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PubMedDate not supplied

Effect of mepyramine on the histaminase release induced by heparin injection and anaphylaxis in guinea pigs.

Injection of heparin as well as antigenic challenge in sensitized guinea pigs are known to produce a release of histaminase into the plasma. In the present study, tissue histaminase estimation was done by Spencer's method (17) and plasma estimation by Kapellar Adler's (7) method. Mepyramine pretreatment considerably decreased the histaminase release by both heparin and anaphylaxis. Mepyramine did not antagonise the anticoagulant action of heparin in vitro.

Amine Oxidase (Copper-Containing)↗
PubMed1981

Tumor and placental histaminase, I. affinity chromatography purification and characterization of the placental enzyme.

Histaminase (diamine oxidase) is an enzyme produced at very high levels by the decidua of the placenta and is found to be associated with a number of human cancers. A procedure for the affinity chromatography purification of this enzyme is described. In this procedure, cadaverine-AH-sepharose was used to bind the enzyme in the placental extract. After extensive washing of the column with 2.5% Triton X-100 in 1 M NaCl, the enzyme was released from the column by 0.1 N chromotropic acid. This purification, essentially a one step procedure, provided 1800-fold purification, and yielded mg quantities of histaminase, homogeneous by SDS-gel electrophoresis and immunodiffusion tests. The procedure usually recovered more than 40% of the enzyme applied and the specific activity of the final enzyme preparation was around 5000 units/mg protein. SDS-gel electrophoresis of the enzyme in different concentrations of acrylamide indicated that the subunit molecular weight of histaminase was about 90,000. Isoelectric focusing of the enzyme in polyacrylamide gel revealed 5 major enzyme components. Results of amino acid analyses indicated that the enzyme had a low content of sulfur-containing amino acids and a relatively high content of dicarboxylic amino acids. The availability of this purification will be useful for the development of immunological methods for detections and quantitation of this enzyme in specimens from cancer patients.

Amine Oxidase (Copper-Containing)↗
PubMed1978

Calcitonin and histaminase in C-cell hyperplasia and medullary thyroid carcinoma. A light microscopic and immunohistochemical study.

The thyroid glands of 13 patients with gross medullary thyroid carcinoma (4 sporadic, 9 familial), 3 patients with clinically occult microscopic carcinoma, and 5 patients with C-cell hyperplasia have been studied using routine light microscopy and immunohistochemical techniques. The morphologic features of the spectrum of C-cell proliferative lesions are reviewed, and the distribution of calcitonin and histaminase in these lesions is compared. Calcitonin production is a property of normal, hyperplastic, and neoplastic C cells, and the hormone is present in the majority of tumor cells in medullary carcinoma. In contrast, histaminase is shown to be present only in some cells in medullary carcinoma and not in normal or hyperplastic C cells. We believe that the presence of histaminase in a C-cell proliferative lesion is an atypical phenomenon and indicative of malignancy.

Adolescent↗
PubMed1977

Combined decrease of postheparin-diamine oxidase (histaminase) and postheparin-lipoproteinlipase in inflammatory diseases.

Diamine oxidase (DAO, histaminase), according to Schayer, is an essential enzyme in histamine metabolism. It metabolises also a variety of diamines such as putrescine and cadaverine and is generally accepted to be identical with histaminase. Lipoproteinlipase (LL) is assumed to play an essential role in lipid metabolism. In vertebrates, parenterally applied heparin causes a marked dose-dependent rise of the plasma level of both enzymes mainly due to the release from the enzyme containing organs. The plasmatic level changes of DAO and LL after heparin application (200 U/kg b.wt., i.v.) have been studied in 30 patients suffering from 20 different, predominantly inflammatory diseases. In all cases the release of postheparin diamine oxidase (PHD) and of post-heparin lipoproteinlipase (PHLA) was found to be markedly decreased. There existed a highly significant correlation between the degree of the release of both enzymes (r=0.843, p less than 0.0005). In all patients normal levels of plasma insulin were detected. No correlation was found between PHLA and plasma triglycerides levels. Decrease of PHD respectively PHLA was a more sensitive biochemical parameter than were changes of serum glutamic pyruvic transaminase in acute hepatitis and of C reactive protein (CRP) in chronic inflammatory kidney diseases. This finding is most likely a general phenomenon in inflammatory diseases. Besides hormonal regulation inflammation-dependent effects on PHLA have to be discussed.

