Relevant bibliographies by topics / Histidine decarboxyase

Academic literature on the topic 'Histidine decarboxyase'

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Published: 11 March 2023

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Journal articles on the topic "Histidine decarboxyase"

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MORII, HIDEAKI, and KENTARO KASAMA. "Activity of Two Histidine Decarboxylases from Photobacterium phosphoreum at Different Temperatures, pHs, and NaCl Concentrations." Journal of Food Protection 67, no. 8 (August 1, 2004): 1736–42. http://dx.doi.org/10.4315/0362-028x-67.8.1736.

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The major causative agent of scombroid poisoning is histamine formed by bacterial decarboxylation of histidine. The authors reported previously that histamine was exclusively formed by the psychrotrophic halophilic bacteria Photobacterium phosphoreum in scombroid fish during storage at or below 10°C. Moreover, histamine-forming ability was affected by two histidine decarboxylases: constitutive and inducible enzymes. This article reports the effect of various growth and reaction conditions, such as temperature, pH, and NaCl concentration, on the activity of two histidine decarboxylases that were isolated and separated by gel chromatography from cell-free extracts of P. phosphoreum. The histidine decarboxylase activity of the cell-free extracts was highest in 7°C culture; in 5% NaCl, culture growth was inhibited, and growth was best in the culture grown at pH 6.0. Moreover, percent activity of the constitutive and inducible enzymes was highest for the inducible enzyme in cultures grown at 7°C and pH 7.5 and in 5% NaCl. The temperature and pH dependences of histidine decarboxylase differed between the constitutive and inducible enzymes; that is, the activity of histidine decarboxylases was optimum at 30°C and pH6.5 for the inducible enzyme and 40°C and pH 6.0 for the constitutive enzyme. The differences in the temperature and pH dependences between the two enzymes extended the activity range of histidine decarboxylase under reaction conditions. On the other hand, histidine decarboxylase activity was optimum in 0% NaCl for the two enzymes. Additionally, the effects of reaction temperature, pH, and NaCl concentration on the constitutive enzyme activity of the cell-free extracts were almost the same as those on the whole histidine decarboxylase activity of the cell-free extracts, suggesting that the constitutive enzyme activity reflected the whole histidine decarboxylase activity.
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Akirthasary, Desty. "REVIEW ARTIKEL : ENZIM L-HISTIDIN DEKARBOKSILASE DAN MEKANISME PENGHAMBATAN." Unesa Journal of Chemistry 10, no. 2 (May 30, 2021): 147–57. http://dx.doi.org/10.26740/ujc.v10n2.p147-157.

