scholarly journals Development of Amine-Oxidase-Based Biosensors for Spermine and Spermidine Analysis

2017 ◽  
pp. 75-80 ◽  
Author(s):  
Cristina Tortolini ◽  
Gabriele Favero ◽  
Franco Mazzei
Keyword(s):  
Amine Oxidase

Mitochondrial Oxidation of p-N, N-Dimethylamino-β-Phenethylamine (DAPA)

1975 ◽  
Vol 33 ◽  
pp. 458-459
Author(s):  
W. Allen Shannon ◽  
Hannah L. Wasserkrug ◽  
andArnold M. Seligman
Keyword(s):  
Guinea Pig ◽  
Oxidase Activity ◽  
Amine Oxidase ◽  
Histochemical Demonstration ◽  
Guinea Pig Heart ◽  
Pig Kidney ◽  
Cytoplasmic Vacuoles ◽  
Liver And Kidney ◽  
Mitochondrial Oxidation ◽  
Amine Oxidase Activity

The synthesis of a new substrate, p-N,N-dimethylamino-β-phenethylamine (DAPA)3 (Fig. 1) (1,2), and the testing of it as a possible substrate for tissue amine oxidase activity have resulted in the ultracytochemical localization of enzyme oxidase activity referred to as DAPA oxidase (DAPAO). DAPA was designed with the goal of providing an amine that would yield on oxidation a stronger reducing aldehyde than does tryptamine in the histochemical demonstration of monoamine oxidase (MAO) with tetrazolium salts.Ultracytochemical preparations of guinea pig heart, liver and kidney and rat heart and liver were studied. Guinea pig kidney, known to exhibit high levels of MAO, appeared the most reactive of the tissues studied. DAPAO reaction product appears primarily in mitochondrial outer compartments and cristae (Figs. 2-4). Reaction product is also localized in endoplasmic reticulum, cytoplasmic vacuoles and nuclear envelopes (Figs. 2 and 3) and in the sarcoplasmic reticulum of heart.

IRREVERSIBLE AFFINITY IMMOBILIZATION OF LENTIL SEEDLING AMINE OXIDASE WITH ACTIVITY RETENTION

2007 ◽  
Vol 6 (1) ◽  
pp. 31-35 ◽  
Author(s):  
Enrico Sanjust ◽  
Francesca Sollai ◽  
Barbara Noli ◽  
Giovanni Floris
Keyword(s):  
Amine Oxidase ◽  
Affinity Immobilization ◽  
Lentil Seedling

FRI-314-A novel semicarbazide-sensitive amine oxidase inhibitor, TERN-201, reduces NAS and fibrosis in rodent models of non-alcoholic steatohepatitis

2019 ◽  
Vol 70 (1) ◽  
pp. e534-e535
Author(s):  
Kevin Klucher ◽  
Yujin Wang ◽  
Yingzi Xu ◽  
Randall Halcomb ◽  
Martijn Fenaux
Keyword(s):  
Amine Oxidase ◽  
Oxidase Inhibitor ◽  
Rodent Models ◽  
Alcoholic Steatohepatitis

scholarly journals DEER and RIDME Measurements of the Nitroxide-Spin Labelled Copper-Bound Amine Oxidase Homodimer from Arthrobacter Globiformis

2021 ◽  
Author(s):  
Hannah Russell ◽  
Rachel Stewart ◽  
Christopher Prior ◽  
Vasily S. Oganesyan ◽  
Thembaninkosi G. Gaule ◽  
...  
Keyword(s):  
Dipolar Coupling ◽  
Amine Oxidase ◽  
Spin Labels ◽  
Arthrobacter Globiformis ◽  
Copper Amine Oxidase ◽  
Dipole Interactions ◽  
Nitroxide Spin Labels ◽  
Double Electron Electron Resonance ◽  
Dipolar Modulation ◽  
Paramagnetic Centres

