Effect Of L-histidine Research Articles

The effect of L-histidine on nickel translocation and the activities of antioxidant enzymes in hyperaccumulator (Odontarrhena inflata) and non-accumulator (Aurinia saxatilis) plants

The effect of L-histidine on nickel translocation and the activities of antioxidant enzymes in hyperaccumulator (Odontarrhena inflata) and non-accumulator (Aurinia saxatilis) plants

Effects of L-Histidine and Sodium Acetate on β-Casein Expression in Nutrient-Restricted Bovine Mammary Epithelial Cells

Simple SummaryNutrient restriction is known to decrease the milk production and milk quality of dairy cows. However, providing cows with abundant nutrients also has a disadvantage because it will increase feed costs. Under such a situation, the use of feed additives can be a good strategy to reduce the feed cost. The objective of this study was to investigate the effects of histidine and sodium acetate on β-casein expression in nutrient-restricted bovine mammary epithelial cells. The results indicate that histidine has the potential to increase the β-casein levels in bovine mammary cells when the nutrient is restricted, suggesting that histidine is a potential feed additive for cows in a nutrient-insufficient environment.Nutrient restriction is a challenging condition for the mammary glands of dairy cows. In this condition, supplementing amino acids and energy sources might be a good strategy to improve the concentration of one of the most important caseins in bovine milk. Therefore, the objective of this study was to investigate the effects of L-histidine (His) and sodium acetate (Ace) in a nutrient-restricted (NR) immortalized bovine mammary epithelial cell line (MAC-T cells). The treatments for the MAC-T cells are as follows: experiment (1) 0–5% diluted basal medium; experiment (2) supplementation of 0–9.6 mM of His or Ace in NR or normal conditions; experiment (3) supplementation of 0–9.6 mM of Ace plus 0.15 mM of His in NR or normal conditions. The 1% diluted medium showed no significant effect on the cell viability with the basal medium; thus, it was selected as the NR condition. The relative expression of β-casein was significantly increased in the NR condition with the inclusion of 0.15 mM His alone or with Ace compared to that in control. The supplementation of Ace increased the β-casein level under normal conditions. However, it did not change the expression of β-casein under the NR condition. The results suggest that His has the potential to increase the β-casein expression under the NR condition.

Effect of l-histidine and l-lysine on the properties of oil-in-water emulsions stabilized by porcine myofibrillar proteins at low/high ionic strength

The effects of l-histidine (His) and l-lysine (Lys) on the emulsifying and interfacial properties of porcine myofibrillar proteins (MPs) at low/high ionic strength were investigated to improve physical stability of MPs emulsion at low ionic strength. Results showed that His and Lys increased emulsion stability index, and decreased creaming index at low ionic strength, but caused no significant changes in both indexes at high ionic strength. Additionaly, His and Lys increased the emulsifying activity and apparent viscosity, but decreased the droplet size at both ionic strength. His and Lys also promoted the diffusion of MPs and increased the interfacial pressure. Meanwhile, the interfacial loading of MPs was increased (p < 0.05) by 16.07% and 12.79% at low ionic strength, and by 8.85% and 8.24% at high ionic strength in the presence of Lys and His, respectively. Raman spectra revealed that the α-helix content of MPs was decreased (p < 0.05) by 5.05% and 11.79% at low ionic strength, and by 12.14% and 7.23% at high ionic strength in the presence of Lys and His, respectively. In summary, His and Lys enhanced the stability of MPs emulsion at low ionic strength via changing the structure and interfacial behaviour of MPs.

Effect of l-histidine on the heat-induced aggregation of bighead carp (Aristichthys nobilis) myosin in low/high ionic strength solution

In this study, the effects of l-histidine (L-His) on the aggregation of bighead carp (Aristichthys nobilis) myosin induced by heating in low (0.1) or high (0.5) ionic strength solutions were studied. The solubility of natural myosin was significantly enhanced by L-His both in low and high ionic strength solutions. More small particles are suspended in the heated solution containing L-His, inducing a higher solubility than that solution without L-His. The surface hydrophobicity of myosin in a low ionic strength solution containing L-His is higher than that of myosin without L-His. The results of morphology show that L-His induced myosin to form finer aggregates and a honeycomb-like network in a low/high ionic strength solution during heat treatment. These results demonstrate that L-His might disrupt the electrostatic property of unfolded myosin heat-induced through electrostatic binding with the exposed negatively charged amino acid residues, which might disarrange hydrophobic surfaces, resulting in weakening hydrophobic interactions, which ultimately suppresses the fierce aggregation of carp myosin.

