On the characteristics of mitochondrial monoamine oxidase in pancreas and adipose tissues from genetically obese mice.
The substrate specificity of mitochondrial monoamine oxidase (MAO) in pancreatic and adipose tissues of obese mice and their lean counterparts was determined. The pancreatic MAO of obese mice had a greater specific activity than that of the lean mice. The white adipose tissue MAO was found to be more active than the brown adipose MAO in both groups of mice. While there was no appreciable difference in the MAO activities of brown adipose tissues between obese and lean mice, the enzyme from the white adipose tissue of obese mice had a higher specific activity than that of the lean mice. The higher MAO activity in white adipose tissue was observed when tyramine or serotonin was employed as substrate but not with benzylamine. Examination of mitochondrial MAO from epididymal adipocytes revealed marked differences in the properties of the enzyme between whole adipose tissue and isolated adipocytes. The inhibition characteristics of MAO from these tissues were studied with the specific inhibitors clorgyline and deprenyl.
D000273:Adipose Tissue / Q000201:enzymology*; D000818:Animals; D003010:Clorgyline / Q000494:pharmacology; D008297:Male; D051379:Mice; D008820:Mice, Obese; D008928:Mitochondria / Q000201:enzymology*; D008995:Monoamine Oxidase / Q000378:metabolism*; D008996:Monoamine Oxidase Inhibitors / Q000494:pharmacology; D010179:Pancreas / Q000201:enzymology*; D012642:Selegiline / Q000494:pharmacology; D013379:Substrate Specificity
D008996:Monoamine Oxidase Inhibitors; D012642:Selegiline; D008995:Monoamine Oxidase; D003010:Clorgyline