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Tumor necrosis factor alpha receptors (TNF receptors) are cell surface proteins that bind tumor necrosis factor alpha (TNF-α), a key cytokine involved in inflammation, immune regulation, and cell death. There are two main TNF-α receptors: TNFR1 (also known as p55 or CD120a) and TNFR2 (also known as p75 or CD120b). Both belong to the TNF receptor superfamily, which is characterized by extracellular cysteine-rich domains. TNFR1 contains a "death domain" critical for apoptotic signaling, while TNFR2 lacks this domain but can activate alternative pathways. TNF-alpha exists in two forms: transmembrane form (tmTNF) and soluble form (sTNF). Both forms can bind to both receptors, but with different affinities. Activation leads to diverse cellular outcomes including inflammation, cell survival, proliferation, differentiation, apoptosis or necroptosis depending on context and receptor balance. Dysregulation of TNF receptor signaling is implicated in chronic inflammatory diseases, autoimmune diseases, and neurodegenerative disorders. Therapeutic targeting of these pathways underlies several approved biologic drugs (anti-TNF agents).
Receptor antagonist; binds to TNF-alpha and prevents its interaction with TNF receptors.
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