Renalase has been claimed to degrade catecholamines like adrenaline (epinephrine) and noradrenaline (norepinephrine) in the blood circulation. Dr. Gary Desir's laboratory at Yale School of Medicine discovered and named renalase in 2005 suggest that the human kidney releases this protein into the bloodstream to regulate blood pressure (in addition to other possible, as yet undiscovered, functions). Whether renalase actually oxidizes catecholamine substrates has been widely disputed. The primary evidence for catecholamine oxidation is the detection of H2O2, however catecholamines emanate H2O2 in the presence of O2 in a natural decomposition reaction. In 2013, renalase was claimed to oxidize α-NADH (the normal form of NADH is the β anomer) to β-NAD+, with concomitant reduction of O2 (dioxygen) to H2O2 (hydrogen peroxide). This reaction was proposed to repair aberrant NADH and NADPH forms that are not accepted as cofactors by most nicotinamide-dependent oxidoreductase enzymes.