The effects of L-histidine on the light and perspiration stability of 4,4’-diamino-stilbene-2,2’-disulfonic acid-based fluorescent whiteness agents on cotton fabrics

The influence of L-histidine on the light and perspiration stability of 4,4’-diamino-stilbene-2,2’-disulfonic acid-based fluorescent whiteness agents (DSD-based FWAs) for cotton fabrics was investigated in this paper. The results indicated that the single component L-histidine accelerated the photo-discoloration of DSD-based FWAs. In the absence of L-histidine, DSD-based FWAs tended to have poor light stability in the strongly acidic condition (pH &lt; 4), whereas they had relatively high and consistent stability under the opposite circumstance (pH &gt; 4). However, in the presence of L-histidine solution, the light stability of DSD-based FWAs was poorer than their counterparts without L-histidine, and was enhanced linearly with the growth of pH value. Therefore, absorption actions caused by L-histidine, oxidization-related promotion for FWAs and photo-decomposition of L-histidine in the acidic condition have been proposed to analyze the comprehensive effects of L-histidine in perspiration on the light stability of DSD-based FWAs on cotton fabrics.

Histidine Decarboxylase Deficiency Causes Tourette Syndrome: Parallel Findings in Humans and Mice

Tourette syndrome (TS) is characterized by tics, sensorimotor gating deficiencies, and abnormalities of cortico-basal ganglia circuits. A mutation in histidine decarboxylase (Hdc), the key enzyme for the biosynthesis of histamine (HA), has been implicated as a rare genetic cause. Hdc knockout mice exhibited potentiated tic-like stereotypies, recapitulating core phenomenology of TS; these were mitigated by the dopamine (DA) D2 antagonist haloperidol, a proven pharmacotherapy, and by HA infusion into the brain. Prepulse inhibition was impaired in both mice and humans carrying Hdc mutations. HA infusion reduced striatal DA levels; in Hdc knockout mice, striatal DA was increased and the DA-regulated immediate early gene Fos was upregulated. DA D2/D3 receptor binding was altered both in mice and in humans carrying the Hdc mutation. These data confirm histidine decarboxylase deficiency as a rare cause of TS and identify HA-DA interactions in the basal ganglia as an important locus of pathology.

Effects of l-histidine and histamine H3 receptor modulators on ethanol-induced sedation in mice

Recent studies suggest that the brain histaminergic system and especially the H3 receptors are involved in the regulation of alcohol consumption and alcohol-induced behaviors. Part of this effect might be due to a modulation of ethanol-induced sedation by central histamine. The aim of the present study was to investigate the effects of several histaminergic drugs on ethanol-induced sedation using the loss of righting reflex experimental protocol in female Swiss mice. A pretreatment with l-histidine, the histamine precursor, significantly reduced ethanol-induced sedation, suggesting that brain histamine protects against the sedative effects of ethanol. In a second set of experiments, several H3 receptor agonists (immepip or imetit) and inverse agonists/antagonists (thioperamide, A331440, or BF2.649) were tested. Surprisingly, both H3 receptor agonists and antagonists potentiated the sedative effects of ethanol. This paradoxical effect might be due to the subtle regulatory actions related to the H3 heteroreceptor function.

L-histidine provokes a state-dependent memory retrieval deficit in mice re-exposed to the elevated plus-maze

The effects of L-histidine (LH) on anxiety and memory retrieval were investigated in adult male Swiss Albino mice (weight 30-35 g) using the elevated plus-maze. The test was performed on two consecutive days: trial 1 (T1) and trial 2 (T2). In T1, mice received an intraperitoneal injection of saline (SAL) or LH before the test and were then injected again and retested 24 h later. LH had no effect on anxiety at the dose of 200 mg/kg since there was no difference between the SAL-SAL and LH-LH groups at T1 regarding open-arm entries (OAE) and open-arm time (OAT) (mean ± SEM; OAE: 4.0 ± 0.71, 4.80 ± 1.05; OAT: 40.55 ± 9.90, 51.55 ± 12.10, respectively; P > 0.05, Kruskal-Wallis test), or at the dose of 500 mg/kg (OAE: 5.27 ± 0.73, 4.87 ± 0.66; OAT: 63.93 ± 11.72, 63.58 ± 10.22; P > 0.05, Fisher LSD test). At T2, LH-LH animals did not reduce open-arm activity (OAE and OAT) at the dose of 200 mg/kg (T1: 4.87 ± 0.66, T2: 5.47 ± 1.05; T1: 63.58 ± 10.22; T2: 49.01 ± 8.43 for OAE and OAT, respectively; P > 0.05, Wilcoxon test) or at the dose of 500 mg/kg (T1: 4.80 ± 1.60, T2: 4.70 ± 1.04; T1: 51.55 ± 12.10, T2: 43.88 ± 10.64 for OAE and OAT, respectively; P > 0.05, Fisher LSD test), showing an inability to evoke memory 24 h later. These data suggest that LH does not act on anxiety but does induce a state-dependent memory retrieval deficit in mice.

