Related Experiment Videos
Nitric oxide mediates intracytoplasmic and intranuclear zinc release
D Berendji1, V Kolb-Bachofen, K L Meyer
1Biomedical Research Centre, Heinrich-Heine University, Düsseldorf, Germany.
FEBS Letters
|March 17, 1997
Summary
Nitric oxide (NO) causes zinc (Zn2+) release from proteins in cells. This study shows NO donors increase free Zn2+ in cell cytoplasm and nuclei, potentially affecting gene expression.
Area of Science:
- Biochemistry
- Cell Biology
- Molecular Biology
Background:
- Nitric oxide (NO) is known to disrupt zinc sulfide (ZnS) clusters.
- This disruption leads to the release of free zinc ions (Zn2+) from proteins, including zinc finger transcription factors.
Purpose of the Study:
- To investigate if exogenous NO increases cytoplasmic and nuclear free Zn2+ in living cells.
- To assess the relevance of NO-mediated Zn2+ release in a cellular context.
Main Methods:
- Utilized L929 cells, mouse splenocytes, and rat aorta endothelial cells.
- Cells were labeled with Zinquin-E, a Zn2+-specific fluorophore.
- Treated cells with S-nitrosocysteine or DETA/NO, which are spontaneous NO donors.
- Quantified NO-dependent Zn2+ release in splenocytes using flow cytometry.
Main Results:
- Both NO donors significantly increased Zn2+-dependent fluorescence in the cellular cytosol.
- A notable increase in Zn2+-dependent fluorescence was also observed within the cell nuclei.
- NO-mediated intracellular and intranuclear Zn2+ release was confirmed.
Conclusions:
- Nitrosative stress, induced by NO, mediates the release of intracellular and intranuclear Zn2+.
- This release of free Zn2+ may play a role in altering cellular gene expression patterns.