Self‐aggregation of purified and membrane‐bound erythrocyte CD38 induces extensive decrease of its ADP‐ribosyl cyclase activity
- 6 February 1995
- journal article
- Published by Wiley in FEBS Letters
- Vol. 359 (1) , 35-40
- https://doi.org/10.1016/0014-5793(95)00005-t
Abstract
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 membranesKeywords
This publication has 18 references indexed in Scilit:
- Cell Surface Antigen CD38 Identified as Ecto-Enzyme of NAD Glycohydrolase Has Hyaluronate-Binding ActivityBiochemical and Biophysical Research Communications, 1994
- Self-Aggregation of the Transmembrane Glycoprotein CD38 Purified from Human ErythrocytesBiochemical and Biophysical Research Communications, 1994
- Human lymphocyte antigen CD38 catalyzes the production of cyclic ADP‐riboseFEBS Letters, 1993
- Formation and Hydrolysis of Cyclic ADP-Ribose Catalyzed by Lymphocyte Antigen CD38Science, 1993
- A Single Protein Immunologically Identified as CD38 Displays NAD+ Glycohydrolase, ADP-Ribosyl Cyclase and Cyclic ADP-Ribose Hydrolase Activities at the Outer Surface of Human ErythrocytesBiochemical and Biophysical Research Communications, 1993
- Human CD38 is associated to distinct molecules which mediate transmembrane signaling in different lineagesEuropean Journal of Immunology, 1993
- Production and Hydrolysis of Cyclic ADP-Ribose at the Outer Surface of Human ErythrocytesBiochemical and Biophysical Research Communications, 1993
- Cyclic ADP-Ribose in Insulin Secretion from Pancreatic βCellsScience, 1993
- Cyclic ADP-Ribose: a New Way to Control CalciumScience, 1993
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970