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Cycloheximide Chase Analysis of Protein Degradation in Saccharomyces cerevisiae

Cycloheximide Chase Analysis of Protein Degradation in Saccharomyces cerevisiae

Published on: April 18, 2016

CD38: a NAADP degrading enzyme.

Frederike Schmid¹, Sören Bruhn, Karin Weber

¹Department of Biochemistry and Signal Transduction, University Medical Centre Hamburg-Eppendorf, Hamburg, Germany.

|October 25, 2011

Summary

This summary is machine-generated.

The enzyme CD38 does not synthesize nicotinic acid adenine dinucleotide phosphate (NAADP) in cells or mice. Instead, CD38 appears to degrade NAADP, potentially preventing excessive levels in T cells.

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Area of Science:

Biochemistry
Immunology
Cellular Biology

Background:

CD38 is a known enzyme involved in cellular signaling.
Nicotinic acid adenine dinucleotide phosphate (NAADP) is a crucial second messenger for calcium mobilization.
The precise role of CD38 in NAADP metabolism has been debated.

Purpose of the Study:

To investigate the role of the enzyme CD38 in the synthesis and degradation of NAADP.
To determine if CD38 is essential for NAADP formation in T cells and in vivo.
To clarify whether CD38 acts as a NAADP-forming or NAADP-degrading enzyme.

Main Methods:

Gene silencing of CD38 in Jurkat T cells.
Analysis of NAADP levels in CD38 knockout mice (thymus and spleen).
In vitro experiments assessing NAADP formation and degradation by CD38.

Main Results:

Gene silencing of CD38 did not inhibit NAADP synthesis in Jurkat T cells.
NAADP synthesis remained unaffected in thymus and spleen of CD38 knockout mice.
In vitro studies showed that CD38 efficiently decreased NAADP formation and increased degradation.

Conclusions:

CD38 is not a NAADP-forming enzyme in vivo.
CD38 functions as a NAADP-degrading enzyme, regulating cellular NAADP levels.
This degradation activity may prevent NAADP-induced desensitization in intact cells.