Adult↗
PubMed1977

Phosphopyridoxal complexes with histamine and histidine. (5) The kinetics of cyclic compound formation between histamine and pyridoxal-5'-phosphate in the presence of pig kidney diamine oxidase and rat intestinal histaminase.

Pig kidney diamine oxidase (DAO) and rat intestinal histaminase (Hi-ase) activities are inhibited in vitro by high concentrations of both a substrate (histamine) and a coenzyme (pyridoxal-5'-phosphate). This inhibition may be at least partially associated with the formation of a cyclic compound between histamine (Hi) and pyridoxal-5'-phosphate (PLP). The dynamics of this cyclic compound formation in the presence of both enzymes has been examined. In an incubation mixture containing partially purified pig kidney DAO, the rate of cyclization decreased slightly as compared with a buffer. On the contrary, in the presence of crude rat intestinal histaminase, the rate of cyclization was inhibited significantly; this inhibition was proportional to the amount of enzyme preparation present in the incubation mixture. The possible mechanism of the influence of enzyme protein on the rate of cyclic compound formation, and its possible biological significance, are discussed.

Amine Oxidase (Copper-Containing)↗
PubMed1975

Phosphopyridoxal complexes with histamine and histidine. (3) The influence of presumed complex on activity of rat intestinal histaminase.

Histamine in high concentration inhibits the rat intestinal histaminase (diamine oxidase E.C. 1.4.3.6.). The apparent Km is approximately 4.2 X 10(-5) M. This inhibition can be reversed by an addition of PLP. It was also found that excess of PLP inhibits enzyme activity. It is competitive inhibition. Histamine and other amines which were associated with enzyme inhibition form spectrophotometricaly demonstrable complex with PLP. The possible mechanism of the inhibitory action of PLP and complex with histamine and other amines on rat intestinal histaminase activity are discussed.

Amine Oxidase (Copper-Containing)↗
PubMed1997

The histaminase activity of rat white adipocytes.

OBJECTIVE AND DESIGN: Investigate the reaction conditions which allow the measurement of high affinity histamine oxidation. MATERIAL: Isolated rat white adipocytes. METHODS: The histaminase activity of rat white adipocytes and its inhibition by B24 and MDL 72274 was measured fluorimetrically or radiochemically in different experimental conditions. RESULTS: Histamine oxidation by rat white adipocytes is enhanced by elevated pH and by the presence of bicarbonate ions. Under these conditions the oxidative deamination of histamine by white adipocytes, becomes comparable to that of other histaminases, suggesting that this amine oxidase activity may play a role in the catabolism of histamine in vivo. The specific semicarbazide-sensitive amine oxidase (SSAO) inhibitors MDL 72274 and B24 inhibit the oxidation of both histamine and benzylamine by the adipocyte preparation. CONCLUSIONS: Although there are kinetic differences between the behaviour of these two amine substrates, these results would be consistent with a SSAO being responsible for both activities.

Adipocytes↗
PubMed2006

Histaminase PEGylation: preparation and characterization of a new bioconjugate for therapeutic application.

Copper amine oxidase catalyses the oxidative deamination of primary amino groups of several biogenic amines, one of which is histamine, the principal chemical mediator of the first phase of allergic reactions. Looking forward to a possible future therapeutic application of this enzyme in the field of histamine-mediated afflictions, we developed a simple method for the purification of a histaminase from grass pea shoots, a source particularly enriched with the enzyme. Furthermore, in order to improve its therapeutic potential, in particular to reduce the high impurity due to its heterologous source, we conjugated the protein with poly(ethylene glycol) and tested the molecular, immunogenic and pharmacokinetic properties of the native and modified forms. The PEGylated enzyme showed molecular and enzymatic properties similar to those of the unmodified one, but the PEGylation extended the permanence of the injected drug in the body and eliminated its high immunogenic behaviour. The considerable ease of native histaminase production as well as the improved properties after PEGylation, make this engineered plant enzyme a suitable drug candidate for alternative treatment of histamine-mediated affections.

