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Association of the GPI-anchored leucocyte surface glycoproteins with ganglioside GM3
B Kniep1, T Cinek, P Angelisová
1GBF, Immunobiology Group, Braunschweig, Germany.
The major glycolipid co-immunopurifying with the glycosylphosphatidylinositol-anchored leucocyte surface glycoprotein CD59 from detergent lysates of human T cell lines HPB ALL, Jurkat and myeloid line HL-60 was identified as the glycosphingolipid GM3. Monoclonal antibodies to GM3 immunoprecipitated the same large detergent-resistant, protein-tyrosine kinase containing "GPI-complexes" as antibodies to several GPI-anchored proteins. Therefore GM3 is another component of these large membrane complexes potentially involved in signalling through GPI-anchored receptors or through some glycolipids.
The major glycolipid co-immunopurifying with the glycosylphosphatidylinositol-anchored leucocyte surface glycoprotein CD59 from detergent lysates of human T cell lines HPB ALL, Jurkat and myeloid line HL-60 was identified as the glycosphingolipid GM3. Monoclonal antibodies to GM3 immunoprecipitated the same large detergent-resistant, protein-tyrosine kinase containing "GPI-complexes" as antibodies to several GPI-anchored proteins. Therefore GM3 is another component of these large membrane complexes potentially involved in signalling through GPI-anchored receptors or through some glycolipids.