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PMID:17132099
IaI family members
are captured on the cell surface through covalent
interactions between their heavy chains and hyaluronan
bound to CD44, a cell-surface receptor for hyaluronan
PMID:17132099
IaI family members
are captured on the cell surface through covalent
interactions between their heavy chains and hyaluronan
bound to CD44, a cell-surface receptor for hyaluronan
PMID: 17132099
IL-6 binds its cell surface receptor
PMID: 17132099, 7684902
Daveau et al. (1993) reported that IL-6 down-regulated
levels of H2 and AMBP mRNA and up-regulated
levels of H3 mRNA
PMID: 17132099, 7684902
Daveau et al. (1993) reported that IL-6 down-regulated
levels of H2 and AMBP mRNA and up-regulated
levels of H3 mRNA
indirect
PMID: 17132099, 7684902
Daveau et al. (1993) reported that IL-6 down-regulated
levels of H2 and AMBP mRNA and up-regulated
levels of H3 mRNA
indirect
PMID: 17132099
Cytokine expression
can be induced by transcription factors such as NFkB,
activating protein-1 (AP-1) and Egr-1, depending on
the cell type and stimulus
PMID: 17132099, 10801881
Two types of bikunin-binding proteins are expressed on the surface of some cells: a 40-kDa protein,
which is identical to Link protein, a hyaluronan-binding
protein (Kobayashi et al., 2000); and a 45-kDa, as yet
unidentified bikunin receptor.
PMID: 17132099
Two types of bikunin-binding proteins are expressed on the surface of some cells: a 40-kDa protein,
which is identical to Link protein, a hyaluronan-binding
protein (Kobayashi et al., 2000); and a 45-kDa, as yet
unidentified bikunin receptor.
PMID: 17132099, 15840581
More recent data demonstrated that bikunin interacts
with the Link module of TSG6 (Rugg et al., 2005), cathepsin
B (Liu et al., 2006), or the 41-aa C-terminal region of
the hepatitis E virus ORF3 protein (Tyagi et al., 2005)
PMID: 17132099, 16364318
More recent data demonstrated that bikunin interacts
with the Link module of TSG6 (Rugg et al., 2005), cathepsin
B (Liu et al., 2006), or the 41-aa C-terminal region of
the hepatitis E virus ORF3 protein (Tyagi et al., 2005)
PMID: 17132099, 16140784
More recent data demonstrated that bikunin interacts
with the Link module of TSG6 (Rugg et al., 2005), cathepsin
B (Liu et al., 2006), or the 41-aa C-terminal region of
the hepatitis E virus ORF3 protein (Tyagi et al., 2005
PMID: 17132099
In particular, TLR4
is part of a recognition complex for LPS.
indirect
PMID: 17132099, 11264657, 9916965, 12496270
bikunin inhibits
the LPS-induced increase in calcium influx (Onai and
Kudo, 2001), which triggers a signal that inactivates mitogen-
activated protein kinase kinase wMAPKK (MEK)x/
ERK1/2 and NF-kB, leading to suppression of
LPS-induced cytokine synthesis (Futamura et al., 1999;
Kobayashi et al., 2003);
indirect
PMID: 17132099, 11264657, 9916965, 12496270
bikunin inhibits
the LPS-induced increase in calcium influx (Onai and
Kudo, 2001), which triggers a signal that inactivates mitogen-
activated protein kinase kinase wMAPKK (MEK)x/
ERK1/2 and NF-kB, leading to suppression of
LPS-induced cytokine synthesis (Futamura et al., 1999;
Kobayashi et al., 2003);
indirect
PMID: 17132099, 11264657, 9916965, 12496270
bikunin inhibits
the LPS-induced increase in calcium influx (Onai and
Kudo, 2001), which triggers a signal that inactivates mitogen-
activated protein kinase kinase wMAPKK (MEK)x/
ERK1/2 and NF-kB, leading to suppression of
LPS-induced cytokine synthesis (Futamura et al., 1999;
Kobayashi et al., 2003);
PMID: 17132099, 11264657
bikunin
first directly interacts with bacterial toxins including
LPS, which enhances trapping of bacterial toxins (Onai
and Kudo, 2001);
PMID: 17132099, 10801881
bikunin interacts with activated inflammatory cell surfaces
via CD44-bound Link protein and/or unknown
components, and inactivates some membrane-bound
proteinases (Kobayashi et al., 2000);
PMID: 17132099, 10801881
bikunin interacts with activated inflammatory cell surfaces
via CD44-bound Link protein and/or unknown
components, and inactivates some membrane-bound
proteinases (Kobayashi et al., 2000);
indirect
PMID: 17132099, 15539418
ERK1/2 also phosphorylates
specific nuclear transcription factors
PMID: 17132099
Bikunin inhibits LPS-induced ERK1/2
activation by suppressing an increase in calcium influx,
leading to suppression of ERK1/2-induced activation of
transcription factors, including Egr-1.
