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Vol. 273, Issue 1, 118-125, January 2, 1998
,
From the Cyclic ADP-ribose (cADPR) and
nicotinic acid adenine dinucleotide phosphate (NAADP) have been shown
to mobilize intracellular Ca2+ stores by totally
independent mechanisms, which are pharmacologically distinct from that
activated by inositol trisphosphate. Although cADPR and NAADP are
structurally and functionally different, they can be synthesized by a
single enzyme having ADP-ribosyl cyclase activity. In this study, three
different assays were used to measure the metabolism of cADPR in sea
urchin egg homogenates including a radioimmunoassay, a Ca2+
release assay, and a thin layer chromatographic assay. Soluble and
membrane-bound ADP-ribosyl cyclases were identified and both cyclized
NAD to produce cADPR. The soluble cyclase was half-maximally stimulated
by 5.3 µM cGMP, but not by cAMP, while the membrane-bound form was independent of cGMP. The two forms of the cyclase were also
different in the pH dependence of utilizing nicotinamide guanine
dinucleotide (NGD), a guanine analog of NAD, as substrate, indicating
they are two separate enzymes. The stimulatory effect of cGMP required
ATP or ATP Department of Physiology, University of
Minnesota, Minneapolis, Minnesota 55455 and § Istituto
Policattedra Di Chimica Biologica Universita Degli Studi Di Genova,
Viale Benedetto XV, 1, 16132 Genova, Italy
S (adenosine 5
-O-(3-thiotriphosphate)) and a
cGMP-dependent kinase activity was shown to be present in the soluble fraction. The degradation of cADPR to ADP-ribose was catalyzed by cADPR hydrolase, which was found to be predominantly associated with membranes. Similar to the membrane-bound cyclase, the
cADPR hydrolase activity was also independent of cGMP. Both the soluble
and membrane fractions also catalyzed the synthesis of NAADP through
exchanging the nicotinamide group of NADP with nicotinic acid (NA). The
base-exchange activity was independent of cGMP and the half-maximal
concentrations of NADP and NA needed were about 0.2 mM and
10 mM, respectively. The exchange reaction showed a
preference for acidic pH, contrasting with the neutral pH optimum of
the cyclase activities. The complex metabolic pathways characterized in
this study indicate that there may be a multitude of regulatory
mechanisms for controlling the endogenous concentrations of cADPR and
NAADP.
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