[Are zinc and selenium markers of worsening in HIV infected subjects?].
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Adult↗
Biomedical subjects
T May
Publications and source records attributed to T May.
[Hyponatremia in AIDS. Etiology and diagnosis].
Hyponatremia is a common electrolyte abnormality in AIDS patients. In this study, hyponatremia was defined as natremia less than 130 mmol/l at two different samplings. Medical records of 160 hospitalized AIDS patients were exhaustively reviewed in search for hyponatremia and, if present, of its etiology. 45 cases of hyponatremia were identified in 43 AIDS patients. Two causes were predominant: hypovolemic hyponatremia, due to water and salt losses (11 cases) and the syndrome of inappropriate antidiuretic hormone secretion (10 cases). These results are consistent with those of the literature and were used to develop a simple diagnosis schedule based on the analysis of limited clinical and biological data: hydration status, serum and urinary osmolality, natriuria and creatininemia.
Acquired Immunodeficiency Syndrome↗
A cis-acting element responsible for early gene induction by extracellular cAMP in Dictyostelium discoideum.
We have analysed the promoter of the Dictyostelium discoideum alpha-L-fucosidase (ALF) gene, and have identified a 58 bp fragment responsible for transcriptional activation mediated by extracellular cAMP. Replacement of regulatory sequences in the cAMP-independent actin 15 promoter by this fragment confers cAMP regulation to the hybrid promoter. A cAMP analog with high affinity to the cell surface cAMP receptor can induce transcription from the endogenous as well as from the hybrid promoter. Gel-shift experiments show that the 58 bp fragment is a target for nuclear DNA-binding proteins, and that a specific complex is formed in response to cAMP stimulation. The major cAMP-dependent DNA.protein complex is formed with a 22 bp subfragment which we have termed DCRE (Dictyostelium cAMP responsive element).
Base Composition↗
beta-Carbolines and Tetrahydroisoquinolines: Detection and Function in Mammals.
beta-Carbolines occur in man and rat. The concentration in various tissues is about 100 to 1000 times lower than that of classical neurotransmitters. Administration of beta-carbolines in animals induces overlapping but not identical activity profiles. The molecular modes of action differ. For example, harman (1-methyl-beta-carboline) acts as an endogenous inhibitor of monoamine oxidase [E.C. 1.4.3.4.], subtype A, whereas norharman (beta-carboline) probably acts by stimulation of a specific beta-carboline receptor which is different from the benzodiazepine-GABA receptor complex. There is substantial evidence that tetrahydroisoquinolines occur under physiological conditions as well. Whether tetrahydropapaveroline serves as a precursor of morphinanes in mammals, as has been found in opium poppies, remains to be elucidated.
Journal Article↗
[3H]harman binding experiments. I: A reversible and selective radioligand for monoamine oxidase subtype A in the CNS of the rat.
Harman (1-methyl-beta-carboline) is an endogenous compound with neurotropic properties in rats and humans. In a novel in vitro binding assay, the binding site of [3H]harman has been characterized in the rat crude mitochondrial (P2) fraction. The binding was saturable and reversible. Only a single high-affinity binding site was detected by kinetic, saturation, and displacement analyses in the cerebral cortex of the rat. The linear Scatchard plots revealed equilibrium dissociation constant (KD) values of approximately 2.5 nM at 0 degrees C, approximately 9 nM at 23 degrees C, and approximately 30 nM at 37 degrees C. Among six CNS regions (hypothalamus, hippocampus, cerebral cortex, striatum, cerebellum, and spinal cord), the highest density of binding sites (Bmax) was determined in the hypothalamus (approximately 5.5 pmol/mg of protein) and the lowest in the spinal cord (approximately 2.0 pmol/mg of protein). Several drugs known to affect serotonergic, adrenergic, dopaminergic, cholinergic, or GABAergic neurotransmission inhibited specific binding at best in the micromolar range. In contrast, potent and selective inhibitors of monoamine oxidase subtype A were active in the lower and middle nanomolar range. The displacing potency (apparent Ki) of substrates and inhibitors of monoamine oxidase correlated positively and highly significantly with the corresponding values of the inhibition of monoamine oxidase activity of subtype A (r = 0.92, p less than 0.001, n = 17) but not of subtype B (r = -0.47, p greater than 0.05, n = 15). In conclusion, [3H]harman was identified as a specific ligand of the active site of the A subtype of monoamine oxidase in rat brain.