indirect
PMID: 17132099, 15539418
ERK1/2 also phosphorylates
specific nuclear transcription factors
PMID: 17132099
Bikunin inhibits LPS-induced ERK1/2
activation by suppressing an increase in calcium influx,
leading to suppression of ERK1/2-induced activation of
transcription factors, including Egr-1.
indirect
PMID: 17132099, 15539418
ERK1/2 also phosphorylates
specific nuclear transcription factors
PMID: 17132099
Bikunin inhibits LPS-induced ERK1/2
activation by suppressing an increase in calcium influx,
leading to suppression of ERK1/2-induced activation of
transcription factors, including Egr-1.
indirect
PMID: 17132099, 15539418
ERK1/2 also phosphorylates
specific nuclear transcription factors
PMID: 17132099
Bikunin inhibits LPS-induced ERK1/2
activation by suppressing an increase in calcium influx,
leading to suppression of ERK1/2-induced activation of
transcription factors, including Egr-1.
indirect
PMID: 17132099, 11264657, 9916965, 12496270
bikunin inhibits
the LPS-induced increase in calcium influx (Onai and
Kudo, 2001), which triggers a signal that inactivates mitogen-
activated protein kinase kinase wMAPKK (MEK)x/
ERK1/2 and NF-kB, leading to suppression of
LPS-induced cytokine synthesis (Futamura et al., 1999;
Kobayashi et al., 2003);
indirect
PMID: 17132099, 11264657, 9916965, 12496270
bikunin inhibits
the LPS-induced increase in calcium influx (Onai and
Kudo, 2001), which triggers a signal that inactivates mitogen-
activated protein kinase kinase wMAPKK (MEK)x/
ERK1/2 and NF-kB, leading to suppression of
LPS-induced cytokine synthesis (Futamura et al., 1999;
Kobayashi et al., 2003);
PMID: 17132099
Cytokine expression
can be induced by transcription factors such as NFkB,
activating protein-1 (AP-1) and Egr-1, depending on
the cell type and stimulus
indirect
PMID: 17132099, 11264657, 9916965, 12496270
bikunin inhibits
the LPS-induced increase in calcium influx (Onai and
Kudo, 2001), which triggers a signal that inactivates mitogen-
activated protein kinase kinase wMAPKK (MEK)x/
ERK1/2 and NF-kB, leading to suppression of
LPS-induced cytokine synthesis (Futamura et al., 1999;
Kobayashi et al., 2003);
PMID: 17132099
Bikunin inhibits LPS-induced ERK1/2
activation by suppressing an increase in calcium influx,
leading to suppression of ERK1/2-induced activation of
transcription factors, including Egr-1
PMID: 17132099
Cytokine expression
can be induced by transcription factors such as NFkB,
activating protein-1 (AP-1) and Egr-1, depending on
the cell type and stimulus
indirect
PMID: 17132099
All the effects can
be explained on the basis that bikunin directly interacts
with LPS, inactivates the LPS receptor system, or blocks
calcium influx.