L-histidine provokes a state-dependent memory retrieval deficit in mice re-exposed to the elevated plus-maze

The effects of L-histidine (LH) on anxiety and memory retrieval were investigated in adult male Swiss Albino mice (weight 30-35 g) using the elevated plus-maze. The test was performed on two consecutive days: trial 1 (T1) and trial 2 (T2). In T1, mice received an intraperitoneal injection of saline (SAL) or LH before the test and were then injected again and retested 24 h later. LH had no effect on anxiety at the dose of 200 mg/kg since there was no difference between the SAL-SAL and LH-LH groups at T1 regarding open-arm entries (OAE) and open-arm time (OAT) (mean +/- SEM; OAE: 4.0 +/- 0.71, 4.80 +/- 1.05; OAT: 40.55 +/- 9.90, 51.55 +/- 12.10, respectively; P > 0.05, Kruskal-Wallis test), or at the dose of 500 mg/kg (OAE: 5.27 +/- 0.73, 4.87 +/- 0.66; OAT: 63.93 +/- 11.72, 63.58 +/- 10.22; P > 0.05, Fisher LSD test). At T2, LH-LH animals did not reduce open-arm activity (OAE and OAT) at the dose of 200 mg/kg (T1: 4.87 +/- 0.66, T2: 5.47 +/- 1.05; T1: 63.58 +/- 10.22; T2: 49.01 +/- 8.43 for OAE and OAT, respectively; P > 0.05, Wilcoxon test) or at the dose of 500 mg/kg (T1: 4.80 +/- 1.60, T2: 4.70 +/- 1.04; T1: 51.55 +/- 12.10, T2: 43.88 +/- 10.64 for OAE and OAT, respectively; P > 0.05, Fisher LSD test), showing an inability to evoke memory 24 h later. These data suggest that LH does not act on anxiety but does induce a state-dependent memory retrieval deficit in mice.

Pretreatment with l-histidine produces a shift from methamphetamine-induced stereotypical biting to persistent locomotion in mice

The administration of methamphetamine (METH; 10 mg/kg, i.p.) to male ICR mice induced bizarre behaviors including persistent locomotion and stereotypical behaviors, which were classified into four categories: stereotypical head-bobbing, circling, sniffing, and biting. Pretreatment with l-histidine (750 mg/kg, i.p.) significantly decreased the stereotypical biting induced by METH and significantly increased persistent locomotion. This effect of l-histidine on behavior was completely abolished by simultaneous administration of pyrilamine or ketotifen (brain-penetrating histamine H 1 receptor antagonists; 10 mg/kg each, i.p.), but not by the administration of fexofenadine (a non-sedating histamine H 1 receptor antagonist that does not cross the blood-brain barrier; 20 mg/kg), zolantidine (a brain-penetrating histamine H 2 receptor antagonist; 10 mg/kg), thioperamide, or clobenpropit (brain-penetrating histamine H 3 receptor antagonists; 10 mg/kg each). The histamine content of the hypothalamus was significantly increased by l-histidine treatment. These data suggest that l-histidine modifies the effects of METH through central histamine H 1 receptors.

Possible involvement of phospholipase A(2) and cyclooxygenase in stimulatory action of L-histidine on protein synthesis in L6 myotubes.

Effects of L-histidine and related compounds on protein synthesiswere studied in cultured L6 myotubes. L-Histidine specifically stimulated protein synthesis, whereas D-histidine, histamine, L-arginine and L-lysine did not. Inhibitors of phospholipase A(2), phospholipase C and cyclooxygenase intercepted the stimulatory action of L-histidine on protein synthesis, while inhibitors of protein kinase C and 5-lipoxygenase did not. These results suggest an involvement of phospholipase A(2) and cyclooxygenase in the stimulatory action of L-histidine on protein synthesis in L6 myotubes.

Effects of L-histidine and its structural analogues on human N-myristoyltransferase activity and importance of EEVEH amino acid sequence for enzyme activity.

