rdf:type |
|
lifeskim:mentions |
umls-concept:C0024880,
umls-concept:C0029246,
umls-concept:C0033684,
umls-concept:C0037083,
umls-concept:C0449911,
umls-concept:C0871261,
umls-concept:C1704241,
umls-concept:C1704632,
umls-concept:C1706817,
umls-concept:C1710082,
umls-concept:C2911692
|
pubmed:issue |
16-18
|
pubmed:dateCreated |
2002-9-9
|
pubmed:abstractText |
The generation of signals following engagement of cell surface receptors is an ordered process that requires tight regulation as spurious signals could result in unwanted, and possibly deleterious, cellular responses. Like other cell surface receptors, stimulation of a mast cell via the high affinity IgE receptor (FcepsilonRI) causes multiple biochemical events that ultimately result in cell activation and effector responses. Recently, our knowledge of how these events are ordered has increased. We now have identified some of the molecules involved, how they are organized into macromolecular complexes by FcepsilonRI stimulation, and the role of some of the constituents of these macromolecular signaling complexes in mast cell effector responses. In brief, we review the knowledge on macromolecular signaling complexes used by FcepsilonRI in mast cell activation and provide our view on the regulation of signal generation and its effect on mast cell activation.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin E,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-vav,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, IgE,
http://linkedlifedata.com/resource/pubmed/chemical/lyn protein-tyrosine kinase,
http://linkedlifedata.com/resource/pubmed/chemical/src-Family Kinases
|
pubmed:status |
MEDLINE
|
pubmed:month |
Sep
|
pubmed:issn |
0161-5890
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
38
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1253-8
|
pubmed:dateRevised |
2011-11-2
|
pubmed:meshHeading |
pubmed-meshheading:12217392-Animals,
pubmed-meshheading:12217392-Carrier Proteins,
pubmed-meshheading:12217392-Cell Cycle Proteins,
pubmed-meshheading:12217392-Immunoglobulin E,
pubmed-meshheading:12217392-Macromolecular Substances,
pubmed-meshheading:12217392-Mast Cells,
pubmed-meshheading:12217392-Models, Immunological,
pubmed-meshheading:12217392-Phosphoproteins,
pubmed-meshheading:12217392-Proto-Oncogene Proteins,
pubmed-meshheading:12217392-Proto-Oncogene Proteins c-vav,
pubmed-meshheading:12217392-Receptors, IgE,
pubmed-meshheading:12217392-Signal Transduction,
pubmed-meshheading:12217392-src-Family Kinases
|
pubmed:year |
2002
|
pubmed:articleTitle |
Macromolecular protein signaling complexes and mast cell responses: a view of the organization of IgE-dependent mast cell signaling.
|
pubmed:affiliation |
Molecular Inflammation Section, Molecular Immunology and Inflammation Branch, National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIAMS), National Institute of Health (NIH), Bethesda, MD 20892-1820, USA. juan_rivera@nih.gov
|
pubmed:publicationType |
Journal Article,
Review
|