Animals↗
[3H]harman binding experiments. II: Regional and subcellular distribution of specific [3H]harman binding and monoamine oxidase subtypes A and B activity in marmoset and rat.
[3H]Harman (1-[3H]methyl-beta-carboline) was used in a novel radioligand binding assay to label selectively and with high affinity monoamine oxidase (MAO) type A. The concentration of the enzyme was determined in six CNS regions of the primate species marmoset (Callithrix jacchus) and of the rat: hypothalamus, hippocampus, cerebellum, cerebral cortex, striatum, and spinal cord. The specific [3H]harman binding in the CNS of the marmoset reveals the same pharmacological profile and other characteristics (affinity, saturability, and reversibility) as in the CNS of the rat. The regional distribution of the [3H]harman binding density (Bmax) in the CNS exhibits a distinct pattern in the marmoset and the rat and a 35 (hypothalamus) to 75% (hippocampus) lower Bmax in the marmoset than in the rat. The Bmax values of [3H]harman binding in the CNS of the marmoset and the rat combined as well as those from visceral organs of the rat (liver, heart, lung, thymus, spleen, and kidney) correlated positively and highly significantly with the respective Vmax values of specific MAO activity of the A type but not of the B type, determined with kynuramine as the substrate. In subcellular fractionation experiments with rat cerebral cortex, the highest [3H]harman binding density (Bmax) and MAO-A activity (Vmax) were detected in mitochondrial fractions and severalfold lower values in the synaptosomal membrane fraction. In conclusion, we suggest that [3H]harman binding is a biochemical tool as a selective marker to quantify MAO-A in the CNS of different mammalian species as well as in extraneuronal tissues.
Aging↗
Plasma norharman (beta-carboline) levels are elevated in chronic alcoholics.
Based on the hypothesis that condensation products of neurotransmitters with aldehydes are involved in the pathogenesis of alcoholism, aromatic beta-carbolines (norharman and harman) were measured in the blood plasma of alcoholics and nonalcoholics. The identity of the extracted compounds was confirmed by various elution conditions of the high performance liquid chromatography (HPLC), newly developed radioreceptor assays, and the mass spectrum of norharman. The levels of norharman and harman in nonalcoholics were unchanged after a load with ethanol (1 g/kg body weight). The norharman levels of the alcoholics were significantly higher than that of the nonalcoholic controls (99.5 +/- 26.6 pg/ml vs. 26.9 +/- 10.7 pg/ml; p less than 0.001) and did not change significantly during a 3-week detoxication period. In the subgroup of alcoholics with delirium or hallucinosis, a slight increase of norharman during detoxication could be detected while in alcoholics with vegetative withdrawal symptoms norharman levels dropped slightly over time (p = 0.07). No difference was found with respect to harman between nonalcoholics and alcoholics. These results suggest disturbed regulatory processes in the formation and/or metabolism of norharman in alcoholics. Further investigations are needed to reveal a possible marker function of norharman in alcoholic patients.
Adolescent↗
Absence of mesangial IgA in AIDS: a postmortem study.
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Acquired Immunodeficiency Syndrome↗
Evaluation of dairy food processing wash water solids as a protein source: I. Forage intake, animal performance, ruminal fermentation, and site of digestion in heifers fed medium-quality hay.
