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</svg>
PMID: 10534111
LPS binds its receptor TLR4.
indirect
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].
indirect
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.
indirect
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.
indirect
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].
indirect
indirect
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, 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].
indirect
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
IL-10 binds its corresponding receptor.
indirect
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].
indirect
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].
indirect
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].
indirect
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].
indirect
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].
indirect
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].
indirect
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.
indirect
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.
indirect
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].
indirect
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.