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Self-aggregation of purified and membrane-bound erythrocyte CD38 induces extensive decrease of its ADP-ribosyl
FEBS Letters
|February 6, 1995
Summary
Reduced glutathione (GSH) triggers the self-aggregation of CD38, a key enzyme in cyclic ADP-ribose metabolism. This oligomerization significantly reduces both ADP-ribosyl cyclase and NADase activities of CD38 in vitro and in situ.
Area of Science:
- Biochemistry
- Enzymology
- Molecular Biology
Background:
- CD38 is a bifunctional enzyme involved in cyclic ADP-ribose (cADPR) metabolism, catalyzing both synthesis and hydrolysis.
- CD38 exhibits NAD+ glycohydrolase (NADase) activity, converting NAD+ to nicotinamide and ADP-ribose.
- Purified CD38 undergoes stable oligomerization induced by NAD+ or beta-mercaptoethanol.
Purpose of the Study:
- To investigate the effect of reduced glutathione (GSH) on CD38 oligomerization and enzymatic activity.
- To determine if GSH-induced oligomerization impacts CD38's ADP-ribosyl cyclase and NADase functions.
- To assess the occurrence of GSH-induced CD38 oligomerization and inactivation in situ.
Main Methods:
- Purification of CD38 from human erythrocyte membranes.
- Induction of CD38 oligomerization using reduced glutathione (GSH).
- Enzymatic assays to measure ADP-ribosyl cyclase and NADase activities.
- In situ studies on erythrocyte membranes.
Main Results:
- Reduced glutathione (GSH) induces stable oligomerization of purified CD38.
- GSH-induced CD38 oligomerization leads to a significant decrease in both ADP-ribosyl cyclase and NADase activities.
- Oligomerization and inactivation of CD38 by GSH were also observed in situ on erythrocyte membranes.
Conclusions:
- Reduced glutathione (GSH) is a novel inducer of CD38 oligomerization.
- GSH-mediated oligomerization results in substantial inactivation of CD38's enzymatic functions.
- These findings highlight a new regulatory mechanism for CD38 activity with implications for its biological roles.