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| FORMATION AND HYDROLYSIS OF CYCLIC ADP RIBOSE CATALYZED BY LYMPHOCYTE ANTIGEN-CD38 |
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| Author(s): HOWARD M, GRIMALDI JC, BAZAN JF, LUND FE, SANTOSARGUMEDO L, PARKHOUSE RME, WALSETH TF, LEE HC |
| Source: SCIENCE Volume: 262 Issue: 5136 Pages: 1056-1059 Published: NOV 12 1993 |
| Times Cited: 462 References: 28 |
| 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. |
| Document Type: Article |
| Language: English |
| Reprint Address: HOWARD, M (reprint author), DNAX RES INST MOLEC & CELLULAR BIOL INC, 901 CALIFORNIA AVE, PALO ALTO, CA 94304 USA |
Addresses:
1. INST ANIM HLTH, SURREY GU24 0NF, ENGLAND
2. UNIV MINNESOTA, DEPT PHARMACOL, MINNEAPOLIS, MN 55455 USA
3. UNIV MINNESOTA, DEPT PHYSIOL, MINNEAPOLIS, MN 55455 USA |
| Publisher: AMER ASSOC ADVANCEMENT SCIENCE, 1200 NEW YORK AVE, NW, WASHINGTON, DC 20005 |
| Subject Category: Multidisciplinary Sciences |
| IDS Number: MG187 |
| ISSN: 0036-8075 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |