Increased primary amine oxidase expression and activity in white adipose tissue of obese and diabetic db−/− mice

2011 ◽  
Vol 118 (7) ◽  
pp. 1071-1077 ◽  
Author(s):  
Zsuzsa Iffiú-Soltész ◽  
Josep Mercader ◽  
Danielle Daviaud ◽  
Jérémie Boucher ◽  
Christian Carpéné
Keyword(s):  
Adipose Tissue ◽  
White Adipose Tissue ◽  
Primary Amine ◽  
Amine Oxidase ◽  
Primary Amine Oxidase ◽  
Expression And Activity

scholarly journals Dietary Phenolic Compounds Interfere with the Fate of Hydrogen Peroxide in Human Adipose Tissue but Do Not Directly Inhibit Primary Amine Oxidase Activity

2016 ◽  
Vol 2016 ◽  
pp. 1-15 ◽  
Author(s):  
Christian Carpéné ◽  
Mounia Hasnaoui ◽  
Balázs Balogh ◽  
Peter Matyus ◽  
Alfredo Fernández-Quintela ◽  
...  
Keyword(s):  
Adipose Tissue ◽  
Phenolic Compounds ◽  
Primary Amine ◽  
Amine Oxidase ◽  
Human Adipose Tissue ◽  
3D Models ◽  
Fluorescent Detection ◽  
Computational Docking ◽  
Amine Oxidation ◽  
Primary Amine Oxidase

Resveratrol has been reported to inhibit monoamine oxidases (MAO). Many substrates or inhibitors of neuronal MAO interact also with other amine oxidases (AO) in peripheral organs, such as semicarbazide-sensitive AO (SSAO), known as primary amine oxidase, absent in neurones, but abundant in adipocytes. We asked whether phenolic compounds (resveratrol, pterostilbene, quercetin, and caffeic acid) behave as MAO and SSAO inhibitors. AO activity was determined in human adipose tissue. Computational docking and glucose uptake assays were performed in 3D models of human AO proteins and in adipocytes, respectively. Phenolic compounds fully inhibited the fluorescent detection of H2O2generated during MAO and SSAO activation by tyramine and benzylamine. They also quenched H2O2-induced fluorescence in absence of biological material and were unable to abolish the oxidation of radiolabelled tyramine and benzylamine. Thus, phenolic compounds hampered H2O2detection but did not block AO activity. Only resveratrol and quercetin partially impaired MAO-dependent [14C]-tyramine oxidation and behaved as MAO inhibitors. Phenolic compounds counteracted the H2O2-dependent benzylamine-stimulated glucose transport. This indicates that various phenolic compounds block downstream effects of H2O2produced by biogenic or exogenous amine oxidation without directly inhibiting AO. Phenolic compounds remain of interest regarding their capacity to limit oxidative stress rather than inhibiting AO.

scholarly journals Methylxanthines Inhibit Primary Amine Oxidase and Monoamine Oxidase Activities of Human Adipose Tissue

Medicines ◽  
2020 ◽  
Vol 7 (4) ◽  
pp. 18
Author(s):  
Wiem Haj Ahmed ◽  
Cécile Peiro ◽  
Jessica Fontaine ◽  
Barry J. Ryan ◽  
Gemma K. Kinsella ◽  
...  
Keyword(s):  
Adipose Tissue ◽  
Monoamine Oxidase ◽  
Primary Amine ◽  
Amine Oxidase ◽  
Fluorimetric Determination ◽  
Amine Oxidation ◽  
Direct Demonstration ◽  
Primary Amine Oxidase ◽  
Anti Inflammatory ◽  
Subcutaneous Adipose

