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Results for “HISTAMINASE”

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PubMed1983

Distribution of histaminase in human tumor tissues. An immunohistochemical study.

Tissue samples from 125 cases of a variety of human malignancies and benign conditions were examined for the presence of histaminase by the immunoperoxidase method on conventional pathological specimens. Histaminase was found diffusely in the cytoplasm of cancer cells of primary and metastatic tumors of lung, thyroid gland, pancreas, stomach, esophagus, ovary and pharynx. Histaminase-positive cases were also found in carcinoids, dysgerminomas and in melanoma. The incidence of positive histaminase staining in epithelial malignancies overall was 28/84, and those in sarcoma as well as in benign conditions were 1/22 and 0/19, respectively, excluding placental decidual cells and eosinophils intermingled in the tissues. No significant difference in the incidence of histaminase was found by histological type or by degree of cellular differentiation. The present results thus provided another direct evidence for the production of histaminase by many kinds of tumor cells.

Amine Oxidase (Copper-Containing)↗

PubMed1984

Localization of histaminase to the specific granule of the human neutrophil.

The release of histaminase, a diamine oxidase of the human neutrophil, is initiated by soluble secretagogues. Histaminase is simultaneously inactivated by the reactive oxygen intermediates generated by the respiratory burst. Thus, quantitative assessment of histaminase release relative to other granule markers is best achieved in the presence of superoxide dismutase and catalase. Human neutrophils activated with secretagogues preferential for the specific granule, such as calcium ionophore A23187 in a limited concentration, phorbol myristate acetate (PMA), formyl-methionyl-leucylphenylalanine (fMLP), and concanavalin A, release vitamin B12-binding protein, lysozyme, and histaminase but not beta glucuronidase. PMA activation in the presence of cytochalasin B augments the release of lysozyme and initiates the release of beta glucuronidase through recruitment of the azurophilic granule but has no incremental effect on the release of vitamin B12-binding protein and histaminase observed with PMA alone. Subcellular fractionation of resting neutrophils by sucrose density gradient centrifugation to separate specific granules from two classes of azurophilic granules selectively distributes vitamin B12-binding protein and histaminase to the specific granule fractions.

Amine Oxidase (Copper-Containing)↗

PubMed2004

Effect of a plant histaminase on asthmalike reaction induced by inhaled antigen in sensitized guinea pig.

This study evaluates the effects of a copper amine oxidase (histaminase) purified from the pea seedling as a free or immobilized enzyme on asthmalike reactions to inhaled antigen in actively sensitized guinea pig in vivo. Male albino guinea pigs, sensitized with ovalbumin, were challenged with the antigen given by aerosol; free histaminase or CNBr-Sepharose immobilized histaminase was given intraperitoneally (20 microg, 3 or 24 h before antigen challenge) or by aerosol (4 microg, 30 min before or during ovalbumin aerosol). The following parameters were examined: latency time for the onset of respiratory abnormalities, cough severity score, and occurrence and duration of dyspnea. We also evaluated lung histopathology, mast cell degranulation, and lung myeloperoxidase and malonydialdehyde levels. Histaminase significantly reduced the severity of cough and the occurrence of dyspnea and delayed the onset of respiratory abnormalities. Both enzymes prevented bronchial constriction, pulmonary air space inflation, leukocyte infiltration (evaluated as myeloperoxidase activity), and lipoperoxidation of cell membranes (evaluated as malonyldialdehyde production). No relevant differences in pharmacological potency were noted between free or immobilized enzyme. This study provides evidence that histaminase counteracts acute allergic asthmalike reaction in actively sensitized guinea pigs, raising the possibility of new therapeutic strategies for allergic asthma in humans.

Administration, Inhalation↗

PubMed1995

[An analysis of plasma histaminase in schizophrenic patients and its relationship to clinical parameters].

