PMID: 10534111 LPS binds its receptor TLR4.

PMID: 10534111, 8910586, 9013879 The IL-13Ra1 chain has weak IL-13 binding capacity on its own but binds IL-13 strongly on complexing with the IL-4Ra chain [26, 27].

PMID: 10534111, 8910586, 9013879 The IL-13Ra1 chain has weak IL-13 binding capacity on its own but binds IL-13 strongly on complexing with the IL-4Ra chain [26, 27].

PMID: 10534111 For IL-13, the second bound receptor chain (IL-4Ra) functions to recruit JAK1 to the receptor complex, and to provide a docking site for STAT6 on its intracellular domain and thus provides a mechanism by which the biological effects of IL-4 and IL-13 on monocytes are very similar.

PMID: 10534111 For IL-13, the second bound receptor chain (IL-4Ra) functions to recruit JAK1 to the receptor complex, and to provide a docking site for STAT6 on its intracellular domain and thus provides a mechanism by which the biological effects of IL-4 and IL-13 on monocytes are very similar.

PMID: 10534111, 9573026 There is strong evidence particularly on non-hematopoietic cells that the IL-4Ra chain on binding to IL-4 can heterodimerize with the IL-13Ra1 chain forming the type II IL-4 receptor [28].

PMID: 10534111, 8663118 A second IL-13-specific receptor chain, IL-13Ra2, has been cloned from a human renal carcinoma cell line and binds IL-13 with much higher affinity [29].

PMID: 10534111, 9558115, 10427971 The loss of IL-4- and IL-13-induced STAT6 activation with monocyte differentiation was unique because STATs activated by IFN-g, GM-CSF, and IL-10 were not altered with monocyte culture [16, 17].

PMID: 10534111, 9558115, 10427971 The loss of IL-4- and IL-13-induced STAT6 activation with monocyte differentiation was unique because STATs activated by IFN-g, GM-CSF, and IL-10 were not altered with monocyte culture [16, 17].

PMID: 10534111 IFN-gamma binds its corresponding receptor.

PMID: 10534111 GM-CSF binds its corresponding receptor.

PMID: 10534111, 2786204, 2120129, 2785566, 9558115, 10427971, 9558115, 10427971 2114443 IL-4 inhibited the production of lipopolysaccharide (LPS)-stimulated tumor necrosis factor a (TNF-a), IL-1b, IL-6, IL-10, and prostaglandin E2 (PGE2) [1?4] by monocytes and this regulation occurred for the peptides, at least in part, at the mRNA level. Furthermore, in kinetic studies of mRNA levels for gc and IL-13Ra1 with increasing time of culture for monocytes, as mRNA levels were reduced so too was the ability of IL-4 and IL-13 to suppress LPS-induced TNF-a production [16, 17].

PMID: 10534111 IL-10 binds its corresponding receptor.

PMID: 10534111, 9558115, 10427971 The loss of IL-4- and IL-13-induced STAT6 activation with monocyte differentiation was unique because STATs activated by IFN-g, GM-CSF, and IL-10 were not altered with monocyte culture [16, 17].

PMID: 10534111, 9558115, 10427971 The loss of IL-4- and IL-13-induced STAT6 activation with monocyte differentiation was unique because STATs activated by IFN-g, GM-CSF, and IL-10 were not altered with monocyte culture [16, 17].

PMID: 10534111, 9558115, 10427971 The loss of IL-4- and IL-13-induced STAT6 activation with monocyte differentiation was unique because STATs activated by IFN-g, GM-CSF, and IL-10 were not altered with monocyte culture [16, 17].

PMID: 10534111, 9558115, 10427971 Furthermore, in kinetic studies of mRNA levels for gc and IL-13Ra1 with increasing time of culture for monocytes, as mRNA levels were reduced so too was the ability of IL-4 and IL-13 to suppress LPS-induced TNF-a production [16, 17].

