Structural Basis for Thermal Stability of Human Low-Density Lipoprotein†

Biochemistry ◽  
2005 ◽  
Vol 44 (10) ◽  
pp. 3965-3971 ◽  
Author(s):  
Shobini Jayaraman ◽  
Donald Gantz ◽  
Olga Gursky

Biochemistry ◽  
1998 ◽  
Vol 37 (3) ◽  
pp. 938-944 ◽  
Author(s):  
Ruth Prassl ◽  
Bernhard Schuster ◽  
Peter Laggner ◽  
Claudie Flamant ◽  
Fabienne Nigon ◽  
...  


Author(s):  
Anna Rull ◽  
Shobini Jayaraman ◽  
Donald L. Gantz ◽  
Andrea Rivas-Urbina ◽  
Montserrat Pérez-Cuellar ◽  
...  


Author(s):  
Dean A. Handley ◽  
Cynthia M. Arbeeny ◽  
Larry D. Witte

Low density lipoproteins (LDL) are the major cholesterol carrying particles in the blood. Using cultured cells, it has been shown that LDL particles interact with specific surface receptors and are internalized via a coated pit-coated vesicle pathway for lysosomal catabolism. This (Pathway has been visualized using LDL labeled to ferritin or colloidal gold. It is now recognized that certain lysomotropic agents, such as chloroquine, inhibit lysosomal enzymes that degrade protein and cholesterol esters. By interrupting cholesterol ester hydrolysis, chloroquine treatment results in lysosomal accumulation of cholesterol esters from internalized LDL. Using LDL conjugated to colloidal gold, we have examined the ultrastructural effects of chloroquine on lipoprotein uptake by normal cultured fibroblasts.





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