Previous studies have investigated putative alterations in histamine and histamine receptors in schizophrenia, and evidence in favour of the role of this amine as a neurotransmitter or as a neuromodulator was found. In the present study the activity of plasmatic histaminase was analysed, with histamine and with cadaverine as substrates, in a group of 23 schizophrenic patients and compared with that of healthy controls (n = 32). Plasma histaminase activity was determined using Gordon and Peters spectrophotometric method, and the results were expressed in mumoles of H2O2 transformed/hour/litre of plasma at 25 degrees C. Plasmatic histaminase, using histamine as substrate, was significantly increased in schizophrenic patients as a whole compared with the healthy controls. On the other hand, when cadaverine was used as substrate plasma histaminase was significantly reduced in female schizophrenics but not in males. When patients were divided according to 17 clinical characteristics it was found that the following subgroups were significantly associated to high levels of plasma histaminase (using histamine as substrate): the non mentally deteriorated schizophrenic patients compared with mentally deteriorated schizophrenic patients and those with thymic symptoms as opposed to those without thymic symptoms. An extension of this series and a prospective analysis are required to further define the clinical and biological significance of the alteration of this biochemical parameter in schizophrenia, and particularly in relation with a subgroup of schizophrenia with a more favourable course.

Adolescent↗

PubMed2002

A plant histaminase modulates cardiac anaphylactic response in guinea pig.

The effect of a copper amine oxidase (histaminase) purified from the pea seedling as free or immobilized enzyme on the response to specific antigen was studied in isolated hearts from actively sensitized guinea pigs. In vitro challenge with the specific antigen of hearts from actively sensitized animals evokes a positive inotropic and chronotropic effect, a coronary constriction, followed by dilation and an increase in the amount of histamine and nitrites, the oxidation product of nitric oxide, in the perfusates. In the presence of both forms of histaminases, the positive inotropic and chronotropic responses as well as the coronary constriction and the release of histamine were fully blocked. The amount of nitrites, appearing in the perfusates when anaphylaxis is elicited in the presence of both forms of histaminases, is significantly increased, as well as nitric oxide synthase activity and cyclic GMP content in cardiac tissue, while cardiac calcium overload was significantly prevented. These observations demonstrate that the decrease in the anaphylactic release of histamine and the subsequent abatement of the cardiac response to antigen can be accounted for by the inactivation by histaminase of the released histamine and by a stimulation of endogenous nitric oxide production.

Amine Oxidase (Copper-Containing)↗

PubMed1967

The purification and properties of placental histaminase.

1. Histaminase was extracted from desanguinated human placentae and purified by salt fractionation, ion-exchange chromatography and gel filtration. The purest preparation was still contaminated with haptoglobin-methaemoglobin. 2. Histaminase activity was measured by the o-aminobenzaldehyde method of Holmstedt & Tham (1959), Kapeller-Adler's (1951) test and a modified spectrophotometric indigodisulphonate test of greater sensitivity. 3. Unless contaminant metal ions were removed, enzymic activity on cadaverine, but not on histamine, fell during purification. When EDTA was added to the working buffers, a constant ratio between activities towards cadaverine and histamine was maintained throughout the later stages of purification, and activities towards the two substrates could not be separated by any of the highly resolving chromatographic analyses employed. 4. The purest preparation oxidized histamine, agmatine and benzylamine more slowly than the C(4)-C(6) aliphatic diamines, but mixed-substrate experiments suggested that all these amines were substrates of histaminase. 5. The substrate and inhibitor specificities of placental histaminase were compared with those of related enzymes from other sources.

Amine Oxidase (Copper-Containing)↗

PubMed1975

Elevated histaminase (diamine oxidase) activity in small-cell carcinoma of the lung.

