Release of low density lipoprotein receptors from human fibroblasts or Hela cells by tryptic digestion

1978 ◽  
Vol 84 (2) ◽  
pp. 366-373 ◽  
Author(s):  
Nicola Di Ferrante ◽  
Patricia V. Donnelly ◽  
Daniela T. Di Ferrante ◽  
Salvatore Toma ◽  
Antonio M. Gotto
Keyword(s):  
Hela Cells ◽  
Low Density Lipoprotein ◽  
Human Fibroblasts ◽  
Density Lipoprotein ◽  
Tryptic Digestion ◽  
Low Density ◽  
Lipoprotein Receptors

Occurrence of low density lipoprotein receptors within large pits on the surface of human fibroblasts as demonstrated by freeze-etching

1978 ◽  
Vol 113 (1) ◽  
pp. 1-13 ◽  
Author(s):  
Lelio Orci ◽  
Jean-Louis Carpentier ◽  
A. Perrelet ◽  
Richard G.W. Anderson ◽  
Joseph L. Goldstein ◽  
...  
Keyword(s):  
Low Density Lipoprotein ◽  
Human Fibroblasts ◽  
Density Lipoprotein ◽  
Low Density ◽  
Lipoprotein Receptors ◽  
Freeze Etching

Monensin interrupts the recycling of low density lipoprotein receptors in human fibroblasts

Cell ◽  
1981 ◽  
Vol 24 (2) ◽  
pp. 493-502 ◽  
Author(s):  
Sandip K. Basu ◽  
Joseph L. Goldstein ◽  
Richard G.W. Anderson ◽  
Michael S. Brown
Keyword(s):  
Low Density Lipoprotein ◽  
Human Fibroblasts ◽  
Density Lipoprotein ◽  
Low Density ◽  
Lipoprotein Receptors

scholarly journals Low-density-lipoprotein receptors in human fibroblasts are not degraded in lysosomes

1989 ◽  
Vol 262 (2) ◽  
pp. 681-683 ◽  
Author(s):  
L A F Casciola ◽  
K I Grant ◽  
W Gevers ◽  
G A Coetzee ◽  
D R van der Westhuyzen
Keyword(s):  
Low Density Lipoprotein ◽  
Human Fibroblasts ◽  
Density Lipoprotein ◽  
Receptor Internalization ◽  
Low Density ◽  
Human Skin Fibroblasts ◽  
Lipoprotein Receptors ◽  
Ldl Receptors ◽  
Endocytic Vesicles ◽  
Rate Limiting

The rate of degradation of low-density-lipoprotein (LDL) receptors was measured in cultured human skin fibroblasts by [35S]methionine pulse-chase experiments. The half-life of LDL receptors was unaltered by inclusion of LDL in the medium (t1/2 11 h). Neither lysosomotropic inhibitors (chloroquine or NH4Cl) nor leupeptin inhibited the rate of receptor degradation in the absence of ligand. In cells incubated at 18 degrees C to inhibit the delivery of internalized ligands from endocytic vesicles to lysosomes, receptor degradation continued, but at the expected rate of about six times lower than that at 37 degrees C. Mutant LDL receptors defective in internalization were degraded at the same rate as normal receptors, suggesting that receptor internalization and recycling are not required for basal turnover. We conclude that the rate-limiting steps for, and probably the whole pathway of, degradation of normal LDL receptors does not take place in lysosomes.

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