AbstractIn the study of biological structures, pulse dipolar spectroscopy (PDS) is used to elucidate spin–spin distances at nanometre-scale by measuring dipole–dipole interactions between paramagnetic centres. The PDS methods of Double Electron Electron Resonance (DEER) and Relaxation Induced Dipolar Modulation Enhancement (RIDME) are employed, and their results compared, for the measurement of the dipolar coupling between nitroxide spin labels and copper-II (Cu(II)) paramagnetic centres within the copper amine oxidase from Arthrobacter globiformis (AGAO). The distance distribution results obtained indicate that two distinct distances can be measured, with the longer of these at c.a. 5 nm. Conditions for optimising the RIDME experiment such that it may outperform DEER for these long distances are discussed. Modelling methods are used to show that the distances obtained after data analysis are consistent with the structure of AGAO.

scholarly journals THE INACTIVATION OF AMINE OXIDASE BY ENZYMATIC OXIDATIVE PRODUCTS OF CATECHOL AND ADRENALIN

1942 ◽  
Vol 146 (2) ◽  
pp. 411-419
Author(s):  
Jonas S. Friedenwald ◽  
Heinz Herrmann
Keyword(s):  
Amine Oxidase ◽  
Oxidative Products

scholarly journals SUBSTRATE SPECIFICITY OF AMINE OXIDASE

1943 ◽  
Vol 147 (3) ◽  
pp. 487-503 ◽  
Author(s):  
Gordon A. Alles ◽  
Erik V. Heegaard
Keyword(s):  
Substrate Specificity ◽  
Amine Oxidase

scholarly journals Novel Facet of an Old Dietary Molecule? Direct Influence of Caffeine on Glucose and Biogenic Amine Handling by Human Adipocytes

Molecules ◽  
2021 ◽  
Vol 26 (13) ◽  
pp. 3831
Author(s):  
Wiem Haj Ahmed ◽  
Nathalie Boulet ◽  
Anaïs Briot ◽  
Barry J. Ryan ◽  
Gemma K. Kinsella ◽  
...  
Keyword(s):  
Glucose Transport ◽  
Amine Oxidase ◽  
Human Adipose Tissue ◽  
Lipid Solubility ◽  
Human Adipocytes ◽  
Peripheral Tissues ◽  
Amine Oxidation ◽  
High Lipid ◽  
The Central Nervous System ◽  
High Lipid Solubility

Caffeine is a plant alkaloid present in food and beverages consumed worldwide. It has high lipid solubility with recognized actions in the central nervous system and in peripheral tissues, notably the adipose depots. However, the literature is scant regarding caffeine’s influence on adipocyte functions other than lipolysis, such as glucose incorporation into lipids (lipogenesis) and amine oxidation. The objective of this study was to explore the direct effects of caffeine and of isobutylmethylxanthine (IBMX) on these adipocyte functions. Glucose transport into fat cells freshly isolated from mice, rats, or humans was monitored by determining [3H]-2-deoxyglucose (2-DG) uptake, while the incorporation of radiolabeled glucose into cell lipids was used as an index of lipogenic activity. Oxidation of benzylamine by primary amine oxidase (PrAO) was inhibited by increasing doses of caffeine in human adipose tissue preparations with an inhibition constant (Ki) in the millimolar range. Caffeine inhibited basal and insulin-stimulated glucose transport as well as lipogenesis in rodent adipose cells. The antilipogenic action of caffeine was also observed in adipocytes from mice genetically invalidated for PrAO activity, indicating that PrAO activity was not required for lipogenesis inhibition. These caffeine inhibitory properties were extended to human adipocytes: relative to basal 2-DG uptake, set at 1.0 ± 0.2 for 6 individuals, 0.1 mM caffeine tended to reduce uptake to 0.83 ± 0.08. Insulin increased uptake by 3.86 ± 1.11 fold when tested alone at 100 nM, and by 3.21 ± 0.80 when combined with caffeine. Our results reinforce the recommendation of caffeine’s potential in the treatment or prevention of obesity complications.

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