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Cited by 477

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Separation of Caveolae from Associated Microdomains of GPI-Anchored Proteins

Schnitzer, Jan E., McIntosh, Deirdre P., Dvorak, Ann M., Liu, Jun, Oh, Phil·1995·Science

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 G M1 -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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Metadata

Authors
Schnitzer, J. E., McIntosh, D. P., Dvorak, A. M., Liu, J., & Oh, P.
Venue
Science
Published
1995-09-08
Volume
269
Issue
5229
Pages
1435-1439
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2050465028
Cited by
477
References
0
FWCI
15.60
Type
journal article
Language
en
Open access
closed

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.