Renalase, a new secretory enzyme responsible for selective degradation of catecholamines: achievements and unsolved
A E Medvedev1, A V Veselovsky, V I Fedchenko
1Institute of Biomedical Chemistry, Russian Academy of Medical Sciences, Moscow, 119121, Russia. professor57@yandex.ru
Abstract:
Renalase is a recently discovered secretory enzyme responsible for selective degradation of blood catecholamines. The review summarizes literature data on expression of this enzyme and on its structure and functions. Special attention is paid to unsolved and questionable problems including: 1) prediction of the presence of FAD in the protein structure based on amino acid sequence similarity of renalase with known FAD-dependent enzymes; 2) identity of plasma and urinary renalase; 3) mechanism underlying conversion of inactive renalase into the active form.
Related Concept Videos
Transducer Mechanism: Enzyme-Linked Receptors
Major types that are helpful drug targets include:
Adrenergic Neurons: Neurotransmission
Synthesis: Catecholamine synthesis requires tyrosine, which is taken...
Drugs Affecting Neurotransmitter Release or Uptake
Renal Drug Excretion: Tubular Secretion
Adrenergic Agonists: Indirect-Acting Agents
One mechanism involves depleting stored catecholamines by displacing them from synaptic vesicles. These agents, known as "displacers," are transported into vesicles at the expense of noradrenaline. Examples include amphetamine and tyramine, which lack a catechol moiety, resulting in prolonged action, improved oral bioavailability, and...
Drugs Affecting Neurotransmitter Synthesis