Algorithms↗
PubMed1995

Histaminase activity in patients with vernal keratoconjunctivitis.

PURPOSE: To investigate the activity of histamine-degradating enzymes in tears and plasma of patients with vernal keratoconjunctivitis (VKC). METHOD: Tear and plasma samples were collected from patients with VKC and from age-matched control subjects. Histamine was measured by enzyme-linked immunosorbent assay in acid samples treated with perchloric to deactivate histaminase and in untreated samples. Tear cytology, skin test reactivity to histamine, and the sum clinical score of allergic signs and symptoms in patients with VKC also were evaluated. Nineteen patients with active VKC and six age-matched control subjects participated in this study. RESULTS: In untreated samples, tear histamine (mean +/- standard error of the mean) was 11.15 +/- 2.16 ng/ml in patients with VKC and 0.855 +/- 0.225 ng/ml in control tears (P < 0.001). In treated samples, mean tear histamine was 22.25 +/- 4.17 ng/ml in patients with VKC versus 10.64 +/- 2.85 ng/ml in control subjects (not statistically different). The ratio of histamine in treated to untreated samples (indicating histaminase activity) was significantly lower in patients with VKC (2.30 +/- 0.263) than in control subjects (17.57 +/- 5.97; P = 0.0001). Plasma histamine levels in untreated and treated samples were significantly higher in patients with VKC (untreated, 2.23 +/- 0.334 ng/ml; treated, 4.37 +/- 0.357 ng/ml) than in control subjects (untreated, 0.254 +/- 0.068, P = 0.0002; treated, 2.96 +/- 0.171 ng/ml, P = 0.0082). The enzymatic breakdown of histamine (treated/ untreated) in plasma was significantly decreased in patients with VKC (2.54 +/- 0.447) compared with control subjects (14.78 +/- 4.86; P = 0.0012). Skin reactivity to histamine was not increased in VKC. Tear histamine levels were significantly correlated to tear lymphocyte content in the general population and to tear basophils in the patients with tarsal-vernal VKC only. An increased number of tear eosinophils were correlated with elevated enzyme activity only in patients with tarsal-vernal VKC and to the clinical score only in limbal-vernal patients. CONCLUSION: The enzymatic degradation of histamine was significantly decreased in patients with VKC compared with control subjects in both tears and plasma, suggesting that this dysfunction may be a primary factor in the pathophysiology of VKC.

Adolescent↗
PubMed1978

Variable content of histaminase, L-dopa decarboxylase and calcitonin in small-cell carcinoma of the lung. Biologic and clinical implications.

To ascertain whether the content of endocrine markers is constant in small-cell carcinoma of the lung, levels of three markers of medullary thyroid carcinoma were studied in this tumor. Histaminase was increased in six of six primary tumors (three to 14,000 times), L-dopa decarboxylase in four of six (six to 30 times), and calcitonin in one of one (eight times) over levels in adjacent lung. Marker levels in mediastinal metastases reflected those in primary tumors in four of five patients. However, in four of seven, multiple hepatic metastases contained low to absent levels despite simultaneously high values in chest lesions. Immunohistochemical studies of histaminase revealed that within each primary tumor different cells contained different amounts of the enzyme. Since marker content varied between tumor cells, between primary tumors and between metastases in individual patients we conclude that circulating levels of these three markers cannot be expected necessarily to mirror tumor burden in patients with small-cell lung tumors.

APUD Cells↗
PubMed1978

Small cell carcinoma of the lung: serum calcitonin and serum histaminase (diamine oxidase) at basal levels and stimulated by pentagastrin.