Twelve ruminally, duodenally, and ileally cannulated (average initial BW 313 +/- 20 kg) and 27 intact Hereford heifers (average initial BW 256 +/- 17 kg) were used in two experiments to evaluate dairy food wash water solids (WWS) as a protein source in medium-quality hay diets. Heifers received a basal diet of orchardgrass hay (7.4% CP) and were assigned to one of three supplement treatments: control (C; .9% CP), WWS (18.8% CP)-, and soybean meal (SBM; 19.1% CP)-based supplements (fed at 1.5 kg of DM/d). Supplements were formulated to have similar ME concentrations. Ruminal ammonia concentrations were greater (P less than .10) for WWS- and SBM-supplemented heifers than for C heifers at most sampling times. Moreover, WWS and SBM increased (P less than .10) total VFA (mM) and acetate (mol/100 mol) and lowered propionate (mol/100 mol) at several sampling times. Ruminal fluid volume (liters) was unchanged (P greater than .10) by treatment; however, fluid dilution and flow rate (liters/h) were less (P less than .10) in C heifers than in heifers fed SBM or WWS supplements. Wash water solids and SBM supplementation increased (P less than .10) OM, NDF, and ADF digestibilities compared with C heifers. Feeding WWS and SBM supplements increased BW at 84 d (P less than .10) compared with C-supplemented heifers. Forage intake at 54 and 84 d by heifers supplemented with SBM or WWS was greater (P less than .10) than by C heifers. Control-supplemented heifers had the least, WWS intermediate, and SBM the greatest ADG at 84 d (P less than .10; .14 vs .35 vs .48 kg/d, respectively). These data indicate that WWS may be used as a protein source without serious adverse effects in heifers consuming medium-quality hay for 84 d.
Ammonia↗
Evaluation of dairy food processing wash water solids as a protein source: II. Microbial protein synthesis, duodenal nitrogen flow, and small intestinal amino acid disappearance.
Twelve ruminally, duodenally, and ileally-cannulated Hereford heifers (average initial BW 313 +/- 20 kg) were used in a replicated experiment to evaluate dairy food processing wash water solids (WWS) as a protein source. Heifers were fed 2.8 kg of chopped (7.6 cm) hay and one of three supplements (1.5 kg/d, DM basis). Supplements were formulated to be similar in energy and contained 1.0 (control), 23.2 (WWS), and 21.6% (soybean meal; SBM) CP on an OM basis. Total N and nonammonia N entering the duodenum (g/d) were greater (P less than .10) for heifers fed WWS and SBM supplements than for controls. Bacterial N flow (g/d) at the duodenum was less (P less than .10) for controls (43.9) than for WWS- (63.9) and SBM- (69.9) supplemented heifers. Feed escape N (g/d) was greater (P less than .10) for WWS-fed heifers than for those fed SBM (32.1 vs 20.7 g/d, respectively). Total tract N digestion (g/d) was greatest (P less than .10) for SBM, intermediate for WWS, and least for control heifers. Microbial protein synthesis (g/kg of OM intake) was enhanced (P less than .10) by WWS and SBM supplementation, but efficiency of synthesis (g/kg of OM fermented) did not differ among treatments. Essential amino acid (AA) disappearance in the small intestine (g/d) was less (P less than .10) for control than for the other two treatments. Nonessential AA disappearance was greatest (P less than .10) for the WWS and least (P less than .10) for the control treatment.(ABSTRACT TRUNCATED AT 250 WORDS)
Amino Acids↗
Evaluation of dairy food processing wash water solids as a protein source: III. Nitrogen utilization by heifers fed medium-concentrate diets.