To investigate the possible embryologic relation between small-cell carcinoma of the lung and medullary thyroid carcinoma, we measured plasma histaminase (an enzyme found in medullary carcinoma tissue) in 25 patients with small-cell tumors. The assays used histamine and putrescine as substrates. Thirty-two per cent of the patients by the histamine assay, and 31 per cent by the putrescine, had values greater than +2 S.D. from the mean for 63 normal persons. In contrast, among 20 patients with squamous and large-cell lung tumors, one (by the histamine assay), and two (by the putrescine) had elevated values. In four of five autopsy cases, histaminase was high in small-cell carcinoma tissue. The enzyme in plasma and in tumor behaved as classic histaminase in substrate specificity, and in response to inhibitors. The data support the proposed embryologic relation between small-cell lung carcinoma and medullary thyroid carcinoma, and further associate histaminase with some neural crest tumors.

Amine Oxidase (Copper-Containing)↗

PubMed1978

Response of plasma histaminase activity to heparin in normal subjects and in patients with small cell carcinoma of the lung.

Plasma histaminase (PH) activity only partially reflected the consistently high activity of histaminase in tumor tissue of patients with small cell carcinoma of the lung (SCC). To determine whether heparin might release histaminase from tumor tissue into the circulation as it does from some normal tissues, we studied the response of PH activity to small doses of heparin in 41 patients with SCC and in 57 normal subjects. In patients with SCC, the initial mean PH activity (2.0 U/m) was not different from that in normal subjects (1.7 U/ml). After heparin administration, the mean PH activity was no different between the 2 groups (patients with SCC, 3.1 U/ml; normal subjects, 3.5 U/ml). In both groups, the higher the initial PH activity, the greater the magnitude of the PH activity response to heparin. This relationship was linear (normal subjects, r = 0.88; patients with SCC, r = 0.91). However, in patients with SCC, the increase in post-heparin PH activity, as related to the basal levels, was significantly less than that in normal subjects (P less than 0.001 by analysis of covariance). The data suggested that heparin did not affect the release of histaminase from tumor tissue into plasma to the same degree as it promoted the enzyme's entry from normal tissue sources. The differences between the groups may enable us to differentiate between selected patients with SCC and normal subjects with borderline high PH activity values.

Amine Oxidase (Copper-Containing)↗

PubMed1977

Increased histaminase activity in the atrophic muscle of denervated frog.

Sciatic denervation for 1 month in the frog Rana hexadactyla resulted in progressive atrophy of the gastrocnemius muscle without any change in the total DNA content of the whole muscle. Histamine content of the muscle decreased; glutamic and acid content increased and histidine level remained unaltered on denervation. Histaminase activity localized in the muscle decreased; glutamic acid content increased and histidine level remained unaltered on denervation. Histaminase activity localized in the muscle mitochondria increased on denervation. The histidine-degrading enzymes, histidine ammonia lyase, urocanate hydratase and imidazol-5yl lactate dehydrogenase, are localized in the sarcoplasm of the muscle and their activities are not altered on denervation. The histidine decarboxylase activity localized in the mitochondria is not altered on denervation. The reduction in the histamine content of the atrophied muscle may be due to increased mitochondrial histaminase activity but not due to increased decarboxylation of histidine. The loss of 'trophic influence' due to denervation may be manifested in the impairment of mitochondrial histaminase activity.

Acetylcholine↗

PubMed1977

Histaminase release from human eosinophils.

Phagocytosis of opsonized zymosan by human eosinophils results in a dose-dependent noncytotoxic release of histaminase as well as arylsulfatase and beta-glucuronidase. The calcium ionophore A23187 also stimulates release of eosinophil histaminase at concentrations of ionophore which barely release arylsulfatase and beta-glucuronidase. Zymosan-induced histaminase release from eosinophils but not from neutrophils was abolished or markedly reduced in the presence of cytochalasin B, suggesting a difference in the mechanisms of histaminase release from the two granulocyte cell types.

Amine Oxidase (Copper-Containing)↗

PubMed1982

Complement (C3b) interaction with the human granulocyte receptor: correlation of binding of fluid-phase radiolabeled ligand with histaminase release.

