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PMID: 17470533, 15173835, 11150311, 11781369
TLRs signal the presence, not only of microbe-associated molecular patterns but also of a variety of structures generated or unmasked during tissue injury and inflammation—damage-associated molecular patterns [35 ]. These include degradation products of endogenous tissue matrix macromolecules (e.g., hyaluronan fragments and heparan sulfate), endogenous molecules whose expression is up-regulated during injury or inflammation (e.g., fibronectin extra domain A, and β-defensin 2), molecules released by necrotic cells [e.g., high mobility group box 1 (HMGB1), heat shock proteins (HSPs), and chromatin/Ig complexes], and molecules altered by oxidation (e.g., minimally oxidized LDL).
PMID: 17470533, 15173835, 11150311, 11781369
TLRs signal the presence, not only of microbe-associated molecular patterns but also of a variety of structures generated or unmasked during tissue injury and inflammation—damage-associated molecular patterns [35 ]. These include degradation products of endogenous tissue matrix macromolecules (e.g., hyaluronan fragments and heparan sulfate), endogenous molecules whose expression is up-regulated during injury or inflammation (e.g., fibronectin extra domain A, and β-defensin 2), molecules released by necrotic cells [e.g., high mobility group box 1 (HMGB1), heat shock proteins (HSPs), and chromatin/Ig complexes], and molecules altered by oxidation (e.g., minimally oxidized LDL).
PMID: 17470533, 15173835, 11150311, 11781369
TLRs signal the presence, not only of microbe-associated molecular patterns but also of a variety of structures generated or unmasked during tissue injury and inflammation—damage-associated molecular patterns [35 ]. These include degradation products of endogenous tissue matrix macromolecules (e.g., hyaluronan fragments and heparan sulfate), endogenous molecules whose expression is up-regulated during injury or inflammation (e.g., fibronectin extra domain A, and β-defensin 2), molecules released by necrotic cells [e.g., high mobility group box 1 (HMGB1), heat shock proteins (HSPs), and chromatin/Ig complexes], and molecules altered by oxidation (e.g., minimally oxidized LDL).
PMID: 17470533, 15173835, 11150311, 11781369
TLRs signal the presence, not only of microbe-associated molecular patterns but also of a variety of structures generated or unmasked during tissue injury and inflammation—damage-associated molecular patterns [35 ]. These include degradation products of endogenous tissue matrix macromolecules (e.g., hyaluronan fragments and heparan sulfate), endogenous molecules whose expression is up-regulated during injury or inflammation (e.g., fibronectin extra domain A, and β-defensin 2), molecules released by necrotic cells [e.g., high mobility group box 1 (HMGB1), heat shock proteins (HSPs), and chromatin/Ig complexes], and molecules altered by oxidation (e.g., minimally oxidized LDL).
PMID: 17470533, 15173835, 11150311, 11781369
TLRs signal the presence, not only of microbe-associated molecular patterns but also of a variety of structures generated or unmasked during tissue injury and inflammation—damage-associated molecular patterns [35 ]. These include degradation products of endogenous tissue matrix macromolecules (e.g., hyaluronan fragments and heparan sulfate), endogenous molecules whose expression is up-regulated during injury or inflammation (e.g., fibronectin extra domain A, and β-defensin 2), molecules released by necrotic cells [e.g., high mobility group box 1 (HMGB1), heat shock proteins (HSPs), and chromatin/Ig complexes], and molecules altered by oxidation (e.g., minimally oxidized LDL).
PMID: 17470533, 15173835, 11150311, 11781369
TLRs signal the presence, not only of microbe-associated molecular patterns but also of a variety of structures generated or unmasked during tissue injury and inflammation—damage-associated molecular patterns [35 ]. These include degradation products of endogenous tissue matrix macromolecules (e.g., hyaluronan fragments and heparan sulfate), endogenous molecules whose expression is up-regulated during injury or inflammation (e.g., fibronectin extra domain A, and β-defensin 2), molecules released by necrotic cells [e.g., high mobility group box 1 (HMGB1), heat shock proteins (HSPs), and chromatin/Ig complexes], and molecules altered by oxidation (e.g., minimally oxidized LDL).
PMID: 17470533, 15173835, 11150311, 11781369
TLRs signal the presence, not only of microbe-associated molecular patterns but also of a variety of structures generated or unmasked during tissue injury and inflammation—damage-associated molecular patterns [35 ]. These include degradation products of endogenous tissue matrix macromolecules (e.g., hyaluronan fragments and heparan sulfate), endogenous molecules whose expression is up-regulated during injury or inflammation (e.g., fibronectin extra domain A, and β-defensin 2), molecules released by necrotic cells [e.g., high mobility group box 1 (HMGB1), heat shock proteins (HSPs), and chromatin/Ig complexes], and molecules altered by oxidation (e.g., minimally oxidized LDL).
PMID: 17470533, 15173835, 11150311, 11781369
TLRs signal the presence, not only of microbe-associated molecular patterns but also of a variety of structures generated or unmasked during tissue injury and inflammation—damage-associated molecular patterns [35 ]. These include degradation products of endogenous tissue matrix macromolecules (e.g., hyaluronan fragments and heparan sulfate), endogenous molecules whose expression is up-regulated during injury or inflammation (e.g., fibronectin extra domain A, and β-defensin 2), molecules released by necrotic cells [e.g., high mobility group box 1 (HMGB1), heat shock proteins (HSPs), and chromatin/Ig complexes], and molecules altered by oxidation (e.g., minimally oxidized LDL).
