The Experts below are selected from a list of 96 Experts worldwide ranked by ideXlab platform
Lloyd R Sutherland - One of the best experts on this subject based on the ideXlab platform.
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intestinal permeability and postheparin plasma Diamine Oxidase activity in the prediction of crohn s disease relapse
Inflammatory Bowel Diseases, 1999Co-Authors: Robert J Hilsden, Jon Meddings, James A Hardin, Grant D Gall, Lloyd R SutherlandAbstract:A method of detecting presymptomatic relapse of Crohn's disease could allow for the selective use of maintenance or intensified medical therapy in those with an increased risk of relapse. The aim of this study was to evaluate three potential laboratory markers of relapse: intestinal and gastroduodenal permeability and plasma Diamine Oxidase activity. Intestinal permeability (lactulose/mannitol test), gastroduodenal permeability (urinary sucrose excretion), and postheparin plasma Diamine Oxidase activity were serially measured in 61 adults with Crohn's disease in remission (CDAI 150 and increased by at least 100 points or the need for steroids or surgery). Fourteen patients (23%) relapsed. A cut-off of 0.030 for the lactulose/mannitol ratio was defined. Those with ratios above the cutoff had a 7.0 times greater risk of relapse (p < 0.001). Three subjects who went from a normal ratio to an abnormal ratio relapsed, whereas none of 32 subjects with a repeatedly normal ratio relapsed. Sucrose excretion and plasma Diamine Oxidase activity did not predict relapse. Serial testing of intestinal permeability, but not of gastroduodenal permeability or plasma Diamine Oxidase activity, was useful in predicting relapse in asymptomatic patients.
Kanji Kawachi - One of the best experts on this subject based on the ideXlab platform.
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Localization and changes of Diamine Oxidase during cardiopulmonary bypass in rabbits.
The Journal of surgical research, 2005Co-Authors: Nobuo Tsunooka, Kazutaka Maeyama, Hiromichi Nakagawa, Takashi Doi, Atsushi Horiuchi, Katsutoshi Miyauchi, Yuji Watanabe, Hiroshi Imagawa, Kanji KawachiAbstract:Background We previously observed increased serum Diamine Oxidase activity during clinical cardiopulmonary bypass, indicating small intestinal mucosal ischemia followed by bacterial translocation. Materials and methods In seven female rabbits undergoing cardiopulmonary bypass for 1 h, we analyzed the localization of Diamine Oxidase immunohistochemically, and measured its activity in serum and abdominal organs before and after cardiopulmonary bypass (CPB). Results Preoperatively, Diamine Oxidase activity and immunoreactivity were high in the small intestine, localized to villus tips. Serum activity increased significantly after CPB, whereas small intestinal Diamine Oxidase decreased with mucosal injury. Conclusions In this model serum Diamine Oxidase activity appeared to reflect CPB induced intestinal mucosal injury.
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bacterial translocation secondary to small intestinal mucosal ischemia during cardiopulmonary bypass measurement by Diamine Oxidase and peptidoglycan
European Journal of Cardio-Thoracic Surgery, 2004Co-Authors: Nobuo Tsunooka, Kazutaka Maeyama, Yuji Watanabe, Hiroshi Imagawa, Yoshihiro Hamada, Shinji Takano, Kanji KawachiAbstract:Objective: To demonstrate that small intestinal mucosal ischemia occurs during cardiopulmonary bypass by measuring serum Diamine Oxidase activity, an index of small intestinal mucosal ischemia, in perioerative patients undergoing cardiovascular surgery with and without cardiopulmonary bypass. Methods: Twelve successive patients who underwent coronary artery bypass grafting with cardiopulmonary bypass (Group I) were compared to 10 patients who underwent off-pump coronary artery bypass grafting (Group II). Serum Diamine Oxidase activity, blood lactate concentration, and serum peptidoglycan concentration were measured perioperatively. Results: Serum Diamine Oxidase activity rose after the start of cardiopulmonary bypass and continued to rise throughout cardiopulmonary bypass in Group I, while activity was unchanged in Group II. The serum lactate concentration mirrored the change in the Diamine Oxidase activity in both groups. The peptidoglycan concentration in Group I rose after the start of cardiopulmonary bypass and returned to near normal concentrations after surgery. Conclusions: The parallel rise in Diamine Oxidase activity and the serum lactate concentration in Group I implies that ischemic injury to the mucosa of the small intestine occurs during cardiopulmonary bypass, and the rise in the serum peptidoglycan concentration indicates that bacteremia did occur. Thus, cardiopulmonary bypass causes hypoperfusion of small intestinal mucosa and consequently bacterial translocation. q 2003 Elsevier B.V. All rights reserved.
Alessandro Finazzi Agro - One of the best experts on this subject based on the ideXlab platform.
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Copper reduction by substrate in Diamine Oxidase
FEBS Letters, 2001Co-Authors: Bruno Mondovi, Giuseppe Rotilio, Alessandro Finazzi Agro, Maria Paola Vallogini, Bo G. Malmström, Eraldo AntoniniAbstract:Pig kidney Diamine Oxidase (Diamine: oxygen oxidoreductase, EC 1.4.3.6) similarly to other amine Oxidases [ 1,2] , contains cupric copper and pyridoxal phosphate [3-61. The copper content of pig kidney Diamine Oxidase.is 1 g atom of metal per 90,000 g of protein. All the chemically determined copper can be accounted for by the electron paramagnetic resonance (EPR) spectra of the enzyme. The function of copper in these enzymes is not yet clear. Cupric copper restores the activity of copper-free Diamine Oxidase from pea seedlings [7] , of bovine plasma amine Oxidase [l] and of pig kidney Diamine Oxidase [3]. However, no reduction of copper has been observed by EPR spectra of these enzymes [3,5,6,8]. In the case of pig kidney Diamine Oxidase, although no valence change of copper after addition of excess substrate in the absence of oxygen was observed, changes which were specific for each individual substrate were demonstrated in the EPR spectrum. A direct binding between substrate and copper was not evident [3]. In this communication, we report evidence for reduction of copper in Diamine Oxidase in the presence of substrate.
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Activity and expression of Diamine Oxidase in lentil seedling under different growth conditions
Plant Science, 1991Co-Authors: Mauro Maccarrone, Antonello Rossi, L Avigliano, Alessandro Finazzi AgroAbstract:The activity and expression of Diamine Oxidase during the germination of lentil seeds and in the course of anoxic and thermal stress have been studied. Diamine Oxidase activity, as well as the seedlings growth rate, was found to be markedly higher in dark-grown lentil seedlings than in the light-grown ones. The same was true for the respective protein and mRNA amounts. The specific activity of Diamine Oxidase was decreased by anoxic stress and not affected by thermal stress. The possible physiological meaning of these findings is discussed.
Robert J Hilsden - One of the best experts on this subject based on the ideXlab platform.
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intestinal permeability and postheparin plasma Diamine Oxidase activity in the prediction of crohn s disease relapse
Inflammatory Bowel Diseases, 1999Co-Authors: Robert J Hilsden, Jon Meddings, James A Hardin, Grant D Gall, Lloyd R SutherlandAbstract:A method of detecting presymptomatic relapse of Crohn's disease could allow for the selective use of maintenance or intensified medical therapy in those with an increased risk of relapse. The aim of this study was to evaluate three potential laboratory markers of relapse: intestinal and gastroduodenal permeability and plasma Diamine Oxidase activity. Intestinal permeability (lactulose/mannitol test), gastroduodenal permeability (urinary sucrose excretion), and postheparin plasma Diamine Oxidase activity were serially measured in 61 adults with Crohn's disease in remission (CDAI 150 and increased by at least 100 points or the need for steroids or surgery). Fourteen patients (23%) relapsed. A cut-off of 0.030 for the lactulose/mannitol ratio was defined. Those with ratios above the cutoff had a 7.0 times greater risk of relapse (p < 0.001). Three subjects who went from a normal ratio to an abnormal ratio relapsed, whereas none of 32 subjects with a repeatedly normal ratio relapsed. Sucrose excretion and plasma Diamine Oxidase activity did not predict relapse. Serial testing of intestinal permeability, but not of gastroduodenal permeability or plasma Diamine Oxidase activity, was useful in predicting relapse in asymptomatic patients.
E. Bodner - One of the best experts on this subject based on the ideXlab platform.
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Purification and characterization of Diamine Oxidase from porcine kidney and intestine
Biochimica et biophysica acta, 1997Co-Authors: H. G. Schwelberger, E. BodnerAbstract:Diamine Oxidase, the enzyme catalyzing the oxidative deamination of histamine and other Diamines, was purified from porcine kidney and porcine intestine. During all purification steps the enzymes from both tissues showed identical binding and elution characteristics. The native enzymes are homodimeric glycoproteins with an apparent molecular weight of 186 kDa. Under reducing conditions the subunits migrate at 104 kDa on SDS polyacrylamide gels and the deglycosylated subunits migrate at 93 kDa which corresponds to a carbohydrate content of 11%. The native and deglycosylated forms of kidney and intestinal Diamine Oxidase migrate to the same positions, respectively, on two-dimensional isoelectric focussing/SDS polyacrylamide gels. The sequences of the 21 N-terminal amino acids of both proteins are identical. A polyclonal antibody raised against the kidney enzyme binds equally well to Diamine Oxidase from both kidney and intestine, inhibits the enzymatic activity, and precipitates all Diamine Oxidase activity from tissue homogenates. The kidney and intestinal enzymes have identical substrate specificities, efficiently converting aliphatic Diamines, histamine, and spermidine. For both enzymes the Km values for histamine, putrescine, and spermidine are 0.02 mM, 0.35 mM, and 3.3 mM, respectively. Spermine, aliphatic monoamines, and aromatic mono- and Diamines are poor substrates. In conclusion, the Diamine Oxidase proteins from porcine kidney and intestine are very likely identical and constitute the only Diamine Oxidase activity present in these tissues. The structural identity implies identical functions of the proteins in these organs, namely the protection of the organism against high concentrations of Diamines.
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Purification of human intestinal Diamine Oxidase
Inflammation Research, 1996Co-Authors: H. G. Schwelberger, J. Sattler, E. BodnerAbstract:Diamine Oxidase (DAO; EC 1.4.3.6) catalyzes the oxidative deamination of histamine and other biogenie amines [1]. In mammals, degradation by DAO is the major pathway ofhistamine inactivation in many organs, especially in the intestine where the highest activities of DAO have been reported [2]. Although DAO has been purified from various tissues, the intestinal enzyme has resisted satisfactory characterization due to its instability. In order to learn more ab out the function of DAO in the gastrointestinal tract, we purified Diamine Oxidase from porcine and human intestine.