The interaction of C3b, the major cleavage product of C3, with its receptor on human granulocytes results in important biological functions, including phagocytosis, superoxide generation, and release of a variety of enzymes, including histaminase. We have determined the binding kinetics and isotherm of trypsin-generated fluid-phase dimeric C3b at both 0 degrees C and 37 degrees C using human polymorphonuclear leukocytes (PMN). At 37 degrees C the apparent number of receptors per cell was threefold greater than number at 0 degrees C (66,000 vs 21,000), and the affinity (Ka) was slightly less (3.5 X 10(7) M-1 vs 6 x 10(7) M-1). C3b dimer binding was specifically inhibited by a F(ab,)2 anti-C3b receptor antibody. C3b dimer induced histaminase release in a dose-dependent fashion at a concentration of 1 to 4 X 10(7) molecules/cell, whereas at lower concentrations a dose-dependent inhibition of opsonized zymosan-induced release was noted. These effects were independent of IgG. In contrast, C3b monomer failed to demonstrate measurable direct binding or to induce histaminase release. Histaminase release, however, did occur after incubation of PMN with affinity-linked monomer (anti-C3 F(ab')2-C3b complexes). Monovalent complexes did not affect release. Monomeric C3, C3c, and C3d were without effect; however, affinity-linked C3 and C3c did cause release.

Amine Oxidase (Copper-Containing)↗

PubMed1978

Immunohistochemical localization of histaminase (diamine oxidase) in decidual cells of human placenta.

An immunohistochemical technique has been developed for the localization of histaminase (diamine oxidase) in human placenta. The procedure utilizes antibody to highly purified human placental enzyme prepared in rabbits. Histaminase is shown to be present in the cytoplasm of the decidual cells of the maternal placenta; the staining is specific and can be removed by preabsorption of the antisera with purified antigen. The present demonstration of histaminase in the maternal portion of placenta confirms previous biochemical data suggesting that the enzyme is not a fetal product in this tissue. This study also provides further evidence that the presence of histaminase in some human tumors and in normal tissues like kidney and intestine is the result of the expression of a mature and not a fetal genome.

Amine Oxidase (Copper-Containing)↗

PubMed1976

Histamine metabolism. II. Cellular and subcellular localization of the catabolic enzymes, histaminase and histamine methyl transferase, in human leukocytes.

Histaminase (EC 1.4.3.6) activity has been demonstrated in human eosinophils and neutrophils, but not in mononuclear cells, with the use of a new and specific thin-layer radiochromatographic enzyme assay. Leukocyte histaminase was physicochemically and functionally similar to histaminase isolated from human placenta and was principally localized to the 27,000-g granule-rich fraction of eosinophil and neutrophil homogenates. Histamine methyl transferase (EC 2.1.1.8), on the other hand, was detected in monocytes but not in granulocytes, eosinophils, lymphocytes, or platelets, and was localized solely to the 100,000-g cell sap supernatant fraction. These data suggest a role of human leukocytes in the catabolism of histamine and therefore in the modulation of histamine-mediated inflammatory reactions.

Amine Oxidase (Copper-Containing)↗

PubMed1986

Changes of serum histaminase activity in pollinosis.

In order to study changes in serum histaminolytic enzyme activity in allergic individuals following allergen challenge, serum histaminase activity was measured using the 0-dianisidine peroxidase method in patients with Japanese cedar pollinosis. Significantly higher serum histaminase activity was detected in pollen season than out of season and a significant relationship was recognized between serum histaminase activity and the severity of nasal symptoms.

Adolescent↗

PubMed1981

Studies on histamine and histaminase in spring catarrh (vernal conjunctivitis).

Patients with spring catarrh (vernal conjunctivitis) were studied for blood histamine (36) and plasma histaminase (16), and were compared with control histamine (22) and histaminase (19) levels. The patients group showed significantly higher histamine and lower histaminase levels than the respective controls. In addition, the patients also had higher eosinophil counts and erythrocyte sedimentation rate. The data suggest that a systemic allergic process may be the most important underlying causative factor in this disorder.

