CD38 has both ADP-ribosyl cyclase and cADPR hydrolase activities and is capable of cleaving nicotinamide adenine dinucleotide (NAD) to cyclic ADP ribose (cADPR) which is a trigger for intracellular [Ca.sup.2+] release and hydrolyzing cADPR to ADPR
, respectively .
CD38 is a multifunctional enzyme that has both ADP-ribosyl cyclase and cADPR hydrolase activities, being capable of cleaving [NAD.sup.+] into cADPR and hydrolyzing cADPR to ADPR .
As a catalyst, CD38 has both ADP-ribosyl cyclase and cADPR hydrolase activities in which it cleaves NAD to generate cyclic ADP-ribose (cADPR), a putative [Ca.sup.2+] second messenger, and ADPR , respectively.
The CD38 gene encodes a glycosylated ~45 kDa type II transmembrane protein whose enzymatic activity generates cADPR and adenosine diphosphoribose (ADPR
) from [NAD.sup.+] and nicotinic acid adenine dinucleotide phosphate (NAADP) from [NADP.sup.+].
ROS-induced TRPM2 channel activation most probably occurs indirectly via formation of adenosine diphosphate ribose (ADPR
) which activates the channel by binding to a special domain located at the C-terminus of the channel .
CD38 is simultaneously a receptor and adhesion molecule as well as an ectoenzyme that catalyses the synthesis of ADP ribose (ADPR
), cyclic ADPR
(cAdPR), and nicotinic acid adenine dinucleotide phosphate (NAADP), starting from nicotinamide adenine dinucleotide ([NAD.sup.+]).