Myristoyl-CoA:protein N-myristoyltransferase (NMT) is an essential eukaryotic enzyme that catalyzes the cotranslational transfer of myristate to the NH2-terminal glycine residue of a number of important proteins of diverse function. Human NMT (hNMT) activity was found to be activated by L-histidine in a concentration-dependent manner. In contrast, two structural analogues of L-histidine, L-histidinol and histamine, inhibited hNMT activity in a noncompetitive manner with half-maximal inhibitions of 18 and 1.5 mM, respectively. The inhibition of hNMT activity by L-histidinol was reversed by a 2-fold molar excess of L-histidine, suggesting that L-histidine and L-histidinol were competing for a common site on NMT. Kinetic data indicated that whereas L-histidine enhanced the Vmax, both L-histidinol and histamine decreased the Vmax; none of these compounds altered the Km. Our studies suggest that L-histidine and its analogues may be interacting with His-293, involved in myristoyl-CoA transfer, rather than His-218, and implicated in the transfer of myristoyl-CoA to the peptide substrates. Site-directed mutagenesis of His-293, Val-291, and Glu-290 resulted in proteins with no measurable NMT activity. The most conserved region in the catalytic domain EEVEH (289-293) is critical for the myristoyl-CoA transfer in the NMT-catalyzed reactions. This region will be useful for the design of regulators of NMT function.

The mechanism of the enhancing effects of l-histidine on the clastogenic activities of hydrogen peroxide

The mechanism of the enhancing effects of l-histidine on the clastogenic activities of hydrogen peroxide

P-42 - Effects of L-histidine on locomotion of ICR mice.

P-42 - Effects of L-histidine on locomotion of ICR mice.

Effects of amino acids on zinc transport in rat erythrocytes.

1. A significant proportion of plasma zinc exists complexed with amino acids. The effect of amino acids on the accumulation of radioactive zinc by rat erythrocytes was studied in vitro, to investigate the hypothesis that zinc might be transported into cells as an amino acid-zinc complex. 2. L-Histidine (500 microM-10 mM) stimulated 65Zn uptake; 50 mM-L-histidine gave a slight inhibition of uptake. D-Histidine (500 microM-10 mM) inhibited uptake in a dose-dependent manner. A non-zinc-binding amino acid, L-alanine, did not affect 65Zn uptake. 3. The effect of L-histidine was sodium dependent and temperature dependent, but was DIDS insensitive. These properties suggest that zinc is being transported as a zinc-histidine complex, utilizing an amino acid carrier system. Uptake of zinc in the presence of L-histidine differed from the previously described ionic mechanism, and may represent a physiological route of uptake. 4. L-Histidine stimulated efflux of 65Zn from pre-loaded cells. 5. The relevance of transport of a zinc-histidine complex is discussed with reference to histidinaemia, and as a significant zinc transport system in the presence of the very low ionic zinc concentrations found in plasma.

The Role of Extracellular Medium Components and Specific Amino Acids in the Cytotoxic Response of Escherichia Coli and Chinese Hamster Ovary Cells to Hydrogen Peroxide

A concentration of H2O2 resulting in mode one killing of Escherichia coli is more toxic when exposure to the oxidant is performed in complete medium (K medium), as compared to a saline (M9 salts). Inorganic salts (MgSO4 and CaCl2), thiamine or glucose, when added separately, or combined, to M9 salts had no effect on the cytotoxic response to H2O2. In contrast, the lethality of the oxidant was highly dependent on the presence of the amino acids in the incubation medium. The addition of glucose further enhanced this response. Among the seventeen amino acids which are present in the complete amino acid mixture, only two, i.e. L-histidine and L-cystine, were found to increase the toxicity of H2O2. Again, glucose augmented this response. The effect of these amino acids on the growth inhibitory action of hydrogen peroxide was also tested in Chinese Hamster Ovary cells. It was found that L-histidine was capable of increasing the toxicity of the oxidant whereas all the other amino acids did not affect the toxicity of the oxidant. Glucose only slightly augmented this effect of L-histidine. DNA single strand breakage produced by H2O2 was increased by L-histidine and was not significantly modified by the other amino acids. DNA double strand breakage was also shown to occur in cells exposed to H2O2-L-histidine, and this effect was independent on the presence of glucose. These results demonstrate that the cytotoxic response of bacterial and mammalian cells to challenge with H2O2 is highly dependent on the composition of the extracellular milieu.(ABSTRACT TRUNCATED AT 250 WORDS)

Lack of evidence for the involvement of catecholaminergic mechanisms in the behavioral anti-methamphetamine effect of L-histidine in the mouse.

