Separation of caveolae from associated microdomains of GPI-anchored proteins - PubMed (original) (raw)
. 1995 Sep 8;269(5229):1435-9.
doi: 10.1126/science.7660128.
Affiliations
- PMID: 7660128
- DOI: 10.1126/science.7660128
Separation of caveolae from associated microdomains of GPI-anchored proteins
J E Schnitzer et al. Science. 1995.
Abstract
In situ coating of the surface of endothelial cells in rat lung with cationic colloidal silica particles was used to separate caveolae from detergent-insoluble membranes rich in glycosyl phosphatidylinositol (GPI)-anchored proteins but devoid of caveolin. Immunogold electron microscopy showed that ganglioside GM1-enriched caveolae associated with an annular plasmalemmal domain enriched in GPI-anchored proteins. The purified caveolae contained molecular components required for regulated transport, including various lipid-anchored signaling molecules. Such specialized distinct microdomains may exist separately or together in the plasma membrane to organize signaling molecules and to process surface-bound ligands differentially.
Comment in
- Digging into caveolae.
Parton RG, Simons K. Parton RG, et al. Science. 1995 Sep 8;269(5229):1398-9. doi: 10.1126/science.7660120. Science. 1995. PMID: 7660120 No abstract available.
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