Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Histidine Decarboxylase”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 19 recordsLinked to original sources
PubMedDate not supplied

[Nonpathogenic Neisseria studied for the content of histidine decarboxylase].

Histidine decarboxylase activity was not found in cells of nonpathogenic neisseria, obtained from bronchi of patients with infectious asthma. The absence of the histidine decarboxylase activity in nonpathogenic neisseria cells suggests that the sensitizing activity of these cells was not caused by a direct effect of histamine of bacterial origin on human branchopulmonary tissues.

Asthma↗
PubMed2003

Rat stomach ECL cells: mode of activation of histidine decarboxylase.

Histidine decarboxylase (HDC) occurs in ECL cells in the oxyntic mucosa of rat stomach. It is activated by gastrin. Refeeding of fasted rats or treatment with the proton pump inhibitor omeprazole promptly raised the serum gastrin concentration and consequently the HDC activity and the HDC protein content of the oxyntic mucosa. The food- and omeprazole-induced increase in HDC mRNA expression in the oxyntic mucosa was modest by comparison. Blockade of translation (cycloheximide) but not transcription (actinomycin D) prevented the postprandial rise in HDC activity. The half-life of HDC activity (after blockade of translation) was 94 min in omeprazole-treated rats and 55 min in fasted controls. The rate of enzyme synthesis was estimated to be 15 times higher in omeprazole-treated rats than in fasted controls. Inhibition of histamine uptake into ECL-cell granules by reserpine, a blocker of the vesicular monoamine transporter type-2, lowered the HDC activity and prevented the gastrin-induced HDC activation. We suggest that HDC activation reflects enhanced transcription, translation and/or posttranslational enzyme activation as well as stabilization, and that a high cytosolic histamine concentration suppresses HDC activation.

Animals↗
PubMed1988

Induction of ornithine decarboxylase and histidine decarboxylase activities in rat colon mucosa after application of 12-o-tetradecanoylphorbol-13-acetate (TPA), sodium deoxycholate and indole.

Ornithine decarboxylase (ODC) and histidine decarboxylase (HDC) activities of rat colon mucosa were induced after intrarectal instillation of 12-o-tetradecanoylphorbol-13-acetate (TPA) and sodium deoxycholate. After instillation of sodium deoxycholate, ODC and HDC activities increased rapidly and reached a peak at 4 h, then decreased quickly towards control levels. Both enzymes activities also increased significantly 4 h after instillation in animals treated with TPA and sodium deoxycholate plus indole. However, there were no changes in ODC and HDC activities from 0-8 h after indole administration. These data are the first to show the induction of HDC activity in colon mucosa by TPA and sodium deoxycholate and suggest that the induction of activities in these two enzymes might be one mechanism of their action as cancer promoters.

Animals↗
PubMed1996

Comparison between activation of ornithine decarboxylase and histidine decarboxylase in rat stomach.

We compared the responses of rat stomach ornithine decarboxylase (ODC) and histidine decarboxylase (HDC) to food intake, oral treatment with antisecretagogues, NaHCO3, and hypertonic NaCl, antrectomy, intravenous infusion of gastrin-17, the selective cholecystokinin (CCK)-B/gastrin receptor antagonist L-365,260, and the somatostatin analogue RC-160. The serum gastrin concentration and oxyntic mucosal ODC and HDC activities were higher in freely fed rats than in fasted rats. Food intake in fasted rats raised the serum gastrin concentration and the ODC and HDC activities. Ranitidine, omeprazole, and NaHCO3 raised the serum gastrin concentration and activated ODC and HDC. Hypertonic NaCl raised the ODC activity 200-fold, whereas circulating gastrin and HDC activity were increased only moderately. Infusion of gastrin-17 activated HDC but not ODC. L-365,260 prevented the activation of HDC but not of ODC in response to food intake and treatment with omeprazole, NaHCO3, or hypertonic NaCl. Antrectomy prevented the food- and omeprazole-evoked rise in oxyntic mucosal HDC activity but not the rise in ODC activity. RC-160 suppressed HDC activity after food intake and treatment with omeprazole, NaHCO3, or NaCl. In contrast, RC-160 suppressed omeprazole- and NaHCO3-evoked ODC activation but not that evoked by food intake or NaCl. The results support the view that HDC in the oxyntic mucosa is activated by gastrin and suppressed by somatostatin. The induction of ODC is not mediated by gastrin; ODC activation appears to be related to acid inhibition per se or to mucosal maintenance and repair; somatostatin, or rather the lack of it, might contribute to the induction of ODC after acid blockade. The mechanism behind the activation of rat stomach ODC seems to differ depending on the type of stimulus.

Analgesics↗
PubMed1999

The pest regions containing C-termini of mammalian ornithine decarboxylase and histidine decarboxylase play different roles in protein degradation.

