Renalase—A new understanding of its enzymatic and non-enzymatic activity and its implications for future research

Abstract

Renalase was first described in 2005 and since then it became an object of scientific interest because of its proposed ability to catalyse circulating neurotransmitters and its promising antihypertensive effects. However, further research on the enzymatic activity of renalase did not confirm these initial findings and yielded that renalase serves to oxidize isomeric forms of β-NAD(P)H and recycle them by forming β-NAD(P)+. Moreover, in contrast to initial assumptions, it is indicated that renalase's enzymatic activity is confined to the cell and that extracellular renalase loses its enzymatic properties. These new reports led scientists to question as to whether renalase, as an enzyme, still has the potential to influence various systemic physiological responses (e.g. blood pressure). It was also put into question whether many physiological discoveries published based on the notion that renalase is secreted into the blood and acts by oxidation of catecholamines can still be considered valid. In this article, we attempt to review the literature to confront these doubts and find further possible directions of research on the importance of renalase. Our aim was to evaluate recent reports of non-enzymatic activity for renalase.