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The IL-5 receptor is composed of an α and a βc chain. [23] The α subunit is specific for the IL-5 molecule, whereas the βc subunit also recognised by interleukin 3 (IL-3) and granulocyte-macrophage colony-stimulating factor (GM-CSF). [23] [24] Glycosylation of the Asn196 residue of the Rα subunit appears to be essential for binding of IL-5 ...
Studies have reported that humans express FFAR3 in their: a) enteroendocrine L cells and K cells of the intestines; [10] b) endothelium of blood vessels in the frontal cortex of the brain, [34] pancreatic β-cells, [35] and adipose. i.e., fat, tissue (but not in mouse adipose tissue); [36] c) the vascular endothelium of the myometrium, the epithelium of the amnion, chorion and placenta, and ...
Interleukin 3 (IL3) is a cytokine that regulates hematopoiesis by controlling the production, differentiation and function of granulocytes and macrophages. [ 15 ] [ 16 ] The protein, which exists in vivo as a monomer, is produced in activated T cells and mast cells, [ 15 ] [ 16 ] and is activated by the cleavage of an N-terminal signal sequence.
Inflammatory cytokines play a role in initiating the inflammatory response and to regulate the host defence against pathogens mediating the innate immune response. [4] Some inflammatory cytokines have additional roles such as acting as growth factors. [5] Pro-inflammatory cytokines such as IL-1β, IL-6, and TNF-α also trigger pathological pain ...
The inflammasome was discovered by the team of Jürg Tschopp, at the University of Lausanne, in 2002. [17] [18] In 2002, it was first reported by Martinon et al. [17] that NLRP1 (NLR family PYD-containing 1) could assemble and oligomerize into a structure in vitro, which activated the caspase-1 cascade, thereby leading to the production of pro-inflammatory cytokines, including IL-1β and IL-18.
Type I cytokine receptors are transmembrane receptors expressed on the surface of cells that recognize and respond to cytokines with four α-helical strands. These receptors are also known under the name hemopoietin receptors, and share a common amino acid motif in the extracellular portion adjacent to the cell membrane.
STAT6 is activated by cytokines interleukin-4 (IL-4), and interleukin-13 (IL-13) with their receptors that both contain the α subunit of the IL-4 receptor (IL-4Rα). [8] Tyrosine phosporylation of STAT6 after stimulation by IL-4 results in the formation of STAT6 homodimers that bind specific DNA elements via a DNA-binding domain. [5] [9]
Cytokine redundancy is a term in immunology referring to the phenomenon in which, and the ability of, multiple cytokines to exert similar actions. This phenomenon is largely due to multiple cytokines utilizing common receptor subunits and common intracellular cell signalling molecules / pathways .