PMID: 17470533
Such B cell proliferation is associated with increased expression of MHC Class II, CD80, and CD86.
PMID: 17470533
Such B cell proliferation is associated with increased expression of MHC Class II, CD80, and CD86.
PMID: 17470533
Such B cell proliferation is associated with increased expression of MHC Class II, CD80, and CD86.
Indirect
Indirect
Indirect
PMID: 17470533
Such B cell proliferation is associated with increased expression of MHC Class II, CD80, and CD86.
PMID: 17470533, 8691124, 9653087
The proliferative response is inhibited by subsequent cross-linking of sIgM, which induces B cell growth arrest and apoptosis.
PMID: 17470533, 12960171
LPS has been shown to bind directly to MD-2, leading to the association of LPS/MD-2 complexes with TLR4, and to TLR4 signaling.
PMID: 17470533
This suggests the possibility that when TLR4–MD-2 is highly expressed (e.g., on myeloid cells), lower affinity, heterodimeric interactions inhibit TLR4 multimerization and signaling.
PMID: 17470533, 15852007
Notably, coexpression of RP105–MD-1 in this system inhibits LPS–TLR4–MD-2 complex formation, providing direct evidence that RP105–MD-1 inhibits LPS signaling complex formation.
PMID: 17470533, 15852007
Although TLR4–MD-2 would be expected to have a higher affinity for homodimerization than for heterodimerization with RP105–MD-1, our data suggest the likelihood that homo- and heterodimers can multimerize with further TLR4–MD-2 complexes.
PMID: 17470533
This suggests the possibility that when TLR4–MD-2 is highly expressed (e.g., on myeloid cells), lower affinity, heterodimeric interactions inhibit TLR4 multimerization and signaling.
PMID: 17470533, 15852007
Although TLR4–MD-2 would be expected to have a higher affinity for homodimerization than for heterodimerization with RP105–MD-1, our data suggest the likelihood that homo- and heterodimers can multimerize with further TLR4–MD-2 complexes.
PMID; 17470533, 15852007
These complexes co-IP bidirectionally, demonstrating physical association between TLR4–MD-2 and RP105–MD-1. Of note, MD-1 and MD-2 also co-IP bidirectionally when expressed alone, suggesting that MD-1–MD-2 heterodimerization provides the point of contact between TLR4–MD-2 and RP105–MD-1
Indirect
PMID: 17470533
LPS-induced B cell proliferation is dependent on TLR4.
PMID: 17470533
Using genetic models, we have also shown that RP105 regulates LPS-driven TLR4 signaling in primary mouse DC and macrophages, inhibiting the production of cytokines dependent on both MAL/MyD88 and TRIF/TRIF pathways.
PMID: 17470533
Using genetic models, we have also shown that RP105 regulates LPS-driven TLR4 signaling in primary mouse DC and macrophages, inhibiting the production of cytokines dependent on both MAL/MyD88 and TRIF/TRIF pathways.
PMID: 17470533
Using genetic models, we have also shown that RP105 regulates LPS-driven TLR4 signaling in primary mouse DC and macrophages, inhibiting the production of cytokines dependent on both MAL/MyD88 and TRIF/TRIF pathways.
PMID: 17470533
Using genetic models, we have also shown that RP105 regulates LPS-driven TLR4 signaling in primary mouse DC and macrophages, inhibiting the production of cytokines dependent on both MAL/MyD88 and TRIF/TRIF pathways.
Indirect
Indirect
PMID: 17470533
Using genetic models, we have also shown that RP105 regulates LPS-driven TLR4 signaling in primary mouse DC and macrophages, inhibiting the production of cytokines dependent on both MAL/MyD88 and TRIF/TRIF pathways.
Indirect
Indirect
PMID: 17470533
Using genetic models, we have also shown that RP105 regulates LPS-driven TLR4 signaling in primary mouse DC and macrophages, inhibiting the production of cytokines dependent on both MAL/MyD88 and TRIF/TRIF pathways.
PMID: 17470533, 8691124, 9653087
The proliferative response is inhibited by subsequent cross-linking of sIgM, which induces B cell growth arrest and apoptosis.
PMID: 17470533, 8691124, 9653087
The proliferative response is inhibited by subsequent cross-linking of sIgM, which induces B cell growth arrest and apoptosis.
Indirect
PMID: 17470533, 12714520, 9653087
Anti-RP105-mediated B cell proliferation appears to involve signaling through the Lyn/CD19/Vav complex, along with protein kinase CI/II and the Erk2-specific MAPK kinase, MEK.
Indirect
PMID: 17470533, 12714520, 9653087
Anti-RP105-mediated B cell proliferation appears to involve signaling through the Lyn/CD19/Vav complex, along with protein kinase CI/II and the Erk2-specific MAPK kinase, MEK.
Indirect
Indirect
Indirect
PMID: 17470533, 12714520, 9653087
Anti-RP105-mediated B cell proliferation appears to involve signaling through the Lyn/CD19/Vav complex, along with protein kinase CI/II and the Erk2-specific MAPK kinase, MEK.
Indirect
Indirect
PMID: 17470533, 16951340
Similarly, MZB cells are "primed" to secrete IgM rapidly in response to LPS stimulation; FOB cells take several days for this secretory response to become evident.
Indirect
PMID: 17470533, 12714520, 9653087
Anti-RP105-mediated B cell proliferation appears to involve signaling through the Lyn/CD19/Vav complex, along with protein kinase CI/II and the Erk2-specific MAPK kinase, MEK.