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Updated: Aug 9, 2026
12:07
Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry
Published on: March 24, 2012
Redox regulation by thioredoxin and thioredoxin-binding proteins
A Nishiyama1, H Masutani, H Nakamura
1Department of Biological Responses, Institute for Virus Research, Kyoto University, Japan.
IUBMB Life
|January 25, 2002
Summary
Thioredoxin is a key protein in redox regulation, influencing cell processes and transcription factor activity. New research identifies thioredoxin binding proteins that modulate its function, impacting cellular redox balance.
Area of Science:
- Cellular Biology
- Biochemistry
- Molecular Biology
Background:
- Reduction/oxidation (redox) regulation is crucial in biological processes.
- Thioredoxin is a central protein in the thiol reducing system, impacting cell proliferation and apoptosis.
- Thioredoxin influences DNA binding of transcription factors like NF-kappaB and p53.
Purpose of the Study:
- To identify proteins that interact with thioredoxin.
- To understand the role of thioredoxin interacting proteins in redox regulation.
- To investigate the regulatory mechanisms of thioredoxin activity.
Main Methods:
- Yeast two-hybrid system was employed to identify thioredoxin binding proteins.
- Analysis of thioredoxin's effect on transcription factor activity (e.g., NF-kappaB).
- Investigation of thioredoxin's interaction with signaling molecules like ASK1.
Main Results:
- p40phox (TBP-1) and VDUP1 (TBP-2) were identified as thioredoxin binding proteins.
- VDUP1 negatively regulates thioredoxin expression and reducing activity.
- Thioredoxin inhibits TNF-alpha induced activation of ASK1 and p38 MAP kinase pathway.
Conclusions:
- Thioredoxin interacting proteins, such as VDUP1, play a significant role in modulating thioredoxin's function.
- These interactions are critical for thioredoxin-mediated redox regulation in cellular processes.
- Understanding these interactions provides insights into cellular redox homeostasis and signaling pathways.
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