PMID: 10534111, 10227996 It was recently shown that IL-4 could regulate TNF-a and IL-12 production by IFN-g-activated murine bone marrow-derived macrophages from STAT6-/- mice [31].

PMID: 10534111, 10227996 It was recently shown that IL-4 could regulate TNF-a and IL-12 production by IFN-g-activated murine bone marrow-derived macrophages from STAT6-/- mice [31].

PMID: 10534111 First, a neutralizing antibody to gc blocked IL-4 regulation of LPSinduced TNF-a, but not IL-1b, production.

PMID: 10534111 Second, a mutant IL-4 molecule that was able to bind the IL-4Ra chain but not gc suppressed LPS-induced monocyte IL-1b, but not TNF-a, production.

PMID: 10534111 Second, a mutant IL-4 molecule that was able to bind the IL-4Ra chain but not gc suppressed LPS-induced monocyte IL-1b, but not TNF-a, production.

PMID: 10534111, 2786204, 2120129, 2785566, 2114443 IL-4 inhibited the production of lipopolysaccharide (LPS)-stimulated tumor necrosis factor a (TNF-a), IL-1b, IL-6, IL-10, and prostaglandin E2 (PGE2) [1?4] by monocytes and this regulation occurred for the peptides, at least in part, at the mRNA level.

PMID: 10534111, 10427971 From studies using an antibody to the IL-4Ra chain, we know that this chain is a component of the receptor by which IL-4 and IL-13 signal suppression of LPS-induced IL-1b production by MDMac [17].

PMID: 10534111, 2786204, 2120129, 2785566, 9558115, 10427971, 9558115, 10427971 2114443 IL-4 inhibited the production of lipopolysaccharide (LPS)-stimulated tumor necrosis factor a (TNF-a), IL-1b, IL-6, IL-10, and prostaglandin E2 (PGE2) [1?4] by monocytes and this regulation occurred for the peptides, at least in part, at the mRNA level.

PMID: 10534111, 2786204, 2120129, 2785566, 2114443 IL-4 inhibited the production of lipopolysaccharide (LPS)-stimulated tumor necrosis factor a (TNF-a), IL-1b, IL-6, IL-10, and prostaglandin E2 (PGE2) [1?4] by monocytes and this regulation occurred for the peptides, at least in part, at the mRNA level.

PMID: 10534111, 2786204, 2120129, 2785566, 2114443 IL-4 inhibited the production of lipopolysaccharide (LPS)-stimulated tumor necrosis factor a (TNF-a), IL-1b, IL-6, IL-10, and prostaglandin E2 (PGE2) [1?4] by monocytes and this regulation occurred for the peptides, at least in part, at the mRNA level.

PMID: 10534111, 9573026 It is believed that a site within the A/C helices of IL-4 first binds the IL-4Ra chain with high affinity. A site located near the end of helix D then binds gc, creating an active receptor dimer; mutations of the tyrosine at position 124 greatly reduces this interaction. There is strong evidence particularly on non-hematopoietic cells that the IL-4Ra chain on binding to IL-4 can heterodimerize with the IL-13Ra1 chain forming the type II IL-4 receptor [28].

PMID: 10534111 It is believed that a site within the A/C helices of IL-4 first binds the IL-4Ra chain with high affinity. A site located near the end of helix D then binds gc, creating an active receptor dimer; mutations of the tyrosine at position 124 greatly reduces this interaction.

PMID: 10534111, 7843245 Western blots of gc on monocytes suggested proteins of 58 and 64 kDa but only the 64 kDa protein could associate with the IL-2Rb chain [23].

PMID: 10534111, 2786204, 2120129, 2785566, 2114443 IL-4 inhibited the production of lipopolysaccharide (LPS)-stimulated tumor necrosis factor a (TNF-a), IL-1b, IL-6, IL-10, and prostaglandin E2 (PGE2) [1?4] by monocytes and this regulation occurred for the peptides, at least in part, at the mRNA level.