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      Renalase, a catecholamine-metabolising enzyme?

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          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 2O 2 during incubation of the enzyme with catecholamines. Careful inspection and calculations of the data lead to the conclusion that the rate of H 2O 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.

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          Renalase is a novel, soluble monoamine oxidase that regulates cardiac function and blood pressure.

          The kidney not only regulates fluid and electrolyte balance but also functions as an endocrine organ. For instance, it is the major source of circulating erythropoietin and renin. Despite currently available therapies, there is a marked increase in cardiovascular morbidity and mortality among patients suffering from end-stage renal disease. We hypothesized that the current understanding of the endocrine function of the kidney was incomplete and that the organ might secrete additional proteins with important biological roles. Here we report the identification of a novel flavin adenine dinucleotide-dependent amine oxidase (renalase) that is secreted into the blood by the kidney and metabolizes catecholamines in vitro (renalase metabolizes dopamine most efficiently, followed by epinephrine, and then norepinephrine). In humans, renalase gene expression is highest in the kidney but is also detectable in the heart, skeletal muscle, and the small intestine. The plasma concentration of renalase is markedly reduced in patients with end-stage renal disease, as compared with healthy subjects. Renalase infusion in rats caused a decrease in cardiac contractility, heart rate, and blood pressure and prevented a compensatory increase in peripheral vascular tone. These results identify renalase as what we believe to be a novel amine oxidase that is secreted by the kidney, circulates in blood, and modulates cardiac function and systemic blood pressure.
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            Plasma semicarbazide-sensitive amine oxidase in human (patho)physiology.

            Semicarbazide-sensitive amine oxidases (SSAO) are widely distributed enzymes, with as yet not fully elucidated functions and roles, present in many tissues but also circulating in plasma. The enzyme also functions as an adhesion molecule, the vascular adhesion protein-1. In healthy humans, plasma SSAO activity is constant from birth until 16 years of age, when it drops to lower values, gradually increasing again at advanced ages. When measuring SSAO activity, care should be taken to ensure proper preparation and storage conditions, and it should be realized that quite a few drugs unintentionally are good inhibitors, and sometimes even substrates, of SSAO. Under normal conditions SSAO activity is constant and inter-individual variation is small. In various pathophysiological conditions plasma SSAO activities are increased, most notably in diabetes mellitus (both type I and type II), in congestive heart failure and in cirrhotic liver inflammation. In patients with other vascular and inflammatory diseases plasma SSAO is normal, while it is low in children with congenital lung diseases. Interpretation of these changes is speculative, since source and regulation of plasma SSAO are as yet unknown. However, in two situations where the disease-causing process was ended (transplantation, delivery), plasma SSAO returned to normal. Many questions remain to be answered.
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              Monoamine Oxidase Assays


                Author and article information

                J Neural Transm
                Journal of Neural Transmission
                Springer-Verlag (Vienna )
                26 March 2007
                June 2007
                : 114
                : 6
                : 775-776
                [ ]Department of Internal Medicine, Section of Vascular Pharmacology, Erasmus MC, Rotterdam, The Netherlands
                [ ]Department of Biochemistry, Trinity College, Dublin, Ireland
                © Springer-Verlag 2007
                Amine Oxidase Structure and Function
                Custom metadata
                © Springer-Verlag 2007


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