Investigations were performed to evaluate the incidence of increased serum calcitonin and histaminase in 79 patients with untreated small cell carcinoma of the lung (SSC). In addition, serum calcitonin was measured following pentagastrin stimulation in 19 of these patients. Serum calcitonin was elevated in 54 of 79 patients (68%), 20 patients (25%) having a level usually associated with the diagnosis of medullary carcinoma of the thyroid (MCT). The levels of histaminase, on the other hand, did not differ from the distribution in normals. In three of 19 patients undergoing the pentagastrin stimulation test, calcitonin was significantly increased. Thus, serum calcitonin is frequently elevated in patients with SCC and a positive pentagastrin test is not pathognomonic of MCT.

Amine Oxidase (Copper-Containing)↗
PubMed1979

Complement-dependent histaminase release from human granulocytes.

The role of particle-bound complement proteins in the induction of noncytotoxic enzyme release from human granulocytes was investigated with the use of sera genetically deficient in complement and highly purified complement components. Release of histaminase, one of two important histamine catabolizing enzymes, and beta-glucuronidase from polymorphonuclear leukocytes was solely dependent on particle-bound C3b (the larger cleavage product of the third component of complement) when fluid-phase complement was excluded. The extent of enzyme release was a function of particle-bound C3b input, was reduced by exposing the particles to C3b inactivator, and was blocked by fluid-phase C3b. Phagocytosis of the C3b-coated particles was not required for enzyme release from neutrophils. In contrast, phagocytosis of "opsonized" particles was required for noncytotoxic release of histaminase and arylsulfatase from eosinophils; other proteins, as well as C3b, were able to opsonize particles for induction of enzyme release from eosinophils. These studies suggest a dual role for complement (particularly C3) in modulating vascular permeability phenomena, i.e., release of vasoactive mediators by the action of C3a and C5a, and release of the corresponding enzymes that inactivate the mediators by C3b.

Amine Oxidase (Copper-Containing)↗
PubMed1989

Spectrophotometric kinetic studies and substrate inhibition of hog kidney histaminase activity by an improved 2,4-dinitrophenylhydrazine method.

We improved the experimental procedure for the measurement of hog kidney histaminase activity using histamine as a substrate on the basis of a spectrophotometric estimation of the 2,4-dinitrophenylhydrazone of imidazole acetaldehyde and studied the steady-state kinetics to obtain the basic data for further investigations of the oxidative deamination of histamine. The initial and mean velocities of the enzymatic reaction were calculated and plotted against the amount of enzyme. It was found that the initial velocity increased linearly. The time t alpha necessary to reach the extent of reaction alpha was calculated and plotted against the reciprocal of the enzyme concentration eO. It was found that t alpha was linearly proportional to 1/eO. From Lineweaver-Burk plots, inhibition by high concentration of substrate was evident, and the v-pS curve was bell-shaped, with a pS maximum at 3.2. Km and V were obtained: Km = 7.7 x 10(-5) M, V = 0.0026 mumol/min (0.00075 mumol/min/mg protein). It was concluded that our DNP method was useful for the measurement of hog kidney histaminase activity using histamine as a substrate, basic steady-state kinetic studies and further investigations of substrate inhibition and inhibitory effect.

Amine Oxidase (Copper-Containing)↗
PubMedDate not supplied

Blood histaminase in phlyctenulosis.

Blood Histaminase estimations were done in 42 cases of phlyctenulosis and 25 normal subjects. Significantly higher level of blood Histaminase was found in patients of phlyctenulosis, which may be a consequence of its induction secondary to increased release of histamine in the early phase of disease.

Amine Oxidase (Copper-Containing)↗
PubMed1977

The effect of Escherichia coli endotoxin on plasma histaminase activity in the domestic fowl and the involvement of caeruloplasmin.

