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NO</text>
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PMID: 11890659
The guanylyl cyclases NPR-A and NPR-B contain an extracellular, ligand binding domain whereby NPR-A binds ANP and BNP.
PMID: 11890659
The guanylyl cyclases NPR-A and NPR-B contain an extracellular, ligand binding domain whereby NPR-A binds ANP and BNP.
PMID: 11890659
NPR-B binds CNP.
PMID: 11890659
NPR-C has the potency to internalise and clear the natriuretic
peptides.
PMID: 11890659
NPR-C has the potency to internalise and clear the natriuretic
peptides.Moreover, an increasing number
of reports show that several biological effects of
ANP are mediated through this “clearance”
receptor (NPR-C).
PMID: 11890659
NPR-C has the potency to internalise and clear the natriuretic
peptides.
PMID: 11890659
NPR-C has the potency to internalise and clear the natriuretic
peptides.
PMID: 11890659
NPR-C has the potency to internalise and clear the natriuretic peptides
PMID: 11890659
NPR-C has the potency to internalise and clear the natriuretic
peptides.
PMID: 11890659
NPR-C has the potency to internalise and clear the natriuretic peptides
PMID: 11890659
NPR-C has the potency to internalise and clear the natriuretic
peptides.
PMID: 11890659
NPR-C has the potency to internalise and clear the natriuretic peptides
PMID: 11890659, 8532063, 10865843
In the organism nitric oxide is synthesised by nitric oxide synthases (NOS) from the amino acid L-arginine. Two constitutive nitric oxide synthases,
the endothelial NOS (eNOS, NOS I) and the neuronal NOS (nNOS; NOS III), produce NO that mainly serves as vasodilator.
PMID: 11890659, 8532063, 10865843
In the organism nitric oxide is synthesised by nitric oxide synthases (NOS) from the amino acid L-arginine. Two constitutive nitric oxide synthases,
the endothelial NOS (eNOS, NOS I) and the neuronal NOS (nNOS; NOS III), produce NO that mainly serves as vasodilator.
PMID: 11890659, 8532063, 9303203
NO produced by the inducible isoform of the enzyme (iNOS) is an important mediator of host defence.
PMID: 11890659, 8532063, 1429562
Induction occurs after exposure of cells to cytokines and bacterial products, such
as lipopolysaccharides (LPS).
indirect
PMID: 11890659, 8532063, 1429562
Induction occurs after exposure of cells to cytokines and bacterial products, such as lipopolysaccharides (LPS).
indirect
PMID: 11890659, 9593677, 11257311
ANP was shown to inhibit markedly the activation of the transcription factor NF-kappaB.
The LPS-induced expression of TNF-alpha is inhibited by ANP through binding to the NPR-A. The
inhibitory action involves transcriptional processes with a reduced activation of NF-kappaB and AP1.
PMID: 11890659, 7508926
ANP was shown to inhibit markedly the activation of the transcription factor NF-kappaB which is crucial for the induction of iNOS in
murine macrophages.
PMID: 11890659, 1429562
TNF-alpha is a central proinflammatory cytokine and is regulated transcriptionally; the two
transcription factors NF-kappaB and AP1 are involved.
indirect
PMID: 11890659, 10861050
Besides the reduced activation of NF-kappaB, ANP markedly inhibited AP1 activity
in LPS activated macrophages.
PMID: 11890659, 1429562
TNF-alpha is a central proinflammatory cytokine and is regulated transcriptionally; the two
transcription factors NF-kappaB and AP1 are involved.
indirect
PMID: 11890659, 11257311
The inhibitory action of ANP on the interferon-gamma mediated activation of the p38 mitogen activated protein kinase was suggested
to be the upstream step responsible for the attenuated activation of NF-kappaB in macrophages.
PMID: 11890659, 11257311
The inhibitory action of ANP on the interferon-gamma mediated activation of the p38 mitogen activated protein kinase was suggested
to be the upstream step responsible for the attenuated activation of NF-kappaB in macrophages.
indirect
PMID: 11890659, 7508926
ANP was shown to inhibit markedly the activation of the transcription factor NF-kappaB,
which is crucial for the induction of iNOS in murine macrophages.