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Abstrak. Enzim L-Histidin dekarboksilase merupakan suatu enzim yang digunakan untuk mengkatalis histidin dalam membentuk histamin. Enzim L-Histidin dekarboksilase dapat dimanfaatkan sebagai antialergi, antihistamin serta menjadi komponen dalam memahami mekanisme histamin. Enzim L-histidin dekarboksilase dapat diperoleh dari asam amino yang ada didalam daging, keju dan ikan. Namun sumber utama yaitu ikan busuk disebabkan aktivitas mikroba diatas 4oC dengan waktu cukup lama, kemudian enzim L-Histidin dekarboksilase yang ada dalam ikan akan disintesis menghasilkan histamin. Enzim L-Histidin dekarboksilase terdapat dalam bakteri mesofilik yang tumbuh pada suhu 30oC-37oC. Bakteri tersebut antara lain Morganella morganii, Klebsiella pneumonia, Hafnia alvei, Citrobacter freundii, Clostridium perfringens, Enterobacter aerogenes, Vibrio alginolyticus, dan Proteus sp yang dapat memberikan pengaruh negatif terhadap kesehatan antara lain diare akibat keracunan, sakit kepala, hipotensi, pruritus dan tubuh akan terlihat memerah. Sehingga diperlukan adanya penghambatan aktivitas enzim L- Histidin dekarboksilase. Penghambatan dapat dilakukan untuk mengontrol terbentuknya histamin dengan cara penambahan senyawa yang akan merusak dinding sel suatu bakteri yang mengakibatkan terhentinya fungsi kerja enzim tersebut. Senyawa penghambat yang dapat digunakan dapat berupa senyawa kimiawi seperti asam benzoat atau dapat juga menggunakan senyawa alami yang memiliki kandungan flavonoid, saponin, terpenoid, dan tanin yang akan mencegah pertumbuhan bakteri. Senyawa penghambat tersebut banyak ditemukan pada Teh Hijau, asam jawa, bawang merah atau tanaman rempah lainnya. Kata Kunci : Enzim L-Histidin dekarboksilase, Histidin, Histamin, Abstract. The enzyme L-Histidine decarboxylase is an enzyme used to catalyze histidine to form histamine. The enzyme L-Histidine decarboxylase can be used as antiallergy, antihistamine and a component in understanding the mechanism of histamine. The enzyme L-histidine decarboxylase can be obtained from amino acids present in meat, cheese and fish. However, the main source is rotten fish due to microbial activity above 4oC for a long time, then the L-Histidine decarboxylase enzyme in fish will be synthesized to produce histamine. L-Histidine decarboxylase enzyme is present in mesophilic bacteria that grow at temperatures of 30oC-37oC. These bacteria include Morganella morganii, Klebsiella pneumonia, Hafnia alvei, Citrobacter freundii, Clostridium perfringens, Enterobacter aerogenes, Vibrio alginolyticus, and Proteus sp which can have negative effects on health, including diarrhea due to poisoning, headaches, hypotension, pruritus and the body. looks red. So that it is necessary to inhibit the activity of the enzyme L-Histidine decarboxylase. Inhibition can be done to control the formation of histamine by adding compounds that will damage the cell wall of a bacteria which results in the cessation of the enzyme function. Inhibition compounds that can be used can be chemical compounds such as benzoic acid or you can also use natural compounds that contain flavonoids, saponins, terpenoids, and tannins that will prevent bacterial growth. These inhibiting compounds are found in green tea, tamarind, onions or other spices. Keyword : Decarboxylated L-Histidine Enxymes, HIstidin, Histamine.
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WENDAKOON, CHITRA N., and MORIHIKO SAKAGUCHI. "Inhibition of Amino Acid Decarboxylase Activity of Enterobacter aerogenes by Active Components in Spices." Journal of Food Protection 58, no. 3 (March 1, 1995): 280–83. http://dx.doi.org/10.4315/0362-028x-58.3.280.

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The water and ethanol extracts of several commercially available spices were examined for their inhibitory action on the decarboxylase activity of a crude extract of Enterobacter aerogenes. The water extracts had a negligible effect on histidine decarboxylase activity, except for water extract of cloves which reduced the activity by about 40%. However, the ethanol extracts had a rather higher inhibitory action upon histidine, lysine, and ornithine decarboxylases. Of the spices used, cloves, cinnamon, sage, nutmeg, and allspice were very effective in inhibiting the decarboxylases. Among the components of those spices, cinnamaldehyde and eugenol were found to be effective inhibitors.
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Komori, Hirofumi, Yoko Nitta, Hiroshi Ueno, and Yoshiki Higuchi. "Structural basis for the histamine synthesis by human histidine decarboxylase." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C458. http://dx.doi.org/10.1107/s2053273314095412.