The injection of four-to nine-week-old fowls with Escherichia coli O111:B4 endotoxin (0-1 and 1-0 mg/kg) produced a two to eight fold rise in the histaminase activity of the plasma 24 h afterwards. In some cases this increase was still detectable after 48 h. This activity was strongly correlated with the p-phenylenediamine oxidase activity of caeruloplasmin. Electrophoretic studies with 7-5 per cent polyacrylamide gels indicated that fowl caeruloplasmin also was histaminase and putrescinase activity and that the release of this protein from the liver by endotoxin is largely responsible for the increase in the activity of the plasma. In untreated fowls this activity was lower than published values for several mammals and does not explain the relative resistance of the fowl to the acute effects of endotoxins and large doses of histamine.

Amine Oxidase (Copper-Containing)↗
PubMed1977

Determination of histaminase (diamine oxidase) activity by o-dianisidine test: interference of ceruloplasmin.

Until now o-dianisidine was used as an indicator substance in a test system for the determination of diamine oxidase. More recently, however, this substance was also used to measure ceruloplasmin activity. A study of the test principles revealed that o-dianisidine was the one denominator for both enzymes. As it was found for diamine oxidase the indicator was oxidized via peroxidase mediated H2O2 cleavage. Ceruloplasmin, however, oxidized o-dianisidine directly with resulting free radical formation. An addition of histamine dihydrochloride or putrescine dihydrochloride to an incubation mixture, containing ceruloplasmin as enzyme and o-dianisidine or p-phenylene-diamine as substrates, produced an activation of the enzyme, being more than 10-fold in the presence of 1 X 10(-2) M putrescine at pH 7.0. It was assumed that an allosteric effect of the dihydrochloride component might be responsible for this activation. When the activity of purified diamine oxidase was determined by the o-dianisidine test and by the isotope assay, a very good correlation between both methods was found. But, in a mixture of diamine oxidase and ceruloplasmin, no differentiation between the two enzymic activities by the o-dianisidine test was possible. This observation demonstrated an interference of ceruloplasmin when the o-dianisidine method was used for the determination of diamine oxidase activity. To apply our findings also in vivo the amine oxidase activity increasing in guinea-pig plasma during inflammation, was determined by the o-dianisidine test and by specific methods for some amine oxidase. Despite an enhanced oxidation of the o-dianisidine observed, only an increase of ceruloplasmin activity was found. It was concluded that ceruloplasmin had no 'histaminase activity' as has been assumed by other authors using the o-dianisidine test.

Amine Oxidase (Copper-Containing)↗
PubMed1981

Effect of intrapulmonary heparin on plasma diamine oxidase (histaminase) activity in mice.

Heparin releases diamine oxidase (DAO, histaminase) from binding sites in the intestinal vasculature. Histamine is involved in a number of pathological lesions. In this study we have examined the effect of intrapulmonary administration of heparin on plasma DAO activity in mice. For comparative purposes the same parameter was measured following the administration of an intravenous heparin regimen. The time course and dose-response were examined with the two heparin regimens. The doses of heparin were based on appropriate clinical equivalents. Both heparin regimens showed a dose dependent response (correlation coefficient r = 0.9). The dose of intrapulmonary heparin (10 mg/kg) was 12 times greater than the dose injected intravenously but the DAO response lasted 48 times longer that that obtained from the intravenous heparin regimen.

Amine Oxidase (Copper-Containing)↗
PubMed1992

Histaminase activity in rat lung and its comparison with intestinal mucosal diamine oxidase.

In rat lung microsomes, an enzyme showing high histaminase activity is present. The oxidation of histamine is dependent on the presence of two enzymic activities, both inhibited by alpha-aminoguanidine and by B24, an inhibitor of semicarbazide-sensitive amine oxidases (SSAO) which have benzylamine as preferential substrate. These enzymic activities differ in substrate specificity: one appears to be a classical tissue bound SSAO enzyme with high affinity for benzylamine, the other a diamine oxidase (DAO) with properties that are very different from the classical DAO. This latter enzyme is not inhibition by high histamine concentrations and is more active at pH 8.5 than at pH 7.4.

Amine Oxidase (Copper-Containing)↗