Eight multicannulated heifers (average BW 415 +/- 34 kg) were used in a replicated 4 x 4 Latin square to evaluate fluid milk processing wash water solids (WWS) as a dietary N source. Heifers were fed corn/cottonseed hull-based diets containing soybean meal (control, 0% WWS N) or WWS replacing soybean meal at 33, 67, or 100% of supplemental dietary N. Total tract and ruminal DM and OM digestibilities decreased linearly or cubically (P less than .05) as dietary WWS N increased. Total ruminal VFA concentration (P less than .05) and propionic acid molar proportion (P less than .10) were greater in heifers fed 0 vs 100% WWS N. Heifers fed 0% WWS N had the greatest (P less than .05) ruminal ammonia concentration at all sampling times. Dietary WWS did not affect (P greater than .10) ruminal pH, fluid dilution rate, fluid flow, fluid volume, or turnover time. Total tract N digestibility decreased quadratically (P less than .10) with increasing WWS N in the diet. Supplemental WWS N did not affect (P greater than .10) flow of duodenal ammonia N or bacterial N, or efficiency of microbial N synthesis. Diets containing WWS N resulted in a cubic increase (P less than .10) in duodenal flow of essential amino acids compared with 0% WWS N; however, there were no differences in small intestinal amino acid disappearance. Data indicate that WWS can replace 33% of the soybean meal N in a corn/cottonseed hull-based diet without decreasing ruminal fermentation, fluid digesta kinetics, microbial efficiency, or small intestinal amino acid utilization.
Amino Acids↗
Beta-carbolines and tetrahydroisoquinolines: detection and function in mammals.
beta-Carbolines occur in man and rat. The concentration in various tissues is about 100 to 1000 times lower than that of classical neurotransmitters. Administration of beta-carbolines in animals induces overlapping but not identical activity profiles. The molecular modes of action differ. For example, harman (1-methyl-beta-carboline) acts as an endogenous inhibitor of monoamine oxidase [E.C. 1.4.3.4.], subtype A, whereas norharman (beta-carboline) probably acts by stimulation of a specific beta-carboline receptor which is different from the benzodiazepine-GABA receptor complex. There is substantial evidence that tetrahydroisoquinolines occur under physiological conditions as well. Whether tetrahydropapaveroline serves as a precursor of morphinanes in mammals, as has been found in opium poppies, remains to be elucidated.
Animals↗
[3H]Harman labels selectively and with high affinity the active site of monoamine oxidase (EC 1.4.3.4) subtype A (MAO-A) in rat, marmoset, and pig.
[3H]Harman was used in binding studies with CNS tissue of rat, pig, and marmoset and with visceral organs of the rat. In the mitochondrial fractions of the CNS of the 3 species [3H]harman binding exhibits the same pharmacological profile in displacement studies. A detailed analysis reveals a high specificity for MAO-A. Furthermore, we applied [3H]harman binding to quantify the MAO-A content in 6 CNS regions of each species as well as in 6 visceral organs of the rat.
Animals↗
Fluctuations of unbound and total phenytoin concentrations during the day in epileptic patients on valproic acid comedication.
The influence of daily fluctuations in the concentration of valproic acid (VPA) on the unbound and total concentration of phenytoin (PT) was examined in a prospective study. The serum concentrations of 28 patients with epilepsy (group PT + VPA) who were treated with PT and concurrently with VPA and 15 patients (group PT) who were treated with PT but without VPA comedication were determined at 8.00, 11.00, 14.00, 17.00, and in part at 20.00 h. The results show that there are significantly greater fluctuations in the total PT concentration among patients on VPA than those not on VPA. The fluctuations in the total PT concentration during the day correlated with the fluctuations in the VPA concentration. On the other hand, the fluctuations in the concentrations of unbound PT of patients on VPA were comparable with those not on VPA. In the absence of VPA, the diurnal fluctuations of the total PT concentration correlated highly significantly with the fluctuations of the unbound PT concentration. This is not the case in patients on VPA. Our data are a further indication of the smaller significance of the total PT concentration as compared with the unbound PT concentration in the combined treatment of PT and VPA.
Adolescent↗
Postmortem serum protein binding and brain concentrations of antiepileptic drugs in autoptic specimens from 45 epileptic patients.
