Interleukin-11 (IL-11) is a pleiotropic cytokine in the IL-6 family, which also includes LIF, CNTF, Oncostatin M, Cardiotrophin-1, IL-27 and IL-31 [1-3]. In humans, IL-11 was also independently discovered as an adipogenesis inhibitory factor (AGIF) [3]. The human IL-11 cDNA encodes a 199 amino acid (aa) precursor, which generates a 178 aa, 19 kDa mature unglycosylated protein. Mature human IL-11 shares 88%, 88%, and 96% aa sequence identity with mouse, rat and canine IL-11, respectively. IL-11 is secreted by osteoblasts, synoviocytes, fibroblasts, chondrocytes, intestinal myofibroblasts, and trophoblasts, among other cell types [1]. It is found in the plasma mainly during inflammation, such as that associated with viral infection, cancer, or inflammatory arthritis, and is considered to be primarily anti-inflammatory [1]. It stimulates hematopoiesis and thrombopoiesis, regulates macrophage differentiation, and confers mucosal protection in the intestine [1]. It has also been found to enhance T cell polarization toward Th2, promote B cell IgG production, increase osteoclast bone absorption, protect endothelial cells from oxidative stress, and regulate epithelial proliferation and apoptosis [1]. IL-11 synergizes with several other cytokines to produce these effects, and its effects overlap with those of IL-6 [1]. IL-11 receptor activation requires formation of a complex of two IL-11 molecules with two molecules of the ligand-binding IL-11 R alpha subunit and two molecules of the ubiquitously expressed cell signaling beta subunit, gp130 [4]. A soluble form of IL-11 R alpha can bind IL-11 and either form a signaling complex with gp130 on the cell surface, or inhibit cell surface IL-11 R alpha /gp130 signaling [5-7].
Reference
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