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Curr Opin Lipidol. 1997 Oct;8(5):253-62.

Cell-surface heparan sulfate proteoglycans: dynamic molecules mediating ligand catabolism.

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1
Dorrance H. Hamilton Research Laboratories, Department of Medicine, Jefferson Medical College of Thomas Jefferson University, Philadelphia, PA 19107-6799, USA.

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  • Curr Opin Lipidol 1998 Feb;9(1):80.

Abstract

Though sometimes regarded as merely passive, space-filling components, proteoglycans are in fact metabolically active molecules with carbohydrate and protein domains that are highly conserved throughout evolution, indicating specific, crucial functions. Here we review recent evidence that heparan sulfate proteoglycans, particularly syndecans and perlecan, are able to mediate directly the internalization of lipoproteins and other ligands, without requiring the participation of LDL receptor family members. Thus, heparan sulfate proteoglycans can function as receptors. In the case of syndecan heparan sulfate proteoglycans, efficient internalization is triggered by clustering of the transmembrane and cytoplasmic domains and then proceeds through a noncoated pit pathway, possibly caveolae. The physiologic and pathophysiologic importance of these direct heparan sulfate proteoglycan-mediated catabolic pathways in the liver and in the arterial wall in vivo remains to be settled.

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PMID:
9335948
[Indexed for MEDLINE]
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