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

1981 ◽  
Vol 11 (4) ◽  
pp. 335-338 ◽  
Author(s):  
J. Mahadoo ◽  
C. J. Wright ◽  
L. B. Jaques
Keyword(s):  
Diamine Oxidase ◽  
Histaminase Activity

Temporary suppression of diamine oxidase (histaminase) activity by cysteamine

1962 ◽  
Vol 11 (7) ◽  
pp. 509-514 ◽  
Author(s):  
C. De Marco ◽  
B. Mondoví ◽  
D. Cavallini
Keyword(s):  
Diamine Oxidase ◽  
Histaminase Activity

scholarly journals Vegetal diamine oxidase alleviates histamine-induced contraction of colonic muscles

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Armelle Tchoumi Neree ◽  
Rodolphe Soret ◽  
Lucia Marcocci ◽  
Paola Pietrangeli ◽  
Nicolas Pilon ◽  
...  
Keyword(s):  
Diamine Oxidase ◽  
Therapeutic Potential ◽  
Ex Vivo ◽  
Active Form ◽  
Distal Colon ◽  
Biologically Active ◽  
In Vitro Assays ◽  
Histaminase Activity ◽  
Irritable Bowel

AbstractExcess of histamine in gut lumen generates a pronounced gastrointestinal discomfort, which may include diarrhea and peristalsis dysfunctions. Deleterious effects of histamine can be alleviated with antihistamine drugs targeting histamine receptors. However, many antihistamine agents come with various undesirable side effects. Vegetal diamine oxidase (vDAO) might be a relevant alternative owing to its histaminase activity. Mammalian intestinal mucosa contains an endogenous DAO, yet possessing lower activity compared to that of vDAO preparation. Moreover, in several pathological conditions such as inflammatory bowel disease and irritable bowel syndrome, this endogenous DAO enzyme can be lost or inactivated. Here, we tested the therapeutic potential of vDAO by focusing on the well-known effect of histamine on gut motility. Using ex vivo and in vitro assays, we found that vDAO is more potent than commercial anti-histamine drugs at inhibiting histamine-induced contraction of murine distal colon muscles. We also identified pyridoxal 5′-phosphate (the biologically active form of vitamin B6) as an effective enhancer of vDAO antispasmodic activity. Furthermore, we discovered that rectally administered vDAO can be retained on gut mucosa and remain active. These observations make administration of vDAO in the gut lumen a valid alternative treatment for histamine-induced intestinal dysfunctions.

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

1992 ◽  
Vol 35 (3-4) ◽  
pp. 192-199 ◽  
Author(s):  
G. Ignesti ◽  
G. Banchelli ◽  
L. Raimondi ◽  
R. Pirisino ◽  
F. Buffoni
Keyword(s):  
Diamine Oxidase ◽  
Rat Lung ◽  
Histaminase Activity

Determination of diamine oxidase (histaminase) activity. An interference of aldehyde metabolizing enzymes

1978 ◽  
Vol 8 (4) ◽  
pp. 388-389 ◽  
Author(s):  
A. Fogel ◽  
T. Biegański ◽  
J. Wozniak ◽  
Cz. Máslinski
Keyword(s):  
Diamine Oxidase ◽  
Metabolizing Enzymes ◽  
Histaminase Activity

Interference of aldehyde metabolizing enzymes with diamine oxidase/histaminase/activity as determined by 14C putrescine method

1978 ◽  
Vol 27 (8) ◽  
pp. 1159-1162 ◽  
Author(s):  
Wieslawa Agnieszka Fogel ◽  
Tadeusz Biegański ◽  
Janina Woz'niak ◽  
Czeslaw Maśliński
Keyword(s):  
Diamine Oxidase ◽  
Metabolizing Enzymes ◽  
Histaminase Activity

scholarly journals DETERMINATION OF HISTAMINASE ACTIVITY IN HISTOLOGIC SAMPLES AND ITS QUANTITATIVE DISTRIBUTION IN INTACT HUMAN PLACENTA AND UTERUS

1967 ◽  
Vol 15 (8) ◽  
pp. 431-435 ◽  
Author(s):  
RONALD E. GUNTHER ◽  
DAVID GLICK
Keyword(s):  
Human Placenta ◽  
Diamine Oxidase ◽  
Enzymatic Oxidation ◽  
Optimal Conditions ◽  
Rat Stomach ◽  
Stomach Mucosa ◽  
Tissue Sections ◽  
Peritoneal Mast Cells ◽  
Histaminase Activity

The spectrophotometric method for determination of histaminase, based on measurement of the hydrogen peroxide formed by the enzymatic oxidation of histamine, was modified and adapted to studies on microliter volumes of tissue (placenta) homogenates and microtome sections of tissue (human uterus and attached intact placenta at term). Optimal conditions for these assays were established. From analyses of tissue sections, peak enzyme activities were observed in the decidua, thus supporting the concept that this tissue is a significant source of the increased enzyme in blood plasma during pregnancy in the human. Inhibitor studies with aminoguanidine sulfate showed that the histaminase investigated in the human placenta was diamine oxidase. No histaminase activity was detected in isolated peritoneal mast cells from the rat or in homogenates of rat stomach mucosa.

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