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Histamine is a bioactive amine responsible for a variety of physiological reactions, including allergy, gastric acid secretion, and neurotransmission. In mammals, histamine production from histidine is catalyzed by histidine decarboxylase (HDC). Mammalian HDC is a pyridoxal 5'-phosphate (PLP)-dependent decarboxylase and belongs to the same family as mammalian glutamate decarboxylase (GAD) and mammalian aromatic L-amino acid decarboxylase (AroDC). The decarboxylases of this family function as homodimers and catalyze the formation of physiologically important amines like GABA and dopamine via decarboxylation of glutamate and DOPA, respectively. Despite high sequence homology, both AroDC and HDC react with different substrates. For example, AroDC catalyzes the decarboxylation of several aromatic L-amino acids, but has little activity on histidine. Although such differences are known, the substrate specificity of HDC has not been extensively studied because of the low levels of HDC in the body and the instability of recombinant HDC, even in a well-purified form. However, knowledge about the substrate specificity and decarboxylation mechanism of HDC is valuable from the viewpoint of drug development, as it could help lead to designing of novel drugs to prevent histamine biosynthesis. We have determined the crystal structure of human HDC in complex with inhibitors, histidine methyl ester (HME) and alpha-fluoromethyl histidine (FMH). These structures showed the detailed features of the PLP-inhibitor adduct (external aldimine) in the active site of HDC. These data provided insight into the molecular basis for substrate recognition among the PLP-dependent L-amino acid decarboxylases.
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de las RIVAS, BLANCA, ÁNGELA MARCOBAL, ALFONSO V. CARRASCOSA, and ROSARIO MUÑOZ. "PCR Detection of Foodborne Bacteria Producing the Biogenic Amines Histamine, Tyramine, Putrescine, and Cadaverine." Journal of Food Protection 69, no. 10 (October 1, 2006): 2509–14. http://dx.doi.org/10.4315/0362-028x-69.10.2509.

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This study describes an easy PCR method for the detection of foodborne bacteria that potentially produce histamine, tyramine, putrescine, and cadaverine. Synthetic oligonucleotide pairs for the specific detection of the gene coding for each group of bacterial histidine, tyrosine, ornithine, or lysine decarboxylases were designed. Under the conditions used in this study, the assay yielded fragments of 372 and 531 bp from histidine decarboxylase–encoding genes, a 825-bp fragment from tyrosine decarboxylases, fragments of 624 and 1,440 bp from ornithine decarboxylases, and 1,098- and 1,185-bp fragments from lysine decarboxylases. This is the first PCR method for detection of cadaverine-producing bacteria. The method was successfully applied to several biogenic amine–producing bacterial strains.
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Sköldberg, Filip, Fredrik Rorsman, Jaakko Perheentupa, Mona Landin-Olsson, Eystein S. Husebye, Jan Gustafsson, and Olle Kämpe. "Analysis of Antibody Reactivity against Cysteine Sulfinic Acid Decarboxylase, A Pyridoxal Phosphate-Dependent Enzyme, in Endocrine Autoimmune Disease." Journal of Clinical Endocrinology & Metabolism 89, no. 4 (April 1, 2004): 1636–40. http://dx.doi.org/10.1210/jc.2003-031161.

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Abstract The structurally related group II pyridoxal phosphate (PLP)-dependent amino acid decarboxylases glutamic acid decarboxylase (GAD), aromatic l-amino acid decarboxylase (AADC), and histidine decarboxylase (HDC) are known autoantigens in endocrine disorders. We report, for the first time, the prevalence of serum autoantibody reactivity against cysteine sulfinic acid decarboxylase (CSAD), an enzyme that shares 50% amino acid identity with the 65- and 67-kDa isoforms of GAD (GAD-65 and GAD-67), in endocrine autoimmune disease. Three of 83 patients (3.6%) with autoimmune polyendocrine syndrome type 1 (APS1) were anti-CSAD positive in a radioimmunoprecipitation assay. Anti-CSAD antibodies cross-reacted with GAD-65, and the anti-CSAD-positive sera were also reactive with AADC and HDC. The low frequency of anti-CSAD reactivity is in striking contrast to the prevalence of antibodies against GAD-65, AADC, and HDC in APS1 patients, suggesting that different mechanisms control the immunological tolerance toward CSAD and the other group II decarboxylases. Moreover, CSAD may be a useful mold for the construction of recombinant chimerical antigens in attempts to map conformational epitopes on other group II PLP-dependent amino acid decarboxylases.
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Burdychová, Radka. "Identification and typization of bacteria of the genus Enterococcus supposed to be used for the production of functional foods." Acta Universitatis Agriculturae et Silviculturae Mendelianae Brunensis 55, no. 2 (2007): 9–14. http://dx.doi.org/10.11118/actaun200755020009.