PMID: 17132009, 15576631, 15539418
It has previously been demonstrated that bikunin inhibits
the enhanced local expression or translation not only
of proinflammatory cytokines and chemokines, but also
of intercellular cell adhesion molecules (ICAM), inducible
nitric oxide synthase (iNOS) (Inoue et al., 2005), and tissue
factor (Molor-Erdene et al., 2005b).
PMID: 17132009, 15539418, 15576631
It has previously been demonstrated that bikunin inhibits
the enhanced local expression or translation not only
of proinflammatory cytokines and chemokines, but also
of intercellular cell adhesion molecules (ICAM), inducible
nitric oxide synthase (iNOS) (Inoue et al., 2005), and tissue
factor (Molor-Erdene et al., 2005b).
PMID: 17132009, 15576631, 15539418
It has previously been demonstrated that bikunin inhibits
the enhanced local expression or translation not only
of proinflammatory cytokines and chemokines, but also
of intercellular cell adhesion molecules (ICAM), inducible
nitric oxide synthase (iNOS) (Inoue et al., 2005), and tissue
factor (Molor-Erdene et al., 2005b).
indirect
PMID: 17132009, 15576631, 15539418
It has previously been demonstrated that bikunin inhibits
the enhanced local expression or translation not only
of proinflammatory cytokines and chemokines, but also
of intercellular cell adhesion molecules (ICAM), inducible
nitric oxide synthase (iNOS) (Inoue et al., 2005), and tissue
factor (Molor-Erdene et al., 2005b).
indirect
PMID: 17132009, 15576631, 15539418
It has previously been demonstrated that bikunin inhibits
the enhanced local expression or translation not only
of proinflammatory cytokines and chemokines, but also
of intercellular cell adhesion molecules (ICAM), inducible
nitric oxide synthase (iNOS) (Inoue et al., 2005), and tissue
factor (Molor-Erdene et al., 2005b).
indirect
PMID: 17132009, 15576631, 15539418
It has previously been demonstrated that bikunin inhibits
the enhanced local expression or translation not only
of proinflammatory cytokines and chemokines, but also
of intercellular cell adhesion molecules (ICAM), inducible
nitric oxide synthase (iNOS) (Inoue et al., 2005), and tissue
factor (Molor-Erdene et al., 2005b).
indirect
PMID: 17132009, 15576631, 15539418
It has previously been demonstrated that bikunin inhibits
the enhanced local expression or translation not only
of proinflammatory cytokines and chemokines, but also
of intercellular cell adhesion molecules (ICAM), inducible
nitric oxide synthase (iNOS) (Inoue et al., 2005), and tissue
factor (Molor-Erdene et al., 2005b).
PMID: 17132009, 15576631, 15539418
It has previously been demonstrated that bikunin inhibits
the enhanced local expression or translation not only
of proinflammatory cytokines and chemokines, but also
of intercellular cell adhesion molecules (ICAM), inducible
nitric oxide synthase (iNOS) (Inoue et al., 2005), and tissue
factor (Molor-Erdene et al., 2005b).
indirect
PMID: 17132009, 15576631, 15539418
It has previously been demonstrated that bikunin inhibits
the enhanced local expression or translation not only
of proinflammatory cytokines and chemokines, but also
of intercellular cell adhesion molecules (ICAM), inducible
nitric oxide synthase (iNOS) (Inoue et al., 2005), and tissue
factor (Molor-Erdene et al., 2005b).
PMID: 17132099
The STAT1 cascade is one of the major signaling
pathways converting the IFN-g signal into gene
expression, such as iNOS, COX, ICAM, and vascular cell
adhesion molecules (VCAM) critically involved in different
pathologies correlated to the inflammatory process.
indirect
PMID: 17132099
The STAT1 cascade is one of the major signaling
pathways converting the IFN-g signal into gene
expression, such as iNOS, COX, ICAM, and vascular cell
adhesion molecules (VCAM) critically involved in different
pathologies correlated to the inflammatory process.
