Interleukin-17 is a potent pro-inflammatory cytokine produced by activated memory T cells. There are at least six members of the IL-17 family in humans and in mice. As IL-17 shares properties with IL-1 and TNF-alpha; it may induce joint inflammation and bone and cartilage destruction. This cytokine is found in synovial fluids of patients with rheumatoid arthritis; and produced by rheumatoid arthritis synovium. It increases IL-6 production; induces collagen degradation and decreases collagen synthesis by synovium and cartilage and proteoglycan synthesis in cartilage. IL-17 is also able to increase bone destruction and reduce its formation. Blocking of interleukin-17 with specific inhibitors provides a protective inhibition of cartilage and bone degradation.
The Interleukin-17 family proteins, comprising six members (IL-17, IL-17B through IL-17F),are secreted, structurally related proteins that share a conserved cysteine-knot fold near the C-terminus, but have considerable sequence divergence at the N-terminus. IL-17 family proteins are proinflammatory cytokines that induce local cytokine production and are involved in the regulation of immune functions. Among IL-17 family members, IL-17D is most closely related to IL-17B, sharing 27% aa sequence homology. IL-17D is expressed preferentially in skeletal muscle, heart, adipose tissue, lung, pancreas, and nervous system. Like other IL-17 family members, IL-17D modulates immune responses indirectly by stimulating the production of myeloid growth factors and chemokines including IL-6, IL-8, and GM-CSF. IL-17D has also been shown to suppress the proliferation of myeloid progenitors in colony formation assays.
Interleukin-17 is a potent pro-inflammatory cytokine produced by activated memory T cells. There are at least six members of the IL-17 family in humans and in mice. Today; IL-17 represents a family of structurally related cytokines that share a highly conserved C-terminal region but differ from one another in their N-terminal regions and in their distinct biological roles. The six known members of this family; IL-17A through IL-17F; are secreted as homodimers. IL-17F also regulates cartilage matrix turnover and inhibits angiogenesis.
Interleukin-17F (IL-17F) exists in a disulfide-linked heterodimer that belongs to the IL-17 family. IL-17F is expressed in activated; but not resting; CD4+ T-cells and activated monocytes. IL-17F has been shown to stimulate the production of several other cytokines; including IL-6; IL-8; and granulocyte colony-stimulating factor. IL-17F can regulate cartilage matrix turnover and stimulates PBMC and T-cell proliferation. IL-17F is also found to inhibit the angiogenesis of endothelial cells and induce endothelial cells to produce IL2; TGFB1/TGFB; and monocyte chemoattractant protein-1. Defects in IL-17F are the cause of familial candidiasis type 6 (CANDF6).
Interleukin-18 is a secreted protein and it belongs to the IL-1 family. IL-18 is a proinflammatory cytokine and produced by macrophages and other cells. This cytokine can induce the IFN-gamma production of T cells. The combination of this cytokine and IL12 has been shown to inhibit IL-4 dependent IgE and IgG1 production; and enhance IgG2a production of B cells. IL-18 binding protein (IL18BP) can specifically interact with this cytokine; and thus negatively regulate its biological activity. After stimulation with IL-18; natural killer (NK) cells and certain T cells release another important cytokine called interferon-γ (IFN-γ) or type II interferon that plays an important role in activating the macrophages or other cells.
Inserisci la tua e-mail e seleziona le aree di interesse per ricevere le ultime novità, approfondimenti e promozioni.
Seleziona uno o piu ambiti di interesse per ricevere comunicazioni piu utili e mirate.
2025 TEMA Ricerca - All Rights Reserved.
