We have recently identified a novel murine glycoprotein termed sgp-60, which is expressed on the cell surface of T and B lymphocytes. Because of the profound modulatory effects of sgp-60 on activation through the T cell receptor/CD3 complex, we have examined the membrane attachment domain of the molecule. sgp-60 is not expressed on the surface of variants of a T-T hybridoma cell line that are defective in glycosylphosphatidylinositol (GPI) anchor biosynthesis. In wild-type but not in mutant cells, sgp-60 can be labeled with palmitic acid. Furthermore, the molecule can be removed from the cell surface of both T and B lymphocytes by enzymatic digestion with a phosphatidylinositol-specific phospholipase C. We conclude that the sgp-60 molecule is linked to the plasma membrane via a GPI anchor.
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Eur J Immunol
June 1993
Department of Immunology, Juntendo University School of Medicine, Tokyo, Japan.
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View Article and Find Full Text PDFThe sgp-60 molecule is linked to the plasma membrane via a glycosylphosphatidylinositol anchor.
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Department of Pathology, Harvard Medical School, Boston, MA.
We have recently identified a novel murine glycoprotein termed sgp-60, which is expressed on the cell surface of T and B lymphocytes. Because of the profound modulatory effects of sgp-60 on activation through the T cell receptor/CD3 complex, we have examined the membrane attachment domain of the molecule. sgp-60 is not expressed on the surface of variants of a T-T hybridoma cell line that are defective in glycosylphosphatidylinositol (GPI) anchor biosynthesis.
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Department of Pathology, Harvard Medical School, Boston, MA 02115.
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