The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.
ADP-ribosyl Cyclase and CD38 Catalyze the Synthesis of a Calcium-mobilizing Metabolite from NADP+
Open accessAbstract
ADP-ribosyl cyclase catalyzes the cyclization of NAD+ to produce cyclic ADP-ribose (cADPR), which is emerging as an endogenous regulator of the Ca(2+)-induced Ca2+ release mechanism in cells. CD38 is a lymphocyte differentiation antigen which has recently been shown to be a bifunctional enzyme that can synthesize cADPR from NAD+ as well as hydrolyze cADPR to ADP-ribose. In this study, we show that both the cyclase and CD38 can also catalyze the exchange of the nicotinamide group of NADP+ with nicotine acid (NA). The product is nicotinic acid adenine dinucleotide phosphate (NAADP+), a metabolite we have previously shown to be potent in Ca2+ mobilization (Lee, H. C., and Aarhus, R. (1995) J. Biol. Chem. 270, 2152-2157). The switch of the catalysis to the exchange reaction requires acidic pH and NA. The half-maximal effective concentration of NA is about 5 mM for both the cyclase and CD38. In the absence of NA or at neutral pH, the cyclase converts NADP+ to another metabolite, which is identified as cyclic ADP-ribose 2'-phosphate. Under the same conditions, CD38 converts NADP+ to ADP-ribose 2'-phosphate instead, which is the hydrolysis product of cyclic ADP-ribose 2'-phosphate. That two different products of ADP-ribosyl cyclase and CD38, cADPR and NAADP+, are both involved in Ca2+ mobilization suggests a crucial role of these enzymes in Ca2+ signaling.
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Cites
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Formation and Hydrolysis of Cyclic ADP-Ribose Catalyzed by Lymphocyte Antigen CD38
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Self-citationCa 2+ -Induced Ca 2+ Release in Sea Urchin Egg Homogenates: Modulation by Cyclic ADP-Ribose
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Self-citationStructural Determination of a Cyclic Metabolite of NAD+ with Intracellular Ca2+-mobilizing Activity
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Self-citationADP-ribosyl cyclase: an enzyme that cyclizes NAD+ into a calcium-mobilizing metabolite.
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Self-citationRelease of Ca 2+ from Individual Plant Vacuoles by Both InsP 3 and Cyclic ADP-Ribose
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Cited by
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Evolution and function of the ADP ribosyl cyclase/CD38 gene family in physiology and pathology
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Two-pore channels control Ebola virus host cell entry and are drug targets for disease treatment
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Generation, Control, and Processing of Cellular Calcium Signals
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Metadata
- Authors
- Aarhus, R., Graeff, R. M., Dickey, D. M., Walseth, T. F., & Hon, C. L.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1995-12
- Volume
- 270
- Issue
- 51
- Pages
- 30327-30333
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2001695130
- Cited by
- 416
- References
- 24
- FWCI
- 6.50
- Type
- journal article
- Language
- en
- Open access
- hybrid
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