Cachectin; TNF; TNF-alpha; TNFSF2; TNFα; TNF-α; Tumor Necrosis Factor; Tumor necrosis factor alpha; Tumor necrosis factor ligand superfamily member 2; Tumor Necrosis Factor-α
DefinitionThis section has been translated automatically.
Multifunctional proinflammatory cytokine involved in a central function in local and systemic inflammation. TNF-alpha is one of the best-studied representatives of the so-called TNF/TNFR superfamily, a cytokine system that plays a central role in the immune response and organogenesis, especially of the lymphatic system. It plays a central role in the pathogenesis of psoriasis and other inflammatory processes (Crohn's disease, arthritis; pathogenesis of contact allergy). It causes haemorrhagic necrosis in certain tumours.
General informationThis section has been translated automatically.
TNF-α exists biologically in soluble or transmembrane form. TNF-α molecules interact with at least 2 receptors (TNFRc-1 or TNFRc-2). The interaction of TNF-α with its receptors (especially TNFRc-1) activates signalling cascades which can lead to apoptosis (via caspase-8; see below caspases) and cell activation (via NF-κB) (see below transcription factors). The balance of antagonistic effects of both signal inductions depends on the cellular environment in which the stimulation by TNF-α takes place. Relevant for inflammation is the NF-κB mediated reaction, in the course of which pro-inflammatory enzymes such as interleukins (especially IL-6 and IL-8) are released.
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OccurrenceThis section has been translated automatically.
TNF-α is mainly produced and released by macrophages, but also by a large number of other cells such as lymphocytes, mast cells, endothelial cells, heart muscle cells, fibroblasts and neuronal tissue. Large amounts of TNF-α are released in response to bacterial products (e.g. lipopolysaccharides) and interleukin-1β. Formation is stimulated by Toll-like receptors and the MAP signalling pathway as well as NF-kappaB. It also has effects on lipid metabolism, blood clotting, insulin resistance and various endothelial functions.
TherapyThis section has been translated automatically.
Note(s)This section has been translated automatically.
TNF-α was already described in 1975 as a factor that led to tumor regression in bacterial diseases.
LiteratureThis section has been translated automatically.
- Alexis A et al (2005) Off-label dermatologic uses of anti-TNF-a therapies. J Cutan Med Surg 9: 296-302
- Wakefield PE, James WD et al (1991) Tumor necrosis factor. J Am Acad Dermatol 24: 675-685
- Carter PH et al (2001) Photochemically enhanced binding of small molecules to the tumor necrosis factor receptor-1 inhibits the binding of TNF-α. PNAS 98: 11879-11884
- Hehlgans, T et al (2005) The intriguing biology of the tumour necrosis factor/tumour necrosis factor receptor superfamily: players, rules and the games. Immunology 115: 1-20
- Seneschal J et al (2007) Psoriasiform drug eruptions under anti-TNF treatment of arthritis are not true psoriasis. Acta Derm Venereol 87: 77-80
- Tracey KJ (2002) The inflammatory reflex. Nature 420: 853-859