Summerhill R J, Jackson D G, Galione A
Department of Molecular Immunology, John Radcliffe Hospital, Headington, Oxford, UK.
FEBS Lett. 1993 Dec 6;335(2):231-3. doi: 10.1016/0014-5793(93)80735-d.
The human lymphocyte antigen CD38 has been shown to share sequence homology with ADP-ribosyl cyclase, the enzyme that catalyzes the conversion of NAD+ to cyclic ADP-ribose (cADPR), a potent Ca(2+)-mobilizing agent. In this study COS1 cells from African Green Monkey kidney were transiently transfected with CD38 cDNA, inducing expression of authentic CD38 on the cell surface. We demonstrate that CD38 expressed in this manner can convert NAD+ to cADPR in the extracellular medium as assessed by Ca2+ release from sea-urchin egg microsomes.
人类淋巴细胞抗原CD38已被证明与ADP-核糖基环化酶具有序列同源性，该酶催化NAD+转化为环ADP-核糖（cADPR），一种有效的钙动员剂。在本研究中，用CD38 cDNA瞬时转染来自非洲绿猴肾的COS1细胞，诱导细胞表面表达天然CD38。我们证明，通过海胆卵微粒体释放钙离子评估，以这种方式表达的CD38可以在细胞外培养基中将NAD+转化为cADPR。