Background: Methylxanthines including caffeine and theobromine are widely consumed compounds and were recently shown to interact with bovine copper-containing amine oxidase. To the best of our knowledge, no direct demonstration of any interplay between these phytochemicals and human primary amine oxidase (PrAO) has been reported to date. We took advantage of the coexistence of PrAO and monoamine oxidase (MAO) activities in human subcutaneous adipose tissue (hScAT) to test the interaction between several methylxanthines and these enzymes, which are involved in many key pathophysiological processes. Methods: Benzylamine, methylamine, and tyramine were used as substrates for PrAO and MAO in homogenates of subcutaneous adipose depots obtained from overweight women undergoing plastic surgery. Methylxanthines were tested as substrates or inhibitors by fluorimetric determination of hydrogen peroxide, an end-product of amine oxidation. Results: Semicarbazide-sensitive PrAO activity was inhibited by theobromine, caffeine, and isobutylmethylxanthine (IBMX) while theophylline, paraxanthine, and 7-methylxanthine had little effect. Theobromine inhibited PrAO activity by 54% at 2.5 mM. Overall, the relationship between methylxanthine structure and the degree of inhibition was similar to that seen with bovine PrAO, although higher concentrations (mM) were required for inhibition. Theobromine also inhibited oxidation of tyramine by MAO, at the limits of its solubility in a DMSO vehicle. At doses higher than 12 % v/v, DMSO impaired MAO activity. MAO was also inhibited by millimolar doses of IBMX, caffeine and by other methylxanthines to a lesser extent. Conclusions: This preclinical study extrapolates previous findings with bovine PrAO to human tissues. Given that PrAO is a potential target for anti-inflammatory drugs, it indicates that alongside phosphodiesterase inhibition and adenosine receptor antagonism, PrAO and MAO inhibition could contribute to the health benefits of methylxanthines, especially their anti-inflammatory effects.

Identification of Two Imidazole Binding Sites and Key Residues for Substrate Specificity in Human Primary Amine Oxidase AOC3

Biochemistry ◽  
2011 ◽  
Vol 50 (24) ◽  
pp. 5507-5520 ◽  
Author(s):  
Heli Elovaara ◽  
Heidi Kidron ◽  
Vimal Parkash ◽  
Yvonne Nymalm ◽  
Eva Bligt ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Binding Sites ◽  
Primary Amine ◽  
Amine Oxidase ◽  
Primary Amine Oxidase ◽  
Key Residues

scholarly journals Dietary phytochemicals as inhibitors of primary amine oxidase

2017 ◽  
Vol 256 ◽  
pp. S96-S97
Author(s):  
Padraig Shanahan ◽  
Jeff O'sullivan ◽  
Keith F. Tipton ◽  
Gemma Kinsella ◽  
Barry Ryan ◽  
...  
Keyword(s):  
Primary Amine ◽  
Amine Oxidase ◽  
Dietary Phytochemicals ◽  
Primary Amine Oxidase

scholarly journals Primary Amine Oxidase of Escherichia coli Is a Metabolic Enzyme that Can Use a Human Leukocyte Molecule as a Substrate

PLoS ONE ◽  
2015 ◽  
Vol 10 (11) ◽  
pp. e0142367 ◽  
Author(s):  
Heli Elovaara ◽  
Teija Huusko ◽  
Mikael Maksimow ◽  
Kati Elima ◽  
Gennady G. Yegutkin ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Primary Amine ◽  
Amine Oxidase ◽  
Human Leukocyte ◽  
Metabolic Enzyme ◽  
Primary Amine Oxidase

Increased monoamine oxidase and semicarbazide-sensitive amine oxidase activities in white adipose tissue of obese dogs fed a high-fat diet

2006 ◽  
Vol 62 (2) ◽  
pp. 113-123 ◽  
Author(s):  
E. Wanecq ◽  
S. Bour ◽  
P. Verwaerde ◽  
F. Smih ◽  
P. Valet ◽  
...  
Keyword(s):  
Adipose Tissue ◽  
Monoamine Oxidase ◽  
White Adipose Tissue ◽  
High Fat Diet ◽  
Amine Oxidase ◽  
High Fat
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