Abstract
Glycosyl-phosphatidylinositol (GPI)-anchored proteins have been reported to reside in clusters collected over small membrane invaginations called caveolae. The detection of different GPI-anchored proteins with fluorescently labeled monoclonal antibodies showed that these proteins are not constitutively concentrated in caveolae; they enter these structures independently after cross-linking with polyclonal secondary antibodies. Analysis of the cell surface distribution of the GPI-anchored folate receptor by electron microscopy confirms these observations. Thus, multimerization of GPI-anchored proteins regulates their sequestration in caveolae, but in the absence of agents that promote clustering they are diffusely distributed over the plasma membrane.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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3T3 Cells
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Animals
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Antibodies, Monoclonal
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Antigens, CD / analysis
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Antigens, CD / immunology
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Antigens, CD / metabolism
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Antigens, Surface / analysis
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Antigens, Surface / immunology
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Antigens, Surface / metabolism
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CD55 Antigens
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Carrier Proteins / analysis
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Carrier Proteins / immunology
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Carrier Proteins / metabolism*
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Caveolin 1
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Caveolins*
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Cell Membrane / metabolism*
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Cell Membrane / ultrastructure
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Fluorescent Antibody Technique
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Folate Receptors, GPI-Anchored
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Folic Acid / metabolism
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Glycosylphosphatidylinositols / analysis
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Glycosylphosphatidylinositols / metabolism*
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Humans
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Immunoglobulin G / metabolism
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Membrane Glycoproteins / analysis
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Membrane Glycoproteins / immunology
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Membrane Glycoproteins / metabolism
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Membrane Proteins / analysis
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Mice
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Microscopy, Electron
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Receptors, Cell Surface*
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Thy-1 Antigens
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Tumor Cells, Cultured
Substances
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Antibodies, Monoclonal
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Antigens, CD
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Antigens, Surface
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CD55 Antigens
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Carrier Proteins
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Caveolin 1
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Caveolins
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Folate Receptors, GPI-Anchored
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Glycosylphosphatidylinositols
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Immunoglobulin G
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Membrane Glycoproteins
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Membrane Proteins
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Receptors, Cell Surface
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Thy-1 Antigens
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Folic Acid