INTERNALIZATION OF GLYCOSYL-PHOSPHATIDYLINOSITOL (GPI)-ANCHORED LYMPHOCYTE PROTEINS .2. GPI-ANCHORED AND TRANSMEMBRANE MOLECULES INTERNALIZE THROUGH DISTINCT PATHWAYS

被引:57
作者
BAMEZAI, A
GOLDMACHER, VS
ROCK, KL
机构
[1] HARVARD UNIV, SCH MED, DEPT PATHOL, BOSTON, MA 02115 USA
[2] IMMUNOGEN INC, CAMBRIDGE, MA USA
关键词
D O I
10.1002/eji.1830220104
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
Ly-6A.2 (T-cell-activating protein, TAP) and Thy-1 are glycosyl-phosphatidylinositol (GPI)-anchored proteins expressed on the surface of murine T lymphocytes. We have found that Ly-6A.2 (TAP) and Thy-1 are internalized by T cells. In the present study we have investigated whether these GPI-anchored proteins enter cells by endocytosis through coated pits. Two lines of evidence argue against the involvement of coated pits in the internalization of Ly-6A.2 (TAP) and Thy-1. First, drugs that effectively blocked the endocytosis of transferrin receptor and H-2 class I molecules, (which are known to be internalized via coated pits) did not inhibit the internalization of the GPI-anchored proteins. Second, in ultrastructural analyses, Ly-6A2 (TAP) and Thy-1, in contrast to the transferrin receptor, were rarely found in coated pits or vesicles. These observations suggest that the GPI-anchored proteins on T lymphocytes are internalized by a distinct pathway that does not involve endocytosis through coated pits.
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页码:15 / 21
页数:7
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