Internalization of caveolae and their relationship with endosomes in cultured human and mouse endothelial cells

被引：0

作者：

Aoki T. ^{[1
]}

Hagiwara H. ^{[1
]}

Matsuzaki T. ^{[1
]}

Suzuki T. ^{[1
]}

Takata K. ^{[1
]}

机构：

[1] Department of Anatomy and Cell Biology, Gunma University Graduate School of Medicine, Maebashi 371-8511

来源：

Anatomical Science International | 2007年 / 82卷 / 2期

关键词：

Caveola; Caveolin-1; Endothelial cell; Phosphorylation; Rab GTP-binding protein;

D O I：

10.1111/j.1447-073X.2006.00160.x

中图分类号：

学科分类号：

摘要：

Treatment of cells with pervanadate or vanadate induces the phosphorylation of caveolin-1 and its internalization from the cell surface, but the intracellular fate of caveolae has not been fully elucidated. In the present study, we examined the fate of endocytosed caveolae in human umbilical vein endothelial cells and mouse endothelial KOP2.16 cells. The localization of internalized caveolae and their relationship with the endosomes were examined by immunofluorescence microscopy as well as by immunoprecipitation and chasing of biotinylated transferrin. In untreated cells, caveolin-1 was mostly confined to the cell surface. When cells were treated with either pervanadate for 30 min or vanadate for 3 h, many caveolin-1-labeled vesicles were formed inside the cells, some of which were colocalized with Rab5 or Rab4. The internalized caveolin-1 was colocalized with the endocytosed transferrin in the Rab5-, Rab4-or early endosome antigen-1-labeled compartment where caveolin-1 was phosphorylated. It then moved to the Rab11-associated compartment. Immunogold electron microscopy revealed that internalized caveolin-1 colocalized with Rab5 or Rab4 in vesicles larger than caveolae. These results suggest that the internalized caveolae interact with early endosomes. © 2006 Japanese Association of Anatomists.

引用

页码：82 / 97

页数：15

共 53 条

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