Lipid rafts in mast cell signaling
Jazyk angličtina Země Anglie, Velká Británie Médium print
Typ dokumentu časopisecké články, práce podpořená grantem, přehledy
PubMed
12217391
DOI
10.1016/s0161-5890(02)00071-8
PII: S0161589002000718
Knihovny.cz E-zdroje
- MeSH
- antigeny Thy-1 analýza MeSH
- cholesterol fyziologie MeSH
- detergenty farmakologie MeSH
- krysa rodu Rattus MeSH
- mastocyty imunologie MeSH
- membránové mikrodomény chemie účinky léků fyziologie MeSH
- receptory IgE metabolismus MeSH
- signální transdukce * MeSH
- skupina kinas odvozených od src-genu analýza MeSH
- zvířata MeSH
- Check Tag
- krysa rodu Rattus MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- přehledy MeSH
- Názvy látek
- antigeny Thy-1 MeSH
- cholesterol MeSH
- detergenty MeSH
- lyn protein-tyrosine kinase MeSH Prohlížeč
- receptory IgE MeSH
- skupina kinas odvozených od src-genu MeSH
Lipid rafts are defined as plasma membrane microdomains enriched with glycosphingolipids and cholesterol which render them insoluble in non-ionic detergents. Many surface receptors are constitutively or inducibly associated with lipid rafts, and it has been suggested that the rafts function as platforms regulating the induction of signaling pathways. The signaling capacity of lipid rafts has been extensively studied in rat basophilic leukemia cells. An aggregation of lipid raft components, such as glycosylphosphatidylinositol (GPI)-anchored glycoproteins (Thy-1 or TEC-21), triggers cell activation events which are similar to, but not identical with activation via the high-affinity IgE receptor (FcepsilonRI). Although FcepsilonRI in resting cells is not associated with lipid rafts, its aggregation induces a weak association with rafts and subsequent activation events. The properties of lipid rafts as well as the molecular mechanisms of their involvement in signal transduction are poorly understood. This review presents a critical analysis of recent results on structure-function relationship of lipid rafts and their regulatory role in signal transduction in mast cells.
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