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024 7 |a 10.1016/j.clim.2010.06.011  |2 doi 
028 5 2 |a pubmed24n0665.xml 
035 |a (DE-627)NLM199612080 
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040 |a DE-627  |b ger  |c DE-627  |e rakwb 
041 |a eng 
100 1 |a Marron, Thomas U  |e verfasserin  |4 aut 
245 1 0 |a TLR signaling and effector functions are intact in XLA neutrophils 
264 1 |c 2010 
336 |a Text  |b txt  |2 rdacontent 
337 |a ƒaComputermedien  |b c  |2 rdamedia 
338 |a ƒa Online-Ressource  |b cr  |2 rdacarrier 
500 |a Date Completed 07.12.2010 
500 |a Date Revised 23.02.2022 
500 |a published: Print-Electronic 
500 |a Citation Status MEDLINE 
520 |a Copyright © 2010 Elsevier Inc. All rights reserved. 
520 |a Toll-like receptors (TLRs) are essential components of the innate immune system, and their ligands are important activators of neutrophils. Bruton's tyrosine kinase (Btk) has been reported to mediate signaling through toll-like receptors (TLRs) in many cell types, however, the role of Btk in TLR activation of neutrophils remains unclear. Impaired TLR-induced neutrophil function was found in mice with loss of Btk and in humans with TLR-signaling defects, but the integrity of TLR pathways in X-linked agammaglobulinemia (XLA) neutrophils has not been assessed. In this study LPS (TLR4) or an imidazoquinoline compound (TLR7/8) activated XLA neutrophil shedding of surface CD62L, and phosphorylated MAP kinases p38, JNK and ERK. TLR activation also induced normal respiratory burst and retarded apoptosis for XLA neutrophils, comparable to normal controls. These data demonstrate that the loss of Btk in XLA neutrophils does not impair functional responses to TLR signals 
650 4 |a Journal Article 
650 4 |a Research Support, N.I.H., Extramural 
650 4 |a Research Support, Non-U.S. Gov't 
650 7 |a CL097 compound  |2 NLM 
650 7 |a Imidazoles  |2 NLM 
650 7 |a Lipopolysaccharides  |2 NLM 
650 7 |a Quinolines  |2 NLM 
650 7 |a Reactive Oxygen Species  |2 NLM 
650 7 |a Toll-Like Receptors  |2 NLM 
650 7 |a L-Selectin  |2 NLM 
650 7 |a 126880-86-2  |2 NLM 
650 7 |a Granulocyte-Macrophage Colony-Stimulating Factor  |2 NLM 
650 7 |a 83869-56-1  |2 NLM 
650 7 |a Protein-Tyrosine Kinases  |2 NLM 
650 7 |a EC 2.7.10.1  |2 NLM 
650 7 |a Agammaglobulinaemia Tyrosine Kinase  |2 NLM 
650 7 |a EC 2.7.10.2  |2 NLM 
650 7 |a BTK protein, human  |2 NLM 
650 7 |a EC 2.7.10.2  |2 NLM 
650 7 |a Btk protein, mouse  |2 NLM 
650 7 |a EC 2.7.10.2  |2 NLM 
650 7 |a Mitogen-Activated Protein Kinases  |2 NLM 
650 7 |a EC 2.7.11.24  |2 NLM 
650 7 |a Tetradecanoylphorbol Acetate  |2 NLM 
650 7 |a NI40JAQ945  |2 NLM 
700 1 |a Rohr, Kaileen  |e verfasserin  |4 aut 
700 1 |a Martinez-Gallo, Monica  |e verfasserin  |4 aut 
700 1 |a Yu, Joyce  |e verfasserin  |4 aut 
700 1 |a Cunningham-Rundles, Charlotte  |e verfasserin  |4 aut 
773 0 8 |i Enthalten in  |t Clinical immunology (Orlando, Fla.)  |d 1999  |g 137(2010), 1 vom: 01. Okt., Seite 74-80  |w (DE-627)NLM098196855  |x 1521-7035  |7 nnns 
773 1 8 |g volume:137  |g year:2010  |g number:1  |g day:01  |g month:10  |g pages:74-80 
856 4 0 |u http://dx.doi.org/10.1016/j.clim.2010.06.011  |3 Volltext 
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952 |d 137  |j 2010  |e 1  |b 01  |c 10  |h 74-80