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A more recent version of this article appeared on June 1, 2004
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Submitted on August 8, 2003
Revised on December 29, 2003
Accepted on February 25, 2004
1 Department of Pathology & Cancer Research & Treatment Center, University of New Mexico, Albuquerque, New Mexico 87131
2 Department of Mathematics and Statistics, University of New Mexico, Albuquerque, New Mexico 87131
3 Department of Computer Science, University of New Mexico, Albuquerque, New Mexico 87131
4 Laboratory of Cellular and Molecular Biology, Center for Cancer Research, National Cancer Institute, Bethesda, Maryland 20892
5 Materials Characterization Department, Sandia National Laboratories, Albuquerque, New Mexico 87185
* Corresponding author. E-mail address: bwilson{at}salud.unm.edu.
Lipid rafts isolated by detergent extraction and sucrose gradient fractionation from mast cells are enriched for the GPI-linked protein, Thy-1, the ganglioside, GM1, palmitoylated LAT and cross-linked IgE receptors, Fc
RI. This study addresses the relationship of fractionation data to the organization of raft markers in native membranes. Immunogold labeling and electron microscopy shows there is little or no colocalization of the raft markers Thy-1, GM1 and LAT with each other or with FcRI on native membrane sheets prepared from unstimulated cells. External cross-linking of Thy-1 promotes coclustering of Thy-1 with LAT, but not with GM1. Thy-1 and LAT clusters occur on membrane regions without distinctive features. In contrast, external cross-linking of FcRI and GM1 causes their redistribution to electron-dense membrane patches independently of each other and of Thy-1. The distinctive patches that accumulate cross-linked FcRI and GM1 also accumulate osmium, a stain for unsaturated lipids, and are sites for coated vesicle budding. Electron microscopy reveals a more complex and dynamic topographical organization of membrane microdomains than is predicted by biochemical analysis of detergent-resistant membranes.
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