Monoamine oxidase and semicarbazide-sensitive amine oxidase activities in bovine eye

1990 ◽  
pp. 327-330 ◽  
Author(s):  
A. Fernandez de Arriba ◽  
D. Balsa ◽  
K. F. Tipton ◽  
M. Unzeta
Keyword(s):  
Monoamine Oxidase ◽  
Amine Oxidase

scholarly journals Monoamine Oxidase and Semicarbazide-Sensitive Amine Oxidase Kinetic Analysis in Mesenteric Arteries of Patients With Type 2 Diabetes

2011 ◽  
pp. 309-315 ◽  
Author(s):  
S. F. NUNES ◽  
I. V. FIGUEIREDO ◽  
J. S. PEREIRA ◽  
E. T. DE LEMOS ◽  
F. REIS ◽  
...  
Keyword(s):  
Type 2 Diabetes ◽  
Monoamine Oxidase ◽  
Kinetic Parameters ◽  
Amine Oxidase ◽  
Mesenteric Arteries ◽  
Patient Age ◽  
Mao B ◽  
Mao A ◽  
Type 2 Diabetic

Monoamine oxidase (MAO, type A and B) and semicarbazide-sensitive amine oxidase (SSAO) metabolize biogenic amines, however, the impact of these enzymes in arteries from patients with type 2 diabetes remains poorly understood. We investigated the kinetic parameters of the enzymes to establish putative correlations with noradrenaline (NA) content and patient age in human mesenteric arteries from type 2 diabetic patients. The kinetic parameters were evaluated by radiochemical assay and NA content by high-performance liquid chromatography (HPLC). The activity of MAO-A and SSAO in type 2 diabetic vascular tissues was significantly lower compared to the activity obtained in non-diabetic tissues. In the correlation between MAO-A (Km) and NA content, we found a positive correlation for both the diabetic and non-diabetic group, but no correlation was established for patient age. In both groups, MAO-B (Vmax) showed a negative correlation with age. The results show that MAO-A and SSAO activities and NA content of type 2 diabetic tissues are lower compared to the non-diabetic tissues, while MAO-B activity remained unchanged. These remarks suggest that MAO-A and SSAO may play an important role in vascular tissue as well as in the vascular pathophysiology of type 2 diabetes.

A comparison of cardiac and vascular clorgyline-resistant amine oxidase and monoamine oxidase

1982 ◽  
Vol 31 (1) ◽  
pp. 27-35 ◽  
Author(s):  
David E. Clarke ◽  
Geoffrey A. Lyles ◽  
Brian A. Callingham
Keyword(s):  
Monoamine Oxidase ◽  
Amine Oxidase

scholarly journals Ultrastructural cytochemistry of p-N,N-dimethylamino-beta-phenethylamine (DAPA) oxidation reactions. "activation" and inhibition studies.

1976 ◽  
Vol 24 (3) ◽  
pp. 540-555 ◽  
Author(s):  
W A Shannon ◽  
H L Wasserkrug ◽  
A M Seligman
Keyword(s):  
Monoamine Oxidase ◽  
Diamine Oxidase ◽  
Amine Oxidase ◽  
The Other ◽  
Oxidation Reactions ◽  
Fixed Tissue ◽  
Tetrazolium Chloride ◽  
Ultrastructural Cytochemistry ◽  
Inhibition Studies ◽  
Reaction Media

The oxidation of p-N,N-dimethylamino-beta-phenethylamine (DAPA) by amine oxidase(s) (AO), i.e., diamine oxidase (DAO), monoamine oxidase (MAO) and/or possibly other oxidases, has been previously demonstrated. This study reports the results of variations in fixation procedures and the incorporation of a series of possible "activators" and inhibitors into the DAPA oxidase (DAPAO) and DAPAO-BSPT [2-(2'-benzothiazolyl)-5-styryl-3-(4'-phthalhydrazidyl) tetrazolium chloride] reaction media in an attempt to elucidate the oxidase(s) involved. Results of these studies are indicative of at least two different oxidases acting preferentially on one or the other of the two systems. The presence of MAO, especially in unfixed tissue, and DAO, especially in fixed tissue, is denoted and that of other oxidase(s) is connoted.

Inhibition of rat fat cell lipolysis by monoamine oxidase and semicarbazide-sensitive amine oxidase substrates

2003 ◽  
Vol 466 (3) ◽  
pp. 235-243 ◽  
Author(s):  
Virgile Visentin ◽  
Danielle Prévot ◽  
Luc Marti ◽  
Christian Carpéné
Keyword(s):  
Monoamine Oxidase ◽  
Amine Oxidase ◽  
Fat Cell
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