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Redox signalling: from nitric oxide to oxidized lipids
Sruti Shiva1, Doug Moellering, Anup Ramachandran
1Department of Pathology, Center for Free Radical Biology, University of Alabama at Birmingham, 901 19th Street South, Birmingham, AL 35294-32180, USA.
Biochemical Society Symposium
|March 22, 2005
Summary
Cellular redox signaling involves protein modifications by reactive oxygen and nitrogen species (ROS/RNS). These modifications, including S-nitrosation and reactions with lipids, regulate cell signaling pathways and are termed "redox tone".
Area of Science:
- Biochemistry
- Cell Biology
- Molecular Biology
Background:
- Cellular redox signaling regulates cell functions through protein modifications by reactive oxygen and nitrogen species (ROS/RNS).
- Nitric oxide (NO) is a key mediator, inducing protein conformational changes via heme addition or thiol S-nitrosation.
- Other ROS/RNS, like electrophilic lipids, also modify signaling proteins.
Purpose of the Study:
- To review the mechanisms of redox cell signaling.
- To highlight the role of ROS/RNS in protein post-translational modifications.
- To discuss the concept of 'redox tone' in modulating signaling pathways.
Main Methods:
- Literature review of redox signaling mechanisms.
- Analysis of protein modifications by ROS/RNS, including S-nitrosation and lipid adducts.
- Examination of signaling pathways affected by redox modifications.
Main Results:
- ROS/RNS mediate crucial post-translational modifications of signaling proteins.
- NO modulates protein function through heme addition (e.g., guanylate cyclase) and S-nitrosation.
- Oxidative lipid products react with cysteine residues, influencing adaptive responses.
Conclusions:
- Redox signaling, driven by ROS/RNS, significantly alters cellular pathway activity.
- The concept of 'redox tone' describes the overall impact of these modifications on signaling.
- Understanding these mechanisms is vital for comprehending cellular signal transduction.