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Large changes in NAD levels associated with CD38 expression during HL-60 cell differentiation.
Zainab N Al-Abady1, Barbara Durante, A John Moody
1School of Biological Sciences, Plymouth University, Plymouth PL4 8AA, UK.
Biochemical and Biophysical Research Communications
|November 13, 2013
Summary
CD38 enzyme activity lowers intracellular NAD+ levels, impacting cell functions. Inhibiting CD38 restores NAD+ balance, suggesting its role in disease pathogenesis.
Area of Science:
- Biochemistry
- Cell Biology
- Immunology
Background:
- Nicotinamide adenine dinucleotide (NAD) is crucial for metabolism and signaling.
- CD38 is an NAD-dependent enzyme implicated in NAD+ homeostasis and B-cell malignancies.
Purpose of the Study:
- Investigate CD38's role in regulating intracellular NAD+ levels.
- Determine the physiological consequences of altered NAD+ levels due to CD38 activity.
Main Methods:
- Utilized the HL-60 cell line for inducible CD38 expression.
- Measured intracellular NAD+ levels with varying CD38 expression.
- Assessed NAD+-dependent cellular functions during differentiation.
- Employed the CD38 inhibitor, kuromanin.
Main Results:
- Increased CD38 expression led to decreased intracellular NAD+ levels.
- CD38 inhibition (kuromanin) reversed the reduction in NAD+.
- Some, but not all, NAD+-dependent cellular processes were affected by lowered NAD+.
Conclusions:
- CD38 plays a significant role in maintaining intracellular NAD+ homeostasis.
- Altered NAD+ levels due to CD38 activity impact cellular physiology.
- Both enzymatic and cell surface functions of CD38 may contribute to B-cell chronic lymphocytic leukemia (B-CLL) pathogenesis.
