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・ Interleukin 1 receptor, type II
・ Interleukin 10
・ Interleukin 10 receptor, alpha subunit
・ Interleukin 10 receptor, beta subunit
・ Interleukin 11
・ Interleukin 11 receptor alpha subunit
・ Interleukin 12
・ Interleukin 12 receptor, beta 1 subunit
・ Interleukin 12 receptor, beta 2 subunit
・ Interleukin 12 subunit beta
・ Interleukin 13
・ Interleukin 13 receptor, alpha 1
・ Interleukin 15
・ Interleukin 15 receptor, alpha subunit
・ Interleukin 16
Interleukin 17
・ Interleukin 18
・ Interleukin 19
・ Interleukin 2
・ Interleukin 20
・ Interleukin 20 receptor, alpha subunit
・ Interleukin 20 receptor, beta subunit
・ Interleukin 21
・ Interleukin 22
・ Interleukin 23
・ Interleukin 23 subunit alpha
・ Interleukin 24
・ Interleukin 25
・ Interleukin 26
・ Interleukin 27


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Interleukin 17 : ウィキペディア英語版
Interleukin 17

Interleukin 17A (IL-17 or IL-17A), originally identified as a transcript from a rodent T-cell hybridoma by Rouvier ''et al.'' in 1993, is the founding member of a group of cytokines called the IL-17 family. Known as CTLA8 in rodents, IL-17 shows high homology to viral IL-17 encoded by an open reading frame of the T-lymphotropic rhadinovirus ''Herpesvirus saimiri''.
Interleukin 17 is a cytokine that acts as a potent mediator in delayed-type reactions by increasing chemokine production in various tissues to recruit monocytes and neutrophils to the site of inflammation, similar to Interferon gamma. IL-17 is produced by T-helper cells and is induced by IL–23 which results in destructive tissue damage in delayed-type reactions. Interleukin 17 as a family functions as a proinflammatory cytokine that responds to the invasion of the immune system by extracellular pathogens and induces destruction of the pathogen’s cellular matrix. Interleukin 17 acts synergistically with tumor necrosis factor and interleukin-1.
To elicit its functions, IL-17 binds to a type I cell surface receptor called IL-17R of which there are at least three variants IL17RA, IL17RB, and IL17RC.
== Family members ==
In addition to IL-17A, members of the IL-17 family include IL-17B, IL-17C, IL-17D, IL-17E (also called IL-25), and IL-17F. All members of the IL-17 family have a similar protein structure, with four highly conserved cysteine residues critical to their 3-dimensional shape, yet they have no sequence similarity to any other known cytokines. Phylogenetic analysis reveals that among IL-17 family members, the IL-17F isoforms 1 and 2 (ML-1) have the highest homology to IL-17A (sharing 55 and 40% amino acid identity to IL-17A respectively), followed by IL-17B (29%), IL-17D (25%), IL-17C (23%), and IL-17E being most distantly related to IL-17A (17%). These cytokines are all well conserved in mammals, with as much as 62–88% of amino acids conserved between the human and mouse homologs.

抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)
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