The effects of L-histidine (HIS) on the hypermotility and the changes in brain monoamine dynamics induced by methamphetamine (MAMP) were examined in mice. HIS (1000 mg/kg) completely inhibited the hypermotility induced by MAMP (1 mg/kg). MAMP (1 mg/kg) significantly increased the dopamine level and decreased the 3,4-dihydroxyphenylacetic acid level. MAMP (5 and 10 mg/kg) also produced changes in the levels of noradrenaline, serotonin and their metabolites. HIS administered alone caused no significant changes in the levels of these amines and metabolites, nor did it affect MAMP-induced alterations in monoamine dynamics. These results suggest that catecholaminergic mechanisms are not involved in the behavioral anti-MAMP action of HIS.

Effect of L-histidine in vivo on human platelet function and arachidonic acid metabolism

The effect of the amino acid 1-histidine on human platelet function and arachidonic acid metabolism was studied in 18 healthy subjects with increased spontaneous platelet aggregation. The participants received placebo or 1-histidine 3g/day for 7 days. The intake of 1-histidine reduced the degree of spontaneous platelet aggregation (p < 0.05) and inhibited the generation of platelet TXB2 by 47% (p < 0.001) whereas platelet PGE2 synthesis was not affected. The mean 1-histidine plasma concentration increased from 83.l ± 2.4 to 108 ± 8.l μmol/l (p < 0.01) during the study. L-histidine was found to be an effective inhibitor of spontaneous platelet aggregation and platelet TXB2 generation. The present data verify interactions of histidine with human platelet function, probably mediated by arachidonic acid metabolites.

Methods for measuring mutagenicity in urine of rats dosed with [ 14C]DI(2-ethylhexyl)phthalate

Di(2-ethylhexyl)phthalate (DEHP) is extensively used as a plasticizer for vinyl plastic articles. It has been found to be positive in an NCI rodent bioassay but has generally given negative results in in vitro genotoxicity tests. We therefore decided to test the urine of rats fed [ 14C] DEHP for mutagenic activity in the Ames Salmonella test. The recovery of radioactivity from the urine of rats dosed with [ 14C] DEHP was examined by solvent extraction and XAD-2 resin absorption procedures. Both of these procedures were inadequate for quantitative recovery of urinary metabolites required for subsequent mutagenicity testing using the Ames Salmonella/microsome procedure. Recoveries of less than 5% were observed using standard solvent extraction techniques whereas the XAD-2 adsorption technique gave about 67% at high resin/urine ratios. Treatment of the urine with β-glucuronidase/aryl sulfatase did not affect these recoveries. The direct urine plating procedure represents a viable alternative to the above concentration procedures for this phthalate ester. The effects of L-histidine and the β-glucuronidase/aryl sulfatase preparation on the background reversion frequencies of the Ames tester strains is discussed.

Characteristics of a cationic amino acid transport system in the basolateral membrane of the cat salivary epithelium.

The specificity and kinetics of L-lysine influx across the basolateral surface of the cat salivary epithelium have been investigated in the perfused cat submandibular gland using a high-resolution, paired-tracer dilution technique. L-lysine influx was measured at several different perfusate concentrations (0.05-2.5 mM) and was found to be saturable. A Michaelis-Menten analysis based on a single entry site gave a Km of 0.49 +/- 0.08 mM and a Vmax of 231 +/- 20 nmol/min X g. The uptake of L-lysine was highly stereospecific and markedly inhibited by L-arginine (0.25-2.5 mM). The inhibitor constant (Ki) was 0.23 mM, suggesting that the carrier had a greater affinity for L-arginine than L-lysine. When the inhibitory effects of L-histidine (0.5-10 mM) were examined the Ki, estimated at 10 mM, was 4.6 mM. Nine other neutral amino acids (L-alanine, L-serine, L-cysteine, glycine, L-proline, L-homoserine, L-leucine, L-phenylalanine and L-glutamine), and an acidic amino acid (L-aspartate) were also tested at 10 mM and, although several caused inhibition, the Ki was always at least 20 times higher than the measured Km for L-lysine. It is concluded the carrier is highly specific for the L-form of the basic amino acids. The sodium dependence of L-lysine influx was investigated over a range of L-lysine concentrations (0.05-1 mM), and total removal of sodium from the perfusate had no effect on L-lysine influx. In the presence of sodium, L-homoserine, an amino acid not normally present in animal tissues, inhibited L-lysine influx (Ki = 13 mM). This inhibition was not observed in the absence of sodium, and contrasts with the observation that the inhibitory action of L-histidine was sodium independent. The present data suggest that a specific cationic amino acid transport system is operative in the basolateral membrane of the cat salivary epithelium. The properties of this system appear to be similar to the system y+ which has been described in several other cell types.