Adolescent↗

PubMedDate not supplied

Tear histamine and histaminase during the early (EPR) and late (LPR) phases of the allergic reaction and the effects of lodoxamide.

The objectives of this study were two-fold: to identify tear histamine content and its relationship to changes in tear histaminase activity during the early (EPR) and late phases (LPR) of the allergic reaction induced by a conjunctival provocation test (CPT) and to evaluate the effects of lodoxamide on histamine release and allergic signs and symptoms during EPR and LPR. A baseline CPT was administered to 20 allergic patients with no baseline signs or symptoms of allergy. Clinical signs and symptoms were evaluated after 20 minutes and 6 hours. Tear samples were taken after 5-10 minutes and after 6 hours for subsequent analyses of cytology and histamine content (ELISA). Patients were then randomly assigned to receive lodoxamide or placebo four times daily for one week in a double-masked fashion. A second CPT was done after this therapy and the same parameters were re-evaluated. During EPR, tear histamine increased significantly with respect to baseline values (p < 0.05). During LPR, tear histamine increased significantly (p < 0.05) only in histamine inactivated samples. Histaminase enzymes were also significantly less active during the EPR (5.5 +/- 0.7) than the LPR (9.9 +/- 2.3) and at baseline. Histamine levels significantly correlated with allergic signs and symptoms (p < 0.05) only during the EPR. Lodoxamide significantly reduced histamine release during EPR (p < 0.05), allergic signs and symptoms during both EPR (p < 0.001) and LPR (p < 0.005), and tear cytology counts during LPR. In conclusion, greater histaminase activity may account for the smaller amount of tear histamine generally found during LPR, while these enzymes seem to play less of a role during the surge of histamine release and activity in the EPR. Lodoxamide was shown to ideally inhibit various aspects of the allergic reaction: clinical signs and symptoms in both the early and late phases, the primarily EPR-related peak of histamine release, and the primarily LPR-related changes in tear cytology.

Administration, Topical↗

PubMed1978

Immunofluorescent staining of histaminase (diamine oxidase) in human placenta.

An immunofluorescent procedure for the localization of histaminase in human tissue sections has been developed by using a specific antiserum against human placental histaminase. For localization of this enzyme in placental sections, fixation in equal volumes mixture of absolute ethanol and acetone provided the optimum visualization of this enzyme in both frozen sections and paraffin-embedded sections. The immunofluorescent staining of this enzyme in placenta is found to be localized in areas within the maternal decidua, both within the cytoplasm of the decidual cells and in tissue space between the cells. The chorionic villi are completely void of the immunofluorescent stain. Variations in patterns of histaminase localization have been found between term and premature placentas, with the former showing a predominantly intercellular localization and the latter a predominantly intracellular localization. The intercellular localization of this enzyme in the decidua may represent a nonspecific diffusion of the enzyme associated with delivery of the placenta or may reflex a specific functional role of the enzyme in the intercellular space during pregnancy.

Acetone↗

PubMed1976

Histamine metabolism. I. Thin-layer radiochromatographic assays for histaminase and histidine decarboxylase enzyme activities.

Thin-layer radiochromatographic methods for the measurement of histaminase and histidine decarboxylase activities have been developed. The assays are specific for the respective enzymes, are sensitive and reproducible, and can be performed using commercially available substrates. The histaminase assay permits determination of enzyme activity from 2.5 mul of pregnancy sera, 1-2 X 10(6) human granulocytes, and microgram quantities of partially purified human placenta histaminase with an error of less than 5 per cent. The histidine decarboxylase assay permits measurement of nanogram quantities of newly formed histamine from as few as 2 X 10(4) rat peritoneal mast cells or rat basophilic leukemia cells with an error of less than 5 per cent.

Amine Oxidase (Copper-Containing)↗