Ectocellular CD38-catalyzed synthesis and intracellular Ca2+-mobilizing activity of cyclic ADP-ribose

Ectocellular CD38-catalyzed synthesis and intracellular Ca2+-mobilizing activity of cyclic... CD38 is a type-II transmembrane glycoprotein occurring in several hematopoietic and mature blood cells as well as in other cell types, including neurons. Although classified as an orphan receptor, CD38 is also a bifunctional ectoenzyme that catalyzes both the conversion of NAD+ to nicotinamide and cyclic ADP-ribose (cADPR), via an ADP-ribosyl cyclase reaction, and also the hydrolysis of cADPR to ADP-ribose (hydrolase). Major unresolved questions concern the correlation between receptor and catalytic properties of CD38, and also the apparent contradiction between ectocellular generation and intracellular Ca2+-mobilizing activity of cADPR. Results are presented that provide some explanations to this topological paradox in two different cell types. In cultured rat cerebellar granule neurons, extracellular cADPR (either generated by CD38 or directly added) elicited an enhanced intracellular Ca2+ response to KCl-induced depolarization, a process that can be qualified as a Ca2+-induced Ca2+ release (CICR) mechanism. On the other hand, in the CD38+ human Namalwa B lymphoid cells, NAD+ (and thiol compounds as well) induced a two-step process of self-aggregation followed by endocytosis of CD38, which resulted in a shift of cADPR metabolism from the cell surface to the cytosol. Both distinctive types of cellular responses to extracellular NAD+ seem to be suitable to elicit changes in the intracellular Ca2+ homeostasis. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Cell Biochemistry and Biophysics Springer Journals

Ectocellular CD38-catalyzed synthesis and intracellular Ca2+-mobilizing activity of cyclic ADP-ribose

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Publisher
Springer Journals
Copyright
Copyright © 1988 by Humana Press Inc
Subject
Life Sciences; Biochemistry, general; Pharmacology/Toxicology; Biotechnology; Cell Biology
ISSN
1085-9195
eISSN
1559-0283
D.O.I.
10.1007/BF02738309
Publisher site
See Article on Publisher Site

Abstract

CD38 is a type-II transmembrane glycoprotein occurring in several hematopoietic and mature blood cells as well as in other cell types, including neurons. Although classified as an orphan receptor, CD38 is also a bifunctional ectoenzyme that catalyzes both the conversion of NAD+ to nicotinamide and cyclic ADP-ribose (cADPR), via an ADP-ribosyl cyclase reaction, and also the hydrolysis of cADPR to ADP-ribose (hydrolase). Major unresolved questions concern the correlation between receptor and catalytic properties of CD38, and also the apparent contradiction between ectocellular generation and intracellular Ca2+-mobilizing activity of cADPR. Results are presented that provide some explanations to this topological paradox in two different cell types. In cultured rat cerebellar granule neurons, extracellular cADPR (either generated by CD38 or directly added) elicited an enhanced intracellular Ca2+ response to KCl-induced depolarization, a process that can be qualified as a Ca2+-induced Ca2+ release (CICR) mechanism. On the other hand, in the CD38+ human Namalwa B lymphoid cells, NAD+ (and thiol compounds as well) induced a two-step process of self-aggregation followed by endocytosis of CD38, which resulted in a shift of cADPR metabolism from the cell surface to the cytosol. Both distinctive types of cellular responses to extracellular NAD+ seem to be suitable to elicit changes in the intracellular Ca2+ homeostasis.

Journal

Cell Biochemistry and BiophysicsSpringer Journals

Published: Oct 27, 2007

References

  • The lymphocyte surface antigen CD38 acts as a nicotinamide adenine dinucleotide glycohydrolase in human T lymphocytes
    Gelman, L.; Deterre, P.; Gouy, H.; Boumsell, L.; Debré, P.; Bismuth, G.

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