FORMATION AND HYDROLYSIS OF CYCLIC ADP RIBOSE CATALYZED BY LYMPHOCYTE ANTIGEN-CD38
FORMATION AND HYDROLYSIS OF CYCLIC ADP RIBOSE CATALYZED BY LYMPHOCYTE ANTIGEN-CD38
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DOI：
10.1126/science.8235624
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发表时间：
1993-11-12
期刊：
影响因子：
56.9
通讯作者：
LEE, HC
中科院分区：
文献类型：
--
作者：
HOWARD, M;GRIMALDI, JC;LEE, HC
CD38是一种42千道长的糖蛋白，广泛表达于B和T淋巴细胞上。CD38与ADP-核糖环化酶具有结构上的同源性。该酶催化合成具有钙动员活性的烟酰胺腺嘌呤二核苷酸(NAD+)的代谢物环状ADP-核糖(CADPR)。构建并表达了编码小鼠CD38胞外区的互补DNA，纯化了重组可溶性CD38。当加入NAD+时，可溶性CD38催化cADPR的形成和水解。纯化的cADPR增强了激活的小鼠B细胞的增殖反应，可能与CD38在淋巴细胞功能中的酶活性有关。
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.