Proteasome 26S must recognize the PEST region-containing C-terminus of mammalian ornithine decarboxylase (ODC) monomer to proceed with degradation. We have detected PEST regions in both termini of mammalian histidine decarboxylase (HDC). In the present report, a chimaeric ODC/HDC was used to elucidate whether the PEST region-containing C-termini of ODC and HDC are exchangeable. Wild-type rat ODC had an expected antizyme and ATP-dependent degradation. This was not the case for both the chimaera and a C-terminus truncated rat ODC. Results suggest that the PEST region-containing C-terminus of rat HDC should have another role different to confering polypeptide availability to the proteasome.

Adenosine Triphosphate↗
PubMed1976

Specificity in enzyme inhibition. 3. Synthesis of 5-substituted 2,2-dimethyl-4-imidazolidinones as inhibitors of tyrosine decarboxylase and histidine decarboxylase.

2,2-Dimethyl-4-imidazolidinone derivatives of the alpha-amino acids DL-phenylglycine (1), DL-phenylalanine (2), L-tyrosine (3), L-histidine (4), and L-tryptophan (5) were prepared in order to assess their specificity in inhibiting amino acid decarboxylases. Treatment of th alpha-aminonitriles with acetone in the presence of base and heat or treatment of the alpha-amino amides with acetone gave the title compounds in 48-85% yield. The compounds afforded moderate ability to inhibit the decarboxylation of L-phenylalanine, L-tyrosine, or L-histidine in vitro, using crude enzymes. 3 was a better inhibitor of tyrosine decarboxylase (S. faecalis) than 2. 4 and 5 were comparable to 3 in inhibiting tyrosine decarboxylase. 4 was more selective in inhibiting purified histidine decarboxylase (Cl. welchii) than 5, which was inactive. 4 was inactive against fetal rat histidine decarboxylase in vitro.

Animals↗
PubMed1983

Conversion of prohistidine decarboxylase to histidine decarboxylase: peptide chain cleavage by nonhydrolytic serinolysis.

Unlabeled prohistidine decarboxylase and prohistidine decarboxylase containing L-[carboxyl-(18)O]serine or L-[hydroxyl-(18)O]serine were isolated in homogeneous form from mutant 3 of Lactobacillus 30a grown with the appropriately labeled serine. There was no randomization or redistribution of label during growth, isolation of the protein, or enzymatic hydrolysis and reisolation of the labeled amino acids. These proteins were used to show that during proenzyme activation, in which individual pi subunits of the proenzyme are converted to alpha and beta subunits of the active enzyme [Formula: see text] (in which pi, alpha, and beta subunits have the partial structures shown and Prv designates a pyruvoyl group), no (18)O from H(2) (18)O is incorporated into the newly formed carboxyl terminus (Ser-81) of the beta chain, although no labilization of (18)O from proenzyme labeled with L-[carboxyl-(18)O]serine occurred when the proenzyme was activated in H(2) (16)O by the same procedures. The additional oxygen atom present in the carboxyl group of Ser-81 of the beta subunit is transferred from the hydroxyl group of Ser-82 of the proenzyme during the activation reaction. The same result was obtained with wild-type enzyme formed intracellularly. Peptide bond cleavage during activation of the proenzyme thus proceeds by a hitherto unobserved direct or indirect "serinolysis" coupled to alpha,beta-elimination at Ser-82 to yield the pyruvoyl group of the alpha subunit, rather than by hydrolysis. Possible mechanisms for the reaction are discussed briefly.

Amino Acid Sequence↗
PubMed1977

Inhibition of histidine decarboxylase. Derivatives of histidine.

Twenty-eight derivatives of histidine were tested as inhibitors of histidine decarboxylase from rat stomach. Potent inhibition was observed with the methyl ester of L-histidine (1) which had a Ki = 1.8 X 10(-6) M. Substitution on 1 at various positions resulted in a decrease or complete loss of inhibition. Substituent requirements for inhibition of histidine decarboxylase are discussed. A simple disposable apparatus for the radiometric assay of histidine decarboxylase is described.

Animals↗
PubMed1983

Mammalian histidine decarboxylase: effect by protein kinase on mouse mastocytoma histidine decarboxylase.

Mouse mastocytoma histidine decarboxylase is decreased in activity when, in crude preparations, incubated with a cAMP-dependent protein kinase. This effect was not seen with purified preparations of the histidine decarboxylase (specific activity 7-13 mumol X mg-1 X h-1). Further, no incorporation of 32P from AT32P during incubation of this enzyme with the protein kinase could be demonstrated. Therefore, if protein phosphorylation operates in the regulation of the histidine decarboxylase, factors removed during the purification must be involved.

Animals↗
PubMed2002

Spectroscopic analysis of recombinant rat histidine decarboxylase.

Mammalian histidine decarboxylases have not been characterized well owing to their low amounts in tissues and instability. We describe here the first spectroscopic characterization of a mammalian histidine decarboxylase, i.e. a recombinant version of the rat enzyme purified from transformed Escherichia coli cultures, with similar kinetic constants to those reported for mammalian histidine decarboxylases purified from native sources. We analyzed the absorption, fluorescence and circular dichroism spectra of the enzyme and its complexes with the substrate and substrate analogues. The pyridoxal-5'-phosphate-enzyme internal Schiff base is mainly in an enolimine tautomeric form, suggesting an apolar environment around the coenzyme. Michaelis complex formation leads to a polarized, ketoenamine form of the Schiff base. After transaldimination, the coenzyme-substrate Schiff base exists mainly as an unprotonated aldimine, like that observed for dopa decarboxylase. However, the coenzyme-substrate Schiff base suffers greater torsion than that observed in other L-amino acid decarboxylases, which may explain the relatively low catalytic efficiency of this enzyme. The active center is more resistant to the formation of substituted aldamines than the prokaryotic homologous enzyme and other L-amino acid decarboxylases. Characterization of the similarities and differences of mammalian histidine decarboxylase with respect to other homologous enzymes would open new perspectives for the development of new and more specific inhibitors with pharmacological potential.

Animals↗
PubMed2007

Food components inhibiting recombinant human histidine decarboxylase activity.

Histidine decarboxylase (HDC) catalyzes histamine formation from histidine. Histamine is a bioactive amine acting as a neurotransmitter as well as a chemical mediator. Phenolic food components have been tested for their ability to inhibit recombinant human HDC. Epicatechin gallate (ECG) was found to be a potent inhibitor as it inhibited HDC activity in a competitive manner with Ki = 10 muM against l-histidine. Epigallocatechin gallate (EGCG) showed time-dependent inhibition which disappeared under anaerobic conditions. It is probable that time-dependent inhibition could be due to the result of autoxidation of EGCG. The initial burst observed for EGCG suggests that EGCG itself is involved in HDC inhibition as observed for ECG. Our present results have shown that the tested food components can inhibit HDC activity. This inhibition likely affects histamine biosynthesis and possibly leads to controlling the biological action induced by histamine. Therefore, those food components exhibiting HDC inhibitory activity might be potentially useful in controlling histamine-induced biological actions.

Catechin↗
PubMed1985

Pyruvoyl-dependent histidine decarboxylases. Preparation and amino acid sequences of the beta chains of histidine decarboxylase from Clostridium perfringens and Lactobacillus buchneri.

Histidine decarboxylase (HisDCase) from Lactobacillus buchneri was purified to homogeneity. Its subunit structure, (alpha beta)6, and enzymatic properties resemble closely those of the immunologically cross-reactive HisDCase of Lactobacillus 30a (Recsei, P. A., and Snell, E. E. (1984) Annu. Rev. Biochem. 53, 357-387). The complete amino acid sequences of the beta chains of the HisDCase from L. buchneri (81 residues) and Clostridium perfringens (86 residues) were then determined to be a and b, respectively. (a) SEFDKKLNTLGVDRISVSPYKKWSRGYMEPGNIGNGYVSGLKVDAG VVDKTDDMVLDGIGSYDRAETKNAYIGQINMTTAS. (b) TLSEGIHKNIKNIKVRAP KIDKTAISPYDRYCDGYGMPGAYGDGYVSVLKVSVGTVKK TDDILLDGIVSYDRAEINDAYVGQINMLTAS. SEFDKKLNTLGVDRISVSPYKKWSRGYMEPGNIGNGYVSGLKVDAGVV. Although these sequences differ substantially near the NH2-terminal ends, there is striking homology near the COOH termini and also near the NH2 terminus of the two alpha chains (pyruvoyl-Phe-X-Gly-Val-, where X is Ser or Cys). If the four known pyruvoyl-dependent HisDCases arise from inactive proenzymes by the mechanism previously demonstrated for the HisDCase of Lactobacillus 30a (Recsei, P. A., Huynh, Q. K. and Snell, E. E. (1983) Proc. Natl. Acad. Sci. U.S.A. 80, 973-977), then each of these proenzymes has the sequence -Thr-Ala-Ser-Ser-Phe- at the activation site (where -Ser- becomes the COOH terminus of the beta chain and -Ser- becomes the pyruvoyl group blocking the NH2 terminus of the alpha chain), and the sequences around this activation site are highly conserved in all four enzymes. These facts support the assumptions that the four enzymes have evolved from a common ancestral protein, are formed from inactive pyruvate-free proenzymes by similar mechanisms, and have similar catalytic mechanisms.

Amino Acid Sequence↗
PubMed1990

[Histidine decarboxylase activity and free histidine and histamine levels in fish meat].

The activity of histidine decarboxylase was determined in the meat of fresh fish (mackerel, herring, sprat) and in fish stored for 48 hours at +4 degrees C and +18 degrees C. The activity was determined measuring the increase of histamine released from a controlled amount of histidine. A rise was demonstrated in the activity of these enzymes in the meat of fish stored for 48 hours at +18 degrees C. As a result of this activity the histamine level increased considerably, particularly in the meat of these fish species in which the free histidine content exceeds 100 mg/100 g of tissue. The mean activity of histidine decarboxylase obtained in the meat of frozen and fresh fish expressed in nmol of histamine/min/mg of protein was 0.11 +/- 0.06 for mackerel meat, 0.10 +/- 0.04 for herring, and 0.08 +/- 0.04 for sprat.

Animals↗