pubmed-article:10377180 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10377180 | lifeskim:mentions | umls-concept:C0296250 | lld:lifeskim |
pubmed-article:10377180 | lifeskim:mentions | umls-concept:C1705639 | lld:lifeskim |
pubmed-article:10377180 | lifeskim:mentions | umls-concept:C0024880 | lld:lifeskim |
pubmed-article:10377180 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
pubmed-article:10377180 | lifeskim:mentions | umls-concept:C0123242 | lld:lifeskim |
pubmed-article:10377180 | lifeskim:mentions | umls-concept:C0011155 | lld:lifeskim |
pubmed-article:10377180 | lifeskim:mentions | umls-concept:C1334333 | lld:lifeskim |
pubmed-article:10377180 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
pubmed-article:10377180 | pubmed:issue | 12 | lld:pubmed |
pubmed-article:10377180 | pubmed:dateCreated | 1999-7-7 | lld:pubmed |
pubmed-article:10377180 | pubmed:abstractText | SLP-76 is an adapter protein expressed in T cells and myeloid cells that is a substrate for ZAP-70 and Syk. SLP-76-deficient mice exhibit a profound block in T-cell development. We found that although SLP-76 is expressed in mouse mast cells, SLP-76(-/-) mice have normal numbers of mast cells in their skin and bronchi. SLP-76(-/-) mice are resistant to IgE-mediated passive anaphylaxis. SLP-76(-/-) mice sensitized with IgE anti-dinitrophenyl (DNP) and then challenged with DNP-HSA developed only mild and transient tachycardia, failed to increase their plasma histamine level, and all survived the antigen challenge. Bone marrow-derived mast cells (BMMCs) from SLP76(-/-) mice failed to release beta-hexosaminidase and to secrete IL-6 after FcepsilonRI cross-linking. Tyrosine phosphorylation of phospholipase C-gamma1 (but not of Syk) and calcium mobilization in response to IgE cross-linking were reduced in SLP-76-deficient BMMCs. These results suggest that SLP-76 plays an important role in FcepsilonRI-mediated signaling in mast cells. | lld:pubmed |
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pubmed-article:10377180 | pubmed:language | eng | lld:pubmed |
pubmed-article:10377180 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10377180 | pubmed:citationSubset | AIM | lld:pubmed |
pubmed-article:10377180 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10377180 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:10377180 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10377180 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10377180 | pubmed:month | Jun | lld:pubmed |
pubmed-article:10377180 | pubmed:issn | 0021-9738 | lld:pubmed |
pubmed-article:10377180 | pubmed:author | pubmed-author:GehaR SRS | lld:pubmed |
pubmed-article:10377180 | pubmed:author | pubmed-author:LEVYJ PJP | lld:pubmed |
pubmed-article:10377180 | pubmed:author | pubmed-author:MartinT RTR | lld:pubmed |
pubmed-article:10377180 | pubmed:author | pubmed-author:OettgenH CHC | lld:pubmed |
pubmed-article:10377180 | pubmed:author | pubmed-author:Lu-KuoJ MJM | lld:pubmed |
pubmed-article:10377180 | pubmed:author | pubmed-author:PivnioukV IVI | lld:pubmed |
pubmed-article:10377180 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10377180 | pubmed:volume | 103 | lld:pubmed |
pubmed-article:10377180 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10377180 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10377180 | pubmed:pagination | 1737-43 | lld:pubmed |
pubmed-article:10377180 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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