Glycosylation of LDL decreases its ability to interact with high-affinity receptors of human fibroblasts in vitro and decreases its clearance from rabbit plasma in vivo-Reference-Cited by-同舟云学术

Glycosylation of LDL decreases its ability to interact with high-affinity receptors of human fibroblasts in vitro and decreases its clearance from rabbit plasma in vivo

Published:1982-11 Issue:2 Volume:713 Page:199-207
ISSN:0005-2760
Container-title:Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism

Author:

Sasaki Jun,Cottam Gene L.

Publisher

Elsevier BV

Subject

Endocrinology,Biochemistry,Biophysics

Reference32 articles.

1. Binding and Degradation of Low Density Lipoproteins by Cultured Human Fibroblasts

2. The Low-Density Lipoprotein Pathway and its Relation to Atherosclerosis

3. Inhibition of lipoprotein binding to cell surface receptors of fibroblasts following selective modification of arginyl residues in arginine-rich and B apoproteins.

4. Release of low density lipoprotein from its cell surface receptor by sulfated glycosaminoglycans

5. Genetics of the LDL receptor: Evidence that the mutations affecting binding and internalization are allelic

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