Peeters, Maryline; Jouan, Caroline ULg et al

in Analytical Biochemistry (1991), 198(1), 52-59

A sensitive method, based on fluorescence detection, for the determination of thiamin derivatives after precolumn derivatization is described. The separation is achieved on a PRP-1 column using ion-pair ... [more ▼]

A sensitive method, based on fluorescence detection, for the determination of thiamin derivatives after precolumn derivatization is described. The separation is achieved on a PRP-1 column using ion-pair reversed-phase HPLC. This method is especially well adapted to the detection of thiamin triphosphate in complex mixtures such as tissue extracts. The detection limit for TTP is 50 fmol. The contents of thiamin derivatives were determined in primary cultures of rat cerebellar granule neurons and cerebral astrocytes. The amount of TTP is about five times higher in neurons than in astrocytes. Thus in rat brain TTP seems to be essentially associated with neurons and the intracellular concentration is estimated to be about 0.2 microM. Our results suggest the existence, in nerve cells, of specific regulatory mechanisms not related to the blood-brain barrier and responsible for the maintenance of thiamin homeostasis in brain. [less ▲]

Detailed reference viewed: 30 (9 ULg)
Peer Reviewed
See detailRegulation of Ion Uptake in Membrane Vesicles from Rat Brain by Thiamine Compounds
Bettendorff, Lucien ULg; Wins, Pierre; Schoffeniels, Ernest

in Biochemical and Biophysical Research Communications (1990), 171(3), 1137-1144

We examined the effects of thiamine derivatives on ion uptake in rat brain membrane vesicles. Thiamine triphosphate (1 mM) and pyrithiamine (0.1 mM) increase chloride uptake. Preincubation of crude ... [more ▼]

We examined the effects of thiamine derivatives on ion uptake in rat brain membrane vesicles. Thiamine triphosphate (1 mM) and pyrithiamine (0.1 mM) increase chloride uptake. Preincubation of crude homogenate with thiamine or pyrithiamine increases chloride uptake while oxythiamine has the reverse effect. Thiamine and oxythiamine also affect 22Na+ and 86Rb+ uptake in the same way as for 36Cl- but to a lesser extent. Thiamine-dependent 36Cl- uptake is activated by sodium bicarbonate (10 mM) and partially inhibited by bumetanide (0.1 mM) and 2,4-dinitrophenol (0.1 mM). Preincubation with thiamine increases the thiamine triphosphate content of the vesicles. The hypothesis that TTP is the activator of a particular chloride uptake mechanism is discussed. [less ▲]

Detailed reference viewed: 7 (5 ULg)
Peer Reviewed
See detailInjection of Sulbutiamine Induces an Increase in Thiamine Triphosphate in Rat Tissues
Bettendorff, Lucien ULg; Weekers, Laurent ULg; Wins, Pierre et al

in Biochemical Pharmacology (1990), 40(11), 2557-2560

Detailed reference viewed: 57 (6 ULg)