indirect
PMID: 17132099
The STAT1 cascade is one of the major signaling
pathways converting the IFN-g signal into gene
expression, such as iNOS, COX, ICAM, and vascular cell
adhesion molecules (VCAM) critically involved in different
pathologies correlated to the inflammatory process.
indirect
PMID: 17132099
The STAT1 cascade is one of the major signaling
pathways converting the IFN-g signal into gene
expression, such as iNOS, COX, ICAM, and vascular cell
adhesion molecules (VCAM) critically involved in different
pathologies correlated to the inflammatory process.
indirect
PMID: 17132099
The STAT1 cascade is one of the major signaling
pathways converting the IFN-g signal into gene
expression, such as iNOS, COX, ICAM, and vascular cell
adhesion molecules (VCAM) critically involved in different
pathologies correlated to the inflammatory process.
indirect
PMID: 17132099
The STAT1 cascade is one of the major signaling
pathways converting the IFN-g signal into gene
expression, such as iNOS, COX, ICAM, and vascular cell
adhesion molecules (VCAM) critically involved in different
pathologies correlated to the inflammatory process.
PMID: 17132099, 15840581
This reaction seems to be mediated by tumor
necrosis factor-a-stimulated gene-6 (TSG6), a protein
secreted by various cells upon stimulation by inflammatory
cytokines, since IaI is known to bind TSG6 (Rugg et
al., 2005).
indirect
PMID: 17132099, 9703243
It has also been reported that IaI is digested by human
neutrophil elastase to release bikunin (Hirose et al., 1998)
PMID: 17132099
The two predominant forms of bikunin, IaI, which consists of two heavy chains (H1 and H2) and a single bikunin
indirect
PMID: 17132099, 16452202
Furthermore, H2 of IaI down-regulates
protein kinase B (PKB/Akt) phosphorylation (Werbowetski-
Ogilvie et al., 2006; Figure 1).
indirect
PMID: 17132099
here we review
the literature reporting that bikunin decreases the production
of cytokines (TNF-a, IL-1b, IL-6, or IL-8) in cultures
containing inflammatory, cells as well as in animal
and human models.
indirect
PMID: 17132099
here we review
the literature reporting that bikunin decreases the production
of cytokines (TNF-a, IL-1b, IL-6, or IL-8) in cultures
containing inflammatory, cells as well as in animal
and human models.
indirect
PMID: 17132099
here we review
the literature reporting that bikunin decreases the production
of cytokines (TNF-a, IL-1b, IL-6, or IL-8) in cultures
containing inflammatory, cells as well as in animal
and human models.
indirect
PMID: 17132099
here we review
the literature reporting that bikunin decreases the production
of cytokines (TNF-a, IL-1b, IL-6, or IL-8) in cultures
containing inflammatory, cells as well as in animal
and human models.
PMID: 17132009, 15576631, 15539418
It has previously been demonstrated that bikunin inhibits
the enhanced local expression or translation not only
of proinflammatory cytokines and chemokines, but also
of intercellular cell adhesion molecules (ICAM), inducible
nitric oxide synthase (iNOS) (Inoue et al., 2005), and tissue
factor (Molor-Erdene et al., 2005b).
PMID: 17132099, 10801881
bikunin interacts with activated inflammatory cell surfaces
via CD44-bound Link protein and/or unknown
components, and inactivates some membrane-bound
proteinases (Kobayashi et al., 2000);
PMID: 17132099, 10801881
bikunin interacts with activated inflammatory cell surfaces
via CD44-bound Link protein and/or unknown
components, and inactivates some membrane-bound
proteinases (Kobayashi et al., 2000);
indirect
PMID: 17132099, 10801881
bikunin interacts with activated inflammatory cell surfaces
via CD44-bound Link protein and/or unknown
components, and inactivates some membrane-bound
proteinases (Kobayashi et al., 2000);
indirect
PMID: 17132099, 10801881
bikunin interacts with activated inflammatory cell surfaces
via CD44-bound Link protein and/or unknown
components, and inactivates some membrane-bound
proteinases (Kobayashi et al., 2000);