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In this study, the species identification of 12 probiotic strains of the genusEnterococcusfrom Culture Collection of Dairy Microorganisms Lactoflora (CCDM, Milcom, Tábor, Czech Republic) were done using PCR described by DUTKA-MALEN et al. (1995). All strains were classified to be of the genusEnterococcusand speciesE. faecium.These strains are supposed to be used as probiotics for the production of functional foods. According to the fact thatE. faeciumwas described to have decarboxylase activity responsible for biogenic amine production in fermented products, the presence of genes coding for microbial tyrosine and histidine decarboxylase was screened in all strains using PCR described by COTON et al. (2004). Whereas the presence of DNA sequences for histidine decarboxylase was not detected in any strain, specific DNA sequences coding for tyrosine decarboxylases were detected in all tested strains. When applying as starter probiotic cultures to fermented milk products, the production of biogenic amine tyramine have to be observed during both fermentation and storage.
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Pak, Won-Min, Koth-Bong-Woo-Ri Kim, Min-Ji Kim, Ji-Hye Park, Nan-Young Bae, Sun-Hee Park, and Dong-Hyun Ahn. "Effects of Thermal Treatments on Inactivation of Histidine Decarboxylase from Morganella morganii and Photobacterium phosphoreum." Journal of the Korean Society of Food Science and Nutrition 45, no. 3 (March 31, 2016): 396–401. http://dx.doi.org/10.3746/jkfn.2016.45.3.396.

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COSTANTINI, ANTONELLA, MANUELA CERSOSIMO, VINCENZO DEL PRETE, and EMILIA GARCIA-MORUNO. "Production of Biogenic Amines by Lactic Acid Bacteria: Screening by PCR, Thin-Layer Chromatography, and High-Performance Liquid Chromatography of Strains Isolated from Wine and Must." Journal of Food Protection 69, no. 2 (February 1, 2006): 391–96. http://dx.doi.org/10.4315/0362-028x-69.2.391.

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Biogenic amines are frequently found in wine and other fermented food. We investigated the ability of 133 strains of lactic acid bacteria isolated from musts and wines of different origins to produce histamine, tyramine, and putrescine. We detected the genes responsible for encoding the corresponding amino acid decarboxylases through PCR assays using two primer sets for every gene: histidine decarboxylase (hdc), tyrosine decarboxylase (tdc), and ornithine decarboxylase (odc); these primers were taken from the literature or designed by us. Only one strain of Lactobacillus hilgardii was shown to possess the hdc gene, whereas four strains of Lactobacillus brevis had the tdc gene. None of the Oenococcus oeni strains, the main agents of malolactic fermentation, was a biogenic amine producer. All PCR amplicon band–positive results were confirmed by thin-layer chromatography and high-performance liquid chromatography analyses.
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FLEMING, John V., Francisca SÁNCHEZ-JIMÉNEZ, Aurelio A. MOYA-GARCÍA, Michael R. LANGLOIS, and Timothy C. WANG. "Mapping of catalytically important residues in the rat l-histidine decarboxylase enzyme using bioinformatic and site-directed mutagenesis approaches." Biochemical Journal 379, no. 2 (April 15, 2004): 253–61. http://dx.doi.org/10.1042/bj20031525.

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HDC (l-histidine decarboxylase), the enzyme responsible for the catalytic production of histamine from l-histidine, belongs to an evolutionarily conserved family of vitamin B6-dependent enzymes known as the group II decarboxylases. Yet despite the obvious importance of histamine, mammalian HDC enzymes remain poorly characterized at both the biochemical and structural levels. By comparison with the recently described crystal structure of the homologous enzyme l-DOPA decarboxylase, we have been able to identify a number of conserved domains and motifs that are important also for HDC catalysis. This includes residues that were proposed to mediate events within the active site, and HDC proteins carrying mutations in these residues were inactive when expressed in reticulocyte cell lysates reactions. Our studies also suggest that a significant change in quartenary structure occurs during catalysis. This involves a protease sensitive loop, and incubating recombinant HDC with an l-histidine substrate analogue altered enzyme structure so that the loop was no longer exposed for tryptic proteolysis. In total, 27 mutant proteins were used to test the proposed importance of 34 different amino acid residues. This is the most extensive mutagenesis study yet to identify catalytically important residues in a mammalian HDC protein sequence and it provides a number of novel insights into the mechanism of histamine biosynthesis.
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Dissertations / Theses on the topic "Histidine decarboxyase"

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Furuta, Kazuyuki. "Regulation of histamine synthesis through post-translational processing of histidine decarboxylase." 京都大学 (Kyoto University), 2006. http://hdl.handle.net/2433/144287.

