Redoxsignaler

Redoxsignaler is a term used in some scientific discussions to refer to molecules or protein components that convey information about the cellular redox state to signaling networks, acting as messengers in redox signaling. The concept emphasizes the transmitter role of redox-active species or redox-modified proteins within cellular communication pathways. Redox signaling arises from reversible oxidation-reduction events, particularly involving cysteine residues, as well as from small oxidants such as hydrogen peroxide. Redoxsignalers participate by sensing oxidative changes and relaying this information to effectors such as transcription factors, kinases, and metabolic enzymes.

Mechanistically, redoxsignaler function can involve reversible covalent modifications including thiol-disulfide exchange, S-nitrosylation, and S-glutathionylation, or changes in protein oligomerization and interaction patterns. These modifications can alter a protein’s activity, localization, or interactions, enabling downstream responses such as activation of transcription factors like Nrf2, modulation of kinase pathways, or shifts in metabolic control. Some components operate through redox relay systems, where an initial oxidative cue is propagated via a cascade of redox-active proteins, such as families that include peroxiredoxins and thioredoxins.

Examples and scope: while several proteins are recognized for redox-sensitive relay functions, the label redoxsignaler is not a fixed category with a single canonical member. Peroxiredoxins, thioredoxin, and related systems are frequently described as redox relays that propagate redox information. The term redoxsignaler is often used in conceptual discussions to highlight relay function rather than to designate a single molecule.

Relevance: understanding redoxsignaler concepts contributes to insights into physiology and disease, as dysregulated redox signaling is linked to aging, cancer, inflammation, and neurodegeneration. Related topics include redox signaling, reactive oxygen species, redox proteomics, and cysteine-based redox chemistry.