Renalase, a catecholamine-metabolising enzyme?
| Autor: | Frans Boomsma, Keith F. Tipton |
|---|---|
| Přispěvatelé: | Internal Medicine |
| Rok vydání: | 2007 |
| Předmět: |
medicine.medical_specialty
Amine oxidase Antioxidant Monoamine oxidase medicine.medical_treatment Clinical Neurology Kidney Cardiovascular System Cardiovascular Physiological Phenomena Catecholamines Dopamine Internal medicine medicine Animals Humans Monoamine Oxidase Biological Psychiatry Renalase chemistry.chemical_classification Amine Oxidase Structure and Function Chemistry Keywords: Renalase amine oxidase catecholamines metabolism dopamine noradrenaline Hydrogen Peroxide Psychiatry and Mental health medicine.anatomical_structure Endocrinology Enzyme Neurology Biochemistry Catecholamine Neurology (clinical) medicine.drug |
| Zdroj: | Journal of Neural Transmission Journal of Neural Transmission, 114(6), 775-776. Springer-Verlag |
| ISSN: | 0300-9564 |
| Popis: | Recently, a new FAD-dependent amine oxidase, renalase, was described. It was secreted by the kidney into the blood and shown to have significant cardiovascular actions, which were attributed to its catecholamine-metabolising activity. The authors concluded that renalase might be an important regulatory factor in human (patho)physiology. The catecholamine-metabolising activity of renalase in plasma contrasts with previous investigations where catecholamines were found to be stable in human plasma, provided autoxidation is prevented by an antioxidant. The claim of catecholamine-metabolising activity of renalase was based on the generation of H(2)O(2) during incubation of the enzyme with catecholamines. Careful inspection and calculations of the data lead to the conclusion that the rate of H(2)O(2) generation is far too low to be ascribed to enzymatic conversion of catecholamines by renalase. Renalase may well have important cardiovascular functions, but there is no proof that its actions are mediated through catecholamine-metabolising activity. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full text from SpringerLink