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Santibanez, Rodrigo. "The effect of high hydrostatic pressure on histidine decarboxylase and histamine forming bacteria /." Thesis, McGill University, 2007. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=101172.

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Increasing consumer demand for fresh fishery products with minimized loss of their nutritional properties is forcing food industry to look for alternative technologies to maintain the fresh attributes, stability and safety of foods. Demand for fresh tuna fish is no exception, being a valuable source of nutrients with immense health benefits. However, this product is highly perishable and has been commonly implicated in scombroid (histamine) poisoning caused by microbial decarboxylation of histidine contained in high levels in the tissues of scombroid fishes. Current techniques are inadequate for the prevention of histamine formation in fresh fishery products and high pressure processing is a potential alternative for it can inactivate microorganisms and enzymes, without affecting (or only minimally altering) the quality characteristics of foodstuffs. Previous studies have shown a decrease in histamine formation after a high pressure treatment and this study focuses on the effect of high pressure on the histidine decarboxylase enzyme and selected histamine forming microorganisms involved in histamine formation.
Commercial histidine decarboxylase suspended in different media (buffer solution and fish slurry with and without added histidine) was submitted to different high pressure treatments (200--400 MPa) with distinct time durations (0--60 min) at room temperature (20°C--25°C). Enzymatic activity of pressure treated and control samples were then compared by measuring histamine formation. Results were similar in all media; a 200 MPa treatment increased the enzymatic activity a little more than 20% as time increased; a 300 MPa treatment increased activity over 20% at first, followed by a decrease in activity as time increased only to reach a level of residual activity similar or only slightly lower than control samples; and a 400 MPa treatment reduced enzyme activity as time increased to a level of 55% residual activity in a buffer solution where the greatest inactivation was observed.
Enzyme activation and inactivation were affected by a dual effect attributed to a pulse effect, which caused a shift in activity and was independent of the length of the treatment, and a pressure-hold effect, during which activation or inactivation followed first order kinetics. The enzyme appeared highly resistant to pressure in all media as observed from D-values (>2700 min) and pressure sensitivity of destruction rate (zp) values (>500 MPa).
Inactivation of non-pathogen histamine forming bacteria (HFB) Escherichia coli K12 and Bacillus megaterium was evaluated by inoculating cultures in a fish tissue homogenate. Surviving colonies were enumerated after the treatments observing inactivation described by the same dual effect described earlier. Pressures above 300 MPa achieved a significant destruction of E. coli K12 (> 4 log-cycles) while B. megaterium appeared highly resistant for only a 2 log-cycle reduction was observed after at the highest pressure treatment conditions (400 MPa, 20 min).
D-values for both microorganisms decreased as pressure increased being significantly smaller for E. coli K 12, which also appeared to be more sensitive to pressure changes as observed from the zp values (zp = 151.51 MPa and zp = 909.10 MPa for E. coli and B. megaterium respectively. Inactivation caused by the pulse effect appeared very effective for both microorganisms as pressure increased, particularly at 400 MPa (PE > 1.25).
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Sköldberg, Filip. "Studies of Autoantibodies in Systemic and Organ-Specific Autoimmune Disease." Doctoral thesis, Uppsala universitet, Institutionen för medicinska vetenskaper, 2003. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-3421.

