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rdf:type |
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lifeskim:mentions |
umls-concept:C0001271,
umls-concept:C0015127,
umls-concept:C0015576,
umls-concept:C0018270,
umls-concept:C0024880,
umls-concept:C0035820,
umls-concept:C0085409,
umls-concept:C0205217,
umls-concept:C0392756,
umls-concept:C0542341,
umls-concept:C0815089,
umls-concept:C1135629,
umls-concept:C1314792,
umls-concept:C1706853,
umls-concept:C1709985,
umls-concept:C1822704,
umls-concept:C1879748
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pubmed:issue |
2
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pubmed:dateCreated |
2004-2-9
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pubmed:abstractText |
Lnk, SH2-B, and APS form a conserved adaptor protein family. All of those proteins are expressed in mast cells and their possible functions in signaling through c-Kit or FcRI have been speculated. To investigate roles of Lnk, SH2-B or APS in mast cells, we established IL-3-dependent mast cells from Ink-/-, SH2-B-/-, and APS -/- mice. IL-3-dependent growth of those cells was comparable. Proliferation or adhesion mediated by c-Kit as well as degranulation induced by cross-linking FcRI were normal in the absence of Lnk or SH2-B. In contrast, APS-deficient mast cells showed augmented degranulation after cross-linking FcRI compared to wild-type cells, while c-Kit-mediated proliferation and adhesion were kept unaffected. APS-deficient mast cells showed reduced actin assembly at steady state, although their various intracellular responses induced by cross-linking FcRI were indistinguishable compared to wild-type cells. Our results suggest potential roles of APS in controlling actin cytoskeleton and magnitude of degranulation in mast cells.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Aps protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Aps protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Bicyclo Compounds, Heterocyclic,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Cytokines,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-3,
http://linkedlifedata.com/resource/pubmed/chemical/LNK protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Lnk protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-kit,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytokine,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, IgE,
http://linkedlifedata.com/resource/pubmed/chemical/SH2B1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Sh2bpsm1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Sh2bpsm1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Thiazoles,
http://linkedlifedata.com/resource/pubmed/chemical/Thiazolidines,
http://linkedlifedata.com/resource/pubmed/chemical/latrunculin A
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
315
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
356-62
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:14766215-Actins,
pubmed-meshheading:14766215-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:14766215-Animals,
pubmed-meshheading:14766215-Bicyclo Compounds, Heterocyclic,
pubmed-meshheading:14766215-Calcium,
pubmed-meshheading:14766215-Carrier Proteins,
pubmed-meshheading:14766215-Cell Adhesion,
pubmed-meshheading:14766215-Cell Division,
pubmed-meshheading:14766215-Cell Movement,
pubmed-meshheading:14766215-Cell Separation,
pubmed-meshheading:14766215-Cell Survival,
pubmed-meshheading:14766215-Cross-Linking Reagents,
pubmed-meshheading:14766215-Cytokines,
pubmed-meshheading:14766215-Cytoskeleton,
pubmed-meshheading:14766215-Dose-Response Relationship, Drug,
pubmed-meshheading:14766215-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:14766215-Flow Cytometry,
pubmed-meshheading:14766215-Immunoblotting,
pubmed-meshheading:14766215-Immunohistochemistry,
pubmed-meshheading:14766215-Interleukin-3,
pubmed-meshheading:14766215-Mast Cells,
pubmed-meshheading:14766215-Mice,
pubmed-meshheading:14766215-Mice, Transgenic,
pubmed-meshheading:14766215-Protein Binding,
pubmed-meshheading:14766215-Protein-Tyrosine Kinases,
pubmed-meshheading:14766215-Proteins,
pubmed-meshheading:14766215-Proto-Oncogene Proteins c-kit,
pubmed-meshheading:14766215-Receptors, Cytokine,
pubmed-meshheading:14766215-Receptors, IgE,
pubmed-meshheading:14766215-Signal Transduction,
pubmed-meshheading:14766215-Thiazoles,
pubmed-meshheading:14766215-Thiazolidines,
pubmed-meshheading:14766215-Time Factors
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pubmed:year |
2004
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pubmed:articleTitle |
Roles of a conserved family of adaptor proteins, Lnk, SH2-B, and APS, for mast cell development, growth, and functions: APS-deficiency causes augmented degranulation and reduced actin assembly.
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pubmed:affiliation |
Division of Immunology, Department of Microbiology and Immunology, The Institute of Medical Science, The University of Tokyo, Shirokanedai 4-6-1, Minato-ku, Tokyo 108-8639, Japan.
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pubmed:publicationType |
Journal Article
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