scholarly journals Substrate Selectivity of Monoamine Oxidase A, Monoamine Oxidase B, Diamine Oxidase, and Semicarbazide-Sensitive Amine Oxidase in COS-1 Expression Systems

2006 ◽  
Vol 29 (12) ◽  
pp. 2362-2366 ◽  
Author(s):  
Yoshinori Ochiai ◽  
Kunio Itoh ◽  
Eiichi Sakurai ◽  
Mayuko Adachi ◽  
Yorihisa Tanaka
Keyword(s):  
Monoamine Oxidase ◽  
Diamine Oxidase ◽  
Amine Oxidase ◽  
Monoamine Oxidase A ◽  
Monoamine Oxidase B ◽  
Substrate Selectivity ◽  
Expression Systems

scholarly journals Site-specific expression of amine oxidases in breast cancer metastases

Tumor Biology ◽  
2018 ◽  
Vol 40 (5) ◽  
pp. 101042831877682 ◽  
Author(s):  
Yoon Jin Cha ◽  
Woo Hee Jung ◽  
Ja Seung Koo
Keyword(s):  
Breast Cancer ◽  
Metastatic Breast Cancer ◽  
Monoamine Oxidase ◽  
Diamine Oxidase ◽  
Amine Oxidase ◽  
Lung Metastases ◽  
Lysyl Oxidase ◽  
Metastatic Breast ◽  
Monoamine Oxidase B ◽  
Related Proteins

We aimed to evaluate the expression of amine oxidase-related proteins in metastatic breast cancer tissue and determine its clinical implication. A tissue microarray was constructed from a total of 126 metastatic breast tumors (31 bone metastases (24.6%), 36 brain metastases (28.6%), 11 liver metastases (8.7%), and 48 lung metastases (38.1%)). Immunohistochemical staining for amine oxidase-related proteins (lysyl oxidase, diamine oxidase, and monoamine oxidase A and B) was performed. In metastatic breast cancer tissue, lysyl oxidase ( p = 0.001), tumoral diamine oxidase ( p = 0.003), stromal diamine oxidase ( p = 0.047), and stromal monoamine oxidase B ( p = 0.002) were differentially expressed in different metastatic sites. Bone metastases showed low expression of lysyl oxidase, tumoral diamine oxidase, and stromal diamine oxidase. We observed high expression of lysyl oxidase in brain metastases, tumoral diamine oxidase in liver metastases, stromal diamine oxidase in lung metastases, and stromal monoamine oxidase B in bone metastases. Lysyl oxidase positivity was associated with progesterone receptor negativity ( p = 0.001), and monoamine oxidase A positivity was associated with human epidermal growth factor receptor-2 negativity ( p = 0.003) and the luminal A subtype ( p = 0.003). On univariate analysis shorter overall survival was associated with stromal diamine oxidase negativity ( p = 0.008), especially in lung metastases ( p = 0.025), and stromal monoamine oxidase B positivity ( p < 0.001). Stromal monoamine oxidase B positivity was an independent prognostic factor for shorter overall survival in multivariate Cox analysis (hazard ratio, 4.069; 95% confidence interval, 1.649–10.04; p = 0.002). Finally, in metastatic breast cancer, amine oxidase-related proteins were differentially expressed in a manner specific to metastatic site, and stromal monoamine oxidase B expression was correlated with prognosis.

scholarly journals Oxidation of 3-amino-1-phenylprop-1-enes by monoamine oxidase and their use in a continuous assay of the enzyme

1988 ◽  
Vol 256 (3) ◽  
pp. 911-915 ◽  
Author(s):  
C H Williams ◽  
J Lawson ◽  
F R C Backwell
Keyword(s):  
Monoamine Oxidase ◽  
Absorption Coefficient ◽  
Mitochondrial Protein ◽  
Bovine Liver ◽  
Spectrophotometric Assay ◽  
Monoamine Oxidase A ◽  
Monoamine Oxidase B ◽  
High Absorption Coefficient ◽  
Continuous Assay ◽  
High Absorption

3-Amino-1-phenylprop-1-ene (cinnamylamine) and some derivatives were examined as substrates for monoamine oxidases A and B in mitochondria. All of the amines examined were readily oxidized by monoamine oxidase B but much less readily by monoamine oxidase A. E-Cinnamylamine was found to have Km 0.025 mM and Vmax. 3.9 nmol/min per mg of mitochondrial protein. Corresponding values with monoamine oxidase A were 0.026 mM and 0.85 nmol/min per mg respectively. Despite their different stereochemistry, E- and Z-N-methylcinnamylamines were almost equally effective as substrates for monoamine oxidase B. The characteristic u.v. absorbance and high absorption coefficient of cinnamaldehyde, the product produced by enzymic oxidation of cinnamylamine, is utilized in a sensitive continuous spectrophotometric assay for both enzymes in the rat and for the assay of a purified monoamine oxidase B from bovine liver.

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.

scholarly journals Chronic monoamine oxidase-B inhibitor treatment blocks monoamine oxidase-A enzyme activity

2013 ◽  
Vol 121 (4) ◽  
pp. 379-383 ◽  
Author(s):  
Jasmin Bartl ◽  
Thomas Müller ◽  
Edna Grünblatt ◽  
Manfred Gerlach ◽  
Peter Riederer
Keyword(s):  
Enzyme Activity ◽  
Monoamine Oxidase ◽  
Monoamine Oxidase A ◽  
Monoamine Oxidase B ◽  
Inhibitor Treatment
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