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Systemic lupus erythematosus (SLE) is the prototypic systemic autoimmune disease, whereas autoimmune polyendocrine syndrome type 1 (APS1) is a rare autosomal disorder characterized by combinations of organ-specific autoimmune manifestations including hypoparathyroidism and intestinal dysfunction, and may serve as a model for organ-specific autoimmunity. Autoantibodies directed against proteins expressed in the affected tissues are found in both diseases. From a chondrocyte cDNA expression library, we identified the protein AHNAK as an autoantigen in SLE. Anti-AHNAK antibodies were found in 29.5% (18/61) of patients with SLE, 4.6% (5/109) of patients with rheumatoid arthritis, and 1.2% (2/172) of blood donors. Using a candidate approach, we analyzed the prevalence in APS1 and other organ-specific autoimmune diseases, of autoantibodies against the pyridoxal phosphate-dependent enzymes histidine decarboxylase (HDC) and cysteine sulfinic acid decarboxylase (CSAD), which are structurally closely related to known autoantigens. Anti-HDC and anti-CSAD reactivity was detected exclusively in APS1 patient sera. Anti-HDC antibodies were detected in 37.1% (36/97) of the APS1 sera, did not cross-react with aromatic L-amino acid decarboxylase, and were associated with intestinal dysfunction and loss of histamine-producing gastric enterochromaffin-like cells. In contrast, anti-CSAD reactivity was detected in 3.6% (3/83) of APS1 sera and cross-reacted with recombinant glutamic acid decarboxylase. From a parathyroid cDNA expression library, novel spliced transcripts of the CLLD4 gene on human chromosome 13q14, encoding 26 and 31 kDa isoforms recognized by autoantibodies in 3.4% (3/87) of APS1 patients, were identified and found to be preferentially expressed in lung and ovary. Both isoforms contain an N-terminal BTB/POZ domain, similarly to the TNF-alpha-regulated protein B12, localize both to the cytoplasm and nucleus in transfected COS cells, and form oligomers in vitro. The CLLD4 gene is located in a region frequently deleted in several forms of cancer, including lung and ovarian tumors. In conclusion, we have identified and partially characterized AHNAK and HDC as two common targets of autoantibodies in SLE and APS1, respectively. We have also identified CSAD and CLLD4 as two minor autoantigens in APS1, one of which is a novel protein with unknown function.
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Höcker, Michael. "Differentielle Regulation von Schlüsselgenen der gastralen Säuresekretion durch Gastrin, oxidativen Stress und Helicobacter pylori." Doctoral thesis, Humboldt-Universität zu Berlin, Medizinische Fakultät - Universitätsklinikum Charité, 2002. http://dx.doi.org/10.18452/13811.

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Die transkriptionelle Aktivierung des HDC Gens sowie des Chromogranin A Gens in ECL-Zellen der Magenmucosa repräsentiert einen zentralen Mechanismus der Säureregulation durch Gastrin und scheint ausserdem Bedeutung für die Pathogenese der gastroduodenalen Ulkuskrankheit zu haben. Unsere Untersuchungen identifizieren erstmals die molekularen Mechanismen der Gastrin-abhängigen Regulation beider Gene und definieren die beteiligten Transkriptionsfaktoren, regulatorischen DNA-Elemente und intrazellulären Signalwege. Des weiteren wurde durch transgene Untersuchungen die transkriptionelle Regulation des ChromograninA Gens in vivo bestätigt und die neuroendokrin-spezifische Expression eines 4.8kB-langen CgA-Promotorfragmentes demonstriert. Als pathobiologisch relevante Aktivatoren des HDC Gens konnten oxidativer Stress sowie die H. pylori Infektion identifiziert und hinsichtlich ihrer molekularen Wirkungen auf das Schlüsselgen der Histaminsynthese im Magen charakterisiert werden. Diese Ergebnisse dokumentieren einen potentiellen Mechanismus für die Interaktion beider Stimuli mit den physiologischen Regelkreisen der Magensäureregulation und können durch die Definition neuer molekularer Angriffspunkte möglicherweise zur Entwicklung innovativer Therapieansätze beitragen.
Transcriptional activation of the genes encoding histidine decarboxylase and chromogranin A represents a key mechanism of gastrin-dependent acid regulation and also appears to be involved in the pathogenesis of gastroduodenal ulcer disease. Our results for the first time identify the molecular mechanisms underlying gastrin-dependent activation of both genes, and define the transcription factors, regulatory DNA elements and signal transduction pathways involved in this process. Furthermore, transgenic studies confirmed the principle of gastrin-dependent transcriptional activation of the chromogranin A gene in vivo, and demonstrated neuroendocrine-specific expression of a 4.8kB-CgA promotor fragment. In addition, the pathobiological stimuli oxidative stress and H. pylori were molecularly characterized regarding their activating effects on the key gene of gastric histamine sythesis. These results provide potential mechanisms for the interaction of both stimuli with regulatory circuits of gastric acid secretion, and can probably contribute via definition of new molecular targets to the development of inovative therapeutic strategies.
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Rossignoli, Giada. "Aromatic amino acids decarboxylase and histidine decarboxylase: deep functional investigations give insights into pathophysiological mechanisms with possible therapeutic implications." Doctoral thesis, 2019. http://hdl.handle.net/11562/995224.

