Formation and Hydrolysis of Cyclic ADP-Ribose Catalyzed by Lymphocyte Antigen CD38

CD38 is a 42-kilodalton glycoproteln 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$^+$)...

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Veröffentlicht in:	Science (American Association for the Advancement of Science) 1993-11, Vol.262 (5136), p.1056-1059
Hauptverfasser:	Howard, Maureen, Grimaldi, J. Christopher, Bazan, J. Fernando, Lund, Frances E., Santos-Argumedo, Leopoldo, Parkhouse, R. M. E., Walseth, Timothy F., Lee, Hon Cheung
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Diphosphate Ribose - analogs & derivatives Adenosine Diphosphate Ribose - metabolism Adenosine Diphosphate Ribose - pharmacology ADP-ribosyl Cyclase ADP-ribosyl Cyclase 1 Amino Acid Sequence Amino acids Animals Antibodies Antigens, CD Antigens, Differentiation - isolation & purification Antigens, Differentiation - metabolism B lymphocytes B-Lymphocytes - drug effects B-Lymphocytes - metabolism Biological and medical sciences Calcium - metabolism Cell regulation Cellular control mechanisms Cyclic ADP-Ribose Eggs Enzymes Fundamental and applied biological sciences. Psychology Fundamental immunology Hydrolysis Immunobiology Lymphocyte Activation Lymphocyte antigens Lymphocytes Lymphoid cells: ontogeny, maturation, markers, receptors, circulation and recirculation Membrane Glycoproteins Mice Molecular Sequence Data N-Glycosyl Hydrolases - metabolism NAD - metabolism Recombinant Proteins - metabolism T lymphocytes
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Beschreibung
Zusammenfassung:	CD38 is a 42-kilodalton glycoproteln 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.
ISSN:	0036-8075 1095-9203
DOI:	10.1126/science.8235624