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

Maureen Howard; J. Christopher Grimaldi; J. Fernando Bazan; Frances E. Lund; Leopoldo Santos-Argumedo; R. M.E. Parkhouse; Timothy F. Walseth; Hon Cheung Lee

doi:10.1126/science.8235624

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

Maureen Howard, J. Christopher Grimaldi, J. Fernando Bazan, Frances E. Lund, Leopoldo Santos-Argumedo, R. M.E. Parkhouse, Timothy F. Walseth, Hon Cheung Lee

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702 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	1056-1059
Number of pages	4
Journal	Science
Volume	262
Issue number	5136
DOIs	https://doi.org/10.1126/science.8235624
State	Published - 1993
Externally published	Yes

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title = "Formation and hydrolysis of cyclic ADP-ribose catalyzed by lymphocyte antigen CD38",

abstract = "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.",

author = "Maureen Howard and Grimaldi, {J. Christopher} and Bazan, {J. Fernando} and Lund, {Frances E.} and Leopoldo Santos-Argumedo and Parkhouse, {R. M.E.} and Walseth, {Timothy F.} and Lee, {Hon Cheung}",

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doi = "10.1126/science.8235624",

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T1 - Formation and hydrolysis of cyclic ADP-ribose catalyzed by lymphocyte antigen CD38

AU - Howard, Maureen

AU - Grimaldi, J. Christopher

AU - Bazan, J. Fernando

AU - Lund, Frances E.

AU - Santos-Argumedo, Leopoldo

AU - Parkhouse, R. M.E.

AU - Walseth, Timothy F.

AU - Lee, Hon Cheung

PY - 1993

Y1 - 1993

N2 - 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.

AB - 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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JO - Science

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

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