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Role of the coated endocytic vesicle in the uptake of receptor-bound low density lipoprotein in human fibroblasts
Abstract
125I-labeled and ferritin-labeled low density lipoprotein (LDL) were used as visual probes to study the surface distribution of LDL receptors and to examine the mechanism of the endocytosis of this lipoprotein in cultured human fibrobasts. Light microscopic autoradiograms of whole cells incubated with 125I-LDL at 4 degrees C showed that LDL receptors were widely but unevenly distributed over the cell surface. With the electron microscope, we determined that 60-70% of the ferritin-labeled LDL that bound to cells at 4 degrees C was localized over short coated segments of the plasma membrane that accounted for no more than 2% of the total surface area. To study the internalization process, cells were first allowed to bind ferritin-labeled LDL at 4 degrees C and were then warmed to 37 degrees C. Within 10 min, nearly all the surface-bound LDL-ferritin was incorporated into coated endocytic vesicles that were formed by the invagination and pinching-off of the coated membrane regions that contained the receptor-bound LDL. With increasing time at 37 degrees C, these coated vesicles were observed sequentially to migrate through the cytoplasm (1 min), to lose their cytoplasmic coat (2 min), and to fuse with either primary or secondary lysosomes (6 min). The current data indicate that the coated regions of plasma membrane are specialized structures of rapid turnover that function to carry receptor-bound LDL, and perhaps other receptor-bound molecules, into the cell.
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In fibroblasts, many LDLRs appear to be expelled from the invaginating portion of coated pits during pit budding, suggesting that poorly anchored receptors are not readily captured by the budding portion of the coated pit.
“expelled from the invaginating portion of coated pits during pit budding (36), suggesting that poorly anchored receptors are not readily captured by the budding portion of the coated pit.”
From The Modular Adaptor Protein ARH Is Required for Low Density Lipoprotein (LDL) Binding and Internalization but Not for LDL Receptor Clustering in Coated Pits (2004) · cites this paper as [36]
LDLR is translocated to the Golgi network where it is glycosylated and released via vesicles to the plasma membrane, where it is recruited by Dab2 to reside within clathrin-rich pits.
“It is then translocated to the Golgi network where it is glycosylated and released via vesicles to the plasma membrane, where is it recruited by Dab281 to reside within clathrin-rich pits82–84.”
From Pathways and Molecular Mechanisms Governing LDL Receptor Regulation (2025) · cites this paper as [83]
Very quickly, the clathrin coat dissociates and multiple endocytic vesicles fuse to create endosomes.
“Very quickly, the clathrin coat dissociates and multiple endocytic vesicles fuse to create endosomes (4 -6).”
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Metadata
- Authors
- Anderson, R. G. W., Brown, M. S., & Goldstein, J. L.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1977-03
- Volume
- 10
- Issue
- 3
- Pages
- 351-364
- ISSN
- 0092-8674
- Cited by
- 489
- References
- 0
- Language
- en
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