scholarly journals Multivalent Interactions of Human Primary Amine Oxidase with the V and C22 Domains of Sialic Acid-Binding Immunoglobulin-Like Lectin-9 Regulate Its Binding and Amine Oxidase Activity

PLoS ONE ◽  
2016 ◽  
Vol 11 (11) ◽  
pp. e0166935 ◽  
Author(s):  
Heli Elovaara ◽  
Vimal Parkash ◽  
Ruth Fair-Mäkelä ◽  
Outi M. H. Salo-Ahen ◽  
Gabriela Guédez ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Primary Amine ◽  
Oxidase Activity ◽  
Amine Oxidase ◽  
Sialic Acid Binding ◽  
Primary Amine Oxidase ◽  
Multivalent Interactions ◽  
Amine Oxidase Activity

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.

Acrolein produced from polyamines as one of the uraemic toxins

2003 ◽  
Vol 31 (2) ◽  
pp. 371-374 ◽  
Author(s):  
K. Sakata ◽  
K. Kashiwagi ◽  
S. Sharmin ◽  
S. Ueda ◽  
K. Igarashi
Keyword(s):  
Renal Failure ◽  
Chronic Renal Failure ◽  
Oxidase Activity ◽  
Culture Medium ◽  
Cellular Proliferation ◽  
Amine Oxidase ◽  
Early Stage ◽  
Chronic Glomerulonephritis ◽  
Toxic Compound ◽  
Amine Oxidase Activity

It is well known that the addition of spermine or spermidine to culture medium containing ruminant serum inhibits cellular proliferation. This effect is caused by the products of oxidation of polyamines that are generated by serum amine oxidase. Among the products, we found that acrolein is a major toxic compound produced from spermine and spermidine by amine oxidase. We then analysed the level of polyamines (putrescine, spermidine and spermine) and amine oxidase activity in plasma of patients with chronic renal failure. It was found that the levels of putrescine and the amine oxidase activity were increased, whereas spermidine and spermine were decreased in plasma of patients with chronic renal failure. The levels of free and protein-conjugated acrolein were also increased in plasma of patients with chronic renal failure. An increase in putrescine, amine oxidase and acrolein in plasma was observed in all cases such as diabetic nephropathy, chronic glomerulonephritis and nephrosclerosis. These results suggest that acrolein is produced during the early stage of nephritis through kidney damage and also during uraemia through accumulation of polyamines in blood due to the decrease in their excretion into urine.

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 Renalase Prevents AKI Independent of Amine Oxidase Activity

2014 ◽  
Vol 25 (6) ◽  
pp. 1226-1235 ◽  
Author(s):  
Ling Wang ◽  
Heino Velazquez ◽  
Gilbert Moeckel ◽  
John Chang ◽  
Ahrom Ham ◽  
...  
Keyword(s):  
Oxidase Activity ◽  
Amine Oxidase ◽  
Amine Oxidase Activity
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