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Science 12 November 1993:
Vol. 262. no. 5136, pp. 1056 - 1059
DOI: 10.1126/science.8235624

Articles

Science, Vol 262, Issue 5136, 1056-1059
Copyright © 1993 by American Association for the Advancement of Science


articles

Formation and hydrolysis of cyclic ADP-ribose catalyzed by lymphocyte antigen CD38

M Howard, JC Grimaldi, JF Bazan, FE Lund, L Santos-Argumedo, RM Parkhouse, TF Walseth, and HC Lee

DNAX Research Institute, Palo Alto, CA 94304.

CD38 is a 42-kilodalton glycoprotein expressed extensively on B and T lymphocytes. CD38 exhibits a structural homology to Aplysia adenosine diphosphate (ADP)-ribosyl cyclase. This enzyme catalyzes the synthesis of cyclic ADP-ribose (cADPR), a metabolite of nicotinamide adenine dinucleotide (NAD+) with calcium-mobilizing activity. A complementary DNA encoding the extracellular domain of murine CD38 was constructed and expressed, and the resultant recombinant soluble CD38 was purified to homogeneity. Soluble CD38 catalyzed the formation and hydrolysis of cADPR when added to NAD+. Purified cADPR augmented the proliferative response of activated murine B cells, potentially implicating the enzymatic activity of CD38 in lymphocyte function.


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Selective Expression of RT6 Superfamily in Human Bronchial Epithelial Cells.
E. Balducci, K. Horiba, J. Usuki, M. Park, V. J. Ferrans, and J. Moss (1999)
Am. J. Respir. Cell Mol. Biol. 21, 337-346
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Regulation of Nuclear Localization and Transcriptional Activity of TFII-I by Bruton's Tyrosine Kinase.
C. D. Novina, S. Kumar, U. Bajpai, V. Cheriyath, K. Zhang, S. Pillai, H. H. Wortis, and A. L. Roy (1999)
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   Abstract »    Full Text »    PDF »
Mice Deficient for the Ecto-Nicotinamide Adenine Dinucleotide Glycohydrolase CD38 Exhibit Altered Humoral Immune Responses.
D. A. Cockayne, T. Muchamuel, J. C. Grimaldi, H. Muller-Steffner, T. D. Randall, F. E. Lund, R. Murray, F. Schuber, and M. C. Howard (1998)
Blood 92, 1324-1333
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Molecular Mechanism of Human CD38 Gene Expression by Retinoic Acid. IDENTIFICATION OF RETINOIC ACID RESPONSE ELEMENT IN THE FIRST INTRON.
H. Kishimoto, S.-i. Hoshino, M. Ohori, K. Kontani, H. Nishina, M. Suzawa, S. Kato, and T. Katada (1998)
J. Biol. Chem. 273, 15429-15434
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Calcium Signaling by Cyclic ADP-ribose, NAADP, and Inositol Trisphosphate Are Involved in Distinct Functions in Ascidian Oocytes.
M. Albrieux, H. C. Lee, and M. Villaz (1998)
J. Biol. Chem. 273, 14566-14574
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Kinetics of Establishing the Memory B Cell Population as Revealed by CD38 Expression.
A. Ridderstad and D. M. Tarlinton (1998)
J. Immunol. 160, 4688-4695
   Abstract »    Full Text »    PDF »
CD38 is functionally dependent on the TCR/CD3 complex in human T cells.
M. Morra, M. Zubiaur, C. Terhorst, J. Sancho, and F. Malavasi (1998)
FASEB J 12, 581-592
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Expression of CD38 Increases Intracellular Calcium Concentration and Reduces Doubling Time in HeLa and 3T3 Cells.
E. Zocchi, A. Daga, C. Usai, L. Franco, L. Guida, S. Bruzzone, A. Costa, C. Marchetti, and A. De Flora (1998)
J. Biol. Chem. 273, 8017-8024
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CD38 Functions Are Regulated Through an Internalization Step.
A. Funaro, M. Reinis, O. Trubiani, S. Santi, R. Di Primio, and F. Malavasi (1998)
J. Immunol. 160, 2238-2247
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Role of CD38 and Its Ligand in the Regulation of MHC-Nonrestricted Cytotoxic T Cells.
A. Cesano, S. Visonneau, S. Deaglio, F. Malavasi, and D. Santoli (1998)
J. Immunol. 160, 1106-1115
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Cyclic GMP-dependent and -independent Effects on the Synthesis of the Calcium Messengers Cyclic ADP-ribose and Nicotinic Acid Adenine Dinucleotide Phosphate.
R. M. Graeff, L. Franco, A. De Flora, and H. C. Lee (1998)
J. Biol. Chem. 273, 118-125
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Human CD38 (ADP-Ribosyl Cyclase) Is a Counter-Receptor of CD31, an Ig Superfamily Member.
S. Deaglio, M. Morra, R. Mallone, C. M. Ausiello, E. Prager, G. Garbarino, U. Dianzani, H. Stockinger, and F. Malavasi (1998)
J. Immunol. 160, 395-402
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Muscarinic Receptor-mediated Dual Regulation of ADP-ribosyl Cyclase in NG108-15 Neuronal Cell Membranes.
H. Higashida, S. Yokoyama, M. Hashii, M. Taketo, M. Higashida, T. Takayasu, T. Ohshima, S. Takasawa, H. Okamoto, and M. Noda (1997)
J. Biol. Chem. 272, 31272-31277
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