Variability of the topography of low-density lipoprotein (LDL) receptors in the plasma membrane of cultured human skin fibroblasts as revealed by gold-LDL conjugates in conjunction with the surface replication technique

1983 ◽  
Vol 82 (2) ◽  
pp. 143-155 ◽  
Author(s):  
Horst Robenek ◽  
Arpad Hesz ◽  
Jürgen Rassat
1980 ◽  
Vol 186 (1) ◽  
pp. 373-375 ◽  
Author(s):  
I Filipovic ◽  
K von Figura

Preincubation of normal human skin fibroblasts with tunicamycin, which inhibits N-glycosylation of glycoproteins, resulted in a dose-dependent and reversible inhibition of binding and internalization of homologous low-density lipoproteins by the cells. The degradation of the internalized lipoproteins was not affected by the drug. Comparative studies with fibroblasts deficient in low-density-lipoprotein receptors indicated that tunicamycin exerts its inhibitory effect only via the receptor-mediated high-affinity binding and uptake of lipoproteins. These results suggest that expression of low-density-lipoprotein receptors on the cell surface of human skin fibroblasts depends on intact N-glycosylation.


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