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The CD38/cyclic ADP-ribose system: a topological paradox
A De Flora1, L Guida, L Franco
1Institute of Biochemistry, University of Genova, Italy.
The International Journal of Biochemistry & Cell Biology
|January 23, 1998
Summary
CD38 is an ectoenzyme that generates cyclic ADP-ribose (cADPR), a molecule regulating calcium. Its extracellular synthesis and intracellular activity present unique cellular regulation mechanisms.
Area of Science:
- Biochemistry
- Cell Biology
- Immunology
Background:
- CD38 was initially identified as a lymphocyte differentiation antigen.
- It exhibits properties of an orphan receptor involved in cell proliferation and activation.
- CD38 functions as a bifunctional ectoenzyme catalyzing cyclic ADP-ribose (cADPR) formation.
Purpose of the Study:
- To explore the dual nature of CD38 as both a receptor and an enzyme.
- To investigate the mechanisms behind the extracellular synthesis and intracellular activity of cADPR.
- To understand the role of the CD38/cADPR system in cellular regulation.
Main Methods:
- Analysis of CD38's enzymatic activity in various cell types.
- Investigation of cADPR's role in calcium homeostasis.
- Examination of cADPR transport and CD38 internalization mechanisms.
Main Results:
- CD38 catalyzes the formation of cADPR, a second messenger for calcium release.
- Two mechanisms explain cADPR's intracellular action: membrane influx and CD38 internalization.
- CD38/cADPR system demonstrates unusual ectobiochemistry with regulatory potential.
Conclusions:
- CD38's bifunctional nature presents unique challenges in understanding cellular compartmentation.
- The CD38/cADPR system offers novel insights into cellular regulation via ectobiochemistry.
- Further research is needed to fully elucidate the unrecognized properties of this system.