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Aromatic amino acids decarboxylase and histidine decarboxylase (AADC and HDC) are two homologous enzymes responsible for the synthesis of dopamine/serotonin and histamine, respectively, and other minor signalling aromatic amines. All these molecules are main protagonists or regulators of several physiological pathways, which are fundamental both in central nervous system and in peripheral tissues. Alterations of their homeostasis, indeed, as well as of AADC and HDC functioning or expression, cause and/or participate in the development and progression of several often severe and disabling pathological conditions, such as AADC Deficiency and cholangiocarcinoma. Consequently, AADC and HDC characterization might be useful in the pathophysiological understanding of several diseases and in improving/developing new therapeutic strategies. However, the knowledge of the biochemical features of these two crucial enzymes is still rather limited. Thus, the aim of this thesis is to biochemically characterise human HDC, mostly unknown, and to individuate some possible regulative mechanisms for both HDC and AADC. In addition, a neuronal AADC Deficiency cell model, derived from patient induced pluripotent stem cells (iPSCs), was used to evaluate endogenous AADC features, as well as to research further alterations in dopaminergic pathway. Investigations on human recombinant HDC allowed to discover that, surprisingly, its conformation and catalytic efficiency are influenced by redox state: increasing oxidizing conditions, indeed, favour a more stable and active form of the dimeric enzyme, due to the presence of an intermolecular reversible disulphide bridge involving residue Cys180 of both subunits. Then, in solution analyses of a possible phosphorylation of AADC identified Ser193 as protein kinase A target site, and allowed the detection of an effect on enzyme kinetic parameters, in particular an increased affinity for its substrates. Finally, endogenous AADC levels analyses in dopaminergic neurons derived from AADC Deficiency patients suggested a possible positive feedback mechanism that could tend to increase AADC expression, and the same cell model showed alterations in other cell types besides neurons, in particular glia cells, suggesting that variations in neurons-glia cells Abstract 5 interplay could participate in the pathophysiology mechanisms of AADC Deficiency. Altogether, data and information obtained from the performed experiments have increased AADC and HDC knowledge, as well as paved the way for new hypothesis regarding possible efforts in the development of new disease treatments.
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Fernandes, Henrique Silva. "Computational studies addressed to Histidine decarboxylase." Master's thesis, 2016. https://repositorio-aberto.up.pt/handle/10216/89937.

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Fernandes, Henrique Silva. "Computational studies addressed to Histidine decarboxylase." Dissertação, 2016. https://repositorio-aberto.up.pt/handle/10216/89937.

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Abell, Lynn M. "Isotope effects on pyruvoyl and pyridoxal 5'-phosphate dependent histidine decarboxylases a comparison of cofactor energetics /." 1987. http://catalog.hathitrust.org/api/volumes/oclc/16948155.html.

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Thesis (Ph. D.)--University of Wisconsin--Madison, 1987.
Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references (leaves 204-211).
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Books on the topic "Histidine decarboxyase"

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Barancin, Courtney Ellen. Vibrio anguillarum histidine decarboxylase: Role in histamine biosynthesis and iron acquisition. 1996.

