The biogenesis of the MHC class II compartment in human I-Cell Disease B lymphoblasts

被引:63
作者
Glickman, JN
Morton, PA
Slot, JW
Kornfeld, S
Geuze, HJ
机构
[1] WASHINGTON UNIV, SCH MED, DEPT MED, ST LOUIS, MO 63110 USA
[2] MONSANTO CO, DIV IMMUNOL, CHESTERFIELD, MO 63198 USA
[3] UNIV UTRECHT, DEPT CELL BIOL, 3584 CX UTRECHT, NETHERLANDS
关键词
D O I
10.1083/jcb.132.5.769
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The localization and intracellular transport of major histocompatibility complex (MHC) class II molecules and lysosomal hydrolases were studied in I-Cell Disease (ICD) B lymphoblasts, which possess a mannose 6-phosphate (Man-6-P)-independent targeting pathway for lysosomal enzymes. In the trans-Golgi network (TGN), MHC class II-invariant chain complexes colocalized with the lysosomal hydrolase cathepsin D in buds and vesicles that lacked markers of clathrin-coated vesicle-mediated transport. These vesicles fused with the endocytic pathway leading to the formation of ''early'' MHC class II-rich compartments (MIICs). Similar structures were observed in the TGN of normal beta lymphoblasts although they were less abundant. Metabolic labeling and subcellular fractionation experiments indicated that newly synthesized cathepsin D and MHC class II-invariant chain complexes enter a non-clathrin-coated vesicular structure after their passage through the TGN and segregation from the secretory pathway. These vesicles were also devoid of the cation-dependent mannose 6-phosphate (Man-6-P) receptor, a marker of early and late endosomes, These findings suggest that in ICD B lymphoblasts the majority of MHC class II molecules are transported directly from the TGN to ''early'' MIICs and that acid hydrolases can be incorporated into MIICs si multaneously by a Man-6-P-independent process.
引用
收藏
页码:769 / 785
页数:17
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