The free fraction of antiepileptic drugs can, in certain diseases, be greatly increased in the serum. In order to study the significance of this increase for the concentration in the brain, the postmortem concentrations of phenytoin (PT), phenobarbital (PB), carbamazepine (CBZ), and its metabolite carbamazepine-10,11-epoxide (CE) in the serum (total and free), as well as in specimens of the frontal cortex of 45 epileptic patients who died from various causes, were determined. The postmortem free fractions were higher than reported in the literature and varied considerably from subject to subject. For PT the free fraction was 21.7% (median), for PB 68.0%, for CBZ 33.4%, and for its metabolite CE 53.6%. The values for a control group of 236 otherwise healthy epileptic patients were in agreement with those given in the literature, namely 10.4% for PT, 55.6% for PB, 20.9% for CBZ, and 42.5% for CE. Using a nonparametric correlation coefficient (Kendall T), the concentrations in the frontal cortex of the autopsied patients correlated with the postmortem free serum concentrations, especially for the substances with high protein binding (PT and CBZ), better (PT r = 0.88, PB r = 0.86, CBZ r = 0.87, CE r = 0.79) than with the total concentrations (PT r = 0.69, PB r = 0.80, CBZ r = 0.77, CE r = 0.77). The study indicates that in critically ill patients the determination of the free concentration in serum is indispensable. If treatment is orientated solely on the total concentration, unexpectedly high concentrations in the brain and hence possible intoxication of the patient in the critical or final state can result.
Anticonvulsants↗
Sulfamethoxazole-trimethoprim (SMZ-TMP) as an effective therapy for Wegener's granulomatosis (WG)--three more cases.
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Adult↗
Valproic acid-induced carbamazepine-10,11-epoxide toxicity in children and adolescents.
The study of 14 children and adolescents shows that the addition of carbamazepine (CBZ) to a basic valproic acid (VPA) therapy can result in unexpectedly high concentrations of carbamazepine-10,11-epoxide (CE) in the serum (up to 13 micrograms/ml). These concentrations were associated with marked side effects, especially vomiting and tiredness. The concentrations of CBZ were within the therapeutic range. Very high CE concentrations can largely be avoided at the commencement of the CBZ treatment if the CBZ dose is slowly increased. But high CE concentrations (4-8 micrograms/ml) associated with side effects can also be reached in later stages during the build up of CBZ treatment and under steady state conditions. The determination of the CE concentration is important when VPA and CBZ are administered together, especially when side effects occur.
Adolescent↗
Nutrient intake and digestion as influenced by wash water solids as a protein source for lambs fed orchardgrass hay.
Two experiments were conducted with sheep fed orchardgrass hay plus one of four supplements to evaluate use of a cheese processing wash water solid (WWS) material as a protein supplement. In both trials, lambs were fed either a cornstarch control (0% WWS-N) or a protein supplement containing 25, 50 or 75% N from WWS (25, 50 or 75% WWS-N, respectively). The majority of the remaining protein was supplied by soybean meal (SBM). Trial 1 was a replicated 4 x 4 extra-period Latin square. Protein supplementation increased total tract NDF and N digestibilities (P less than .10) 13% and 29%, respectively, compared with the cornstarch control. Total tract N digestibility was depressed (P less than .10) when 75% WWS-N (71.5%) vs 25 or 50% WWS-N (75.9 and 75.9%, respectively) was fed. Total VFA were depressed (P less than .10) 6 and 9 h postfeeding in sheep fed 75% WWS-N compared with the control (78.3 and 74.6 mM vs 98.8 and 94.6 mM for 6 and 9 h, respectively). Two hours postfeeding, lambs fed control had lower (P less than .10) ruminal pH compared with lambs fed 25, 50 and 75% WWS-N (6.2 vs 6.4, 6.5 and 6.5, respectively). Ruminal ammonia concentrations were 5 to 10 mg/dl lower (P less than .10) at all times in control lambs. In Trial 2, a metabolism study, feeding 75% WWS-N resulted in lower N digestibility (P less than .10) than did feeding 25% and 50% WWS-N (47.2 vs 56.4 and 55.2%, respectively). Data suggest that up to 50% of the SBM-N in a protein supplement for wethers may be replaced by WWS-N without adversely altering nutrient digestibility, ruminal fermentation or N metabolism.
Animal Feed↗