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Book chapters on the topic "Histidine decarboxyase"

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Schomburg, Dietmar, and Margit Salzmann. "Histidine decarboxylase." In Enzyme Handbook 1, 83–87. Berlin, Heidelberg: Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-86605-0_20.

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Schayer, Richard W. "Determination of Histidine Decarboxylase Activity." In Methods of Biochemical Analysis, 273–91. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470110348.ch5.

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Watanabe, T., Y. Taguchi, K. Maeyama, and H. Wada. "Formation of Histamine: Histidine Decarboxylase." In Histamine and Histamine Antagonists, 145–63. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-75840-9_13.

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Tanaka, Satoshi, and Atsushi Ichikawa. "Regulation of Mammalian Histamine Synthesis: Histidine Decarboxylase." In Biomedical Aspects of Histamine, 15–30. Dordrecht: Springer Netherlands, 2010. http://dx.doi.org/10.1007/978-90-481-9349-3_2.

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Hackert, M. L., K. Clinger, S. R. Ernst, E. H. Parks, and E. E. Snell. "Structures of Pyruvoyl-Dependent Histidine Decarboxylase and Mutant-3 Prohistidine Decarboxylase from Lactobacillus 30A." In Crystallography in Molecular Biology, 403–11. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4684-5272-3_37.

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Ohtsu, Hiroshi. "Histamine Synthesis and Lessons Learned from Histidine Decarboxylase Deficient Mice." In Advances in Experimental Medicine and Biology, 21–31. Boston, MA: Springer US, 2010. http://dx.doi.org/10.1007/978-1-4419-8056-4_3.

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Wada, H., M. Ando-Yamamoto, H. Hayashi, Y. Taguchi, H. Fukui, and T. Watanabe. "Demonstration of Immunochemical Cross-Reactivity of Dopa Decarboxylase and Histidine Decarboxylase Using Antibodies Against the Two Enzymes." In Biochemistry of Vitamin B6, 55–58. Basel: Birkhäuser Basel, 1987. http://dx.doi.org/10.1007/978-3-0348-9308-4_11.

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Panula, P., O. Häppölä, T. Watanabe, H. Wada, and H. Päivärinta. "Immunohistochemistry of Histamine and Histidine Decarboxylase in SIF Cells and Intestinal Nerves." In Histochemistry and Cell Biology of Autonomic Neurons and Paraganglia, 51–55. Berlin, Heidelberg: Springer Berlin Heidelberg, 1987. http://dx.doi.org/10.1007/978-3-642-72749-8_9.

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Shan, Ling, Ai-Min Bao, and Dick F. Swaab. "Changes in Histidine Decarboxylase, Histamine N-Methyltransferase and Histamine Receptors in Neuropsychiatric Disorders." In Handbook of Experimental Pharmacology, 259–76. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/164_2016_125.

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Pittenger, Christopher. "Histidine Decarboxylase Knockout Mice as a Model of the Pathophysiology of Tourette Syndrome and Related Conditions." In Handbook of Experimental Pharmacology, 189–215. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/164_2016_127.

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Conference papers on the topic "Histidine decarboxyase"

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Schulman, ES, SC Pugliese, S. Ansaloni, P. Mannam, H. Nishi, M. Bouchard, and SA Saunders. "RNA Interference-Induced Gene Silencing of Histidine Decarboxylase Produces Human Mast Cells Deficient in Histamine." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a3708.

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Chen, Xiaowei, Yoshihiro Takemoto, Karan K. Nagar, Timothy H. Chu, Zhengyu Jiang, Wenju Chang, Richard A. Friedman, Yagnesh H. Tailor, Daniel L. Worthley, and Timothy C. Wang. "Abstract LB-272: Histidine decarboxylase (Hdc)-expressing myeloid cells support Foxp3+ Treg cells and promote colorectal cancer progression." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-lb-272.

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You might also be interested in the extended bibliographies on the topic 'Histidine decarboxyase' for particular source types:
Journal articles
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