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.

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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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