Self‐aggregation of purified and membrane‐bound erythrocyte CD38 induces extensive decrease of its ADP‐ribosyl cyclase activity

FEBS Letters

Calder, Lesley¹  Zocchi, Elena²  Guida, Lucrezia²  Franco, Luisa²  De Flora, Antonio² 

[1] Division of Virology, National Institute for Medical Research, Mill Hill, UK;Institute of Biochemistry, University of Genoa, and Advanced Biotechnology Center, Viale Benedetto XV/1, 16132 Genoa, Italy

关键词: CD38;    Erythrocyte;    Oligomerization;    ADP-ribosyl cyclase;    NAD+ glycohydrolase;    Enzyme inactivation;   

DOI  :  10.1016/0014-5793(95)00005-T

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The transmembrane glycoprotein CD38 is a bifunctional enzyme that catalyzes at its ectocellular domain both the synthesis and the hydrolysis of cyclic ADP-ribose (cADPR). The complete reaction, converting NAD⁺ to nicotinamide and ADP-ribose, reproduces an NAD⁺glycohydrolase (NADase) reaction. CD38 purified from human erythrocyte membranes has been recently shown to undergo stable oligomerization induced by either NAD⁺ or β-mercaptoethanol. We demonstrate that oligomerization is also triggered by reduced glutathione (GSH) and that the GSH-induced self-aggregation of purified CD38 is accompanied by extensive and comparable decrease of its ADP-ribosyl cyclase and NADase activities. GSH-induced oligomerization of CD38 and strong enzyme inactivation take place also in situ on erythrocyte membranes.

【 授权许可】

Unknown