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Cell-surface heparan sulfate proteoglycans: dynamic molecules mediating ligand catabolism
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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Ligands bound to heparan sulfate chains can piggy-back into the cell.
“Thus, ligands bound to the heparan sulfate chains can “piggy-back” into the cell (5), which operationally defines syndecan-1 as an endocytic receptor of broad specificity.”
From Syndecan-1 is the primary heparan sulfate proteoglycan mediating hepatic clearance of triglyceride-rich lipoproteins in mice (2009) · cites this paper as [5]
A large body of data indicates that proteoglycans can act as independent endocytic receptors for a variety of ligands, both natural and synthetic.
“Finally, a large body data indicates that proteoglycans can act as independent endocytic receptors for a variety of ligands, both natural and synthetic (5, 64, 65).”
From Syndecan-1 is the primary heparan sulfate proteoglycan mediating hepatic clearance of triglyceride-rich lipoproteins in mice (2009) · cites this paper as [5]
Membrane-bound proteoglycans can act as endocytic receptors facilitating the uptake of various ligands and metabolites.
“Additionally, membrane-bound proteoglycans can act as endocytic receptors facilitating the uptake of various ligands and metabolites (4,5).”
From Liver heparan sulfate proteoglycans mediate clearance of triglyceride-rich lipoproteins independently of LDL receptor family members (2007) · cites this paper as [4]
Since membrane proteoglycans undergo clustering and constitutive endocytosis, lipoproteins bound to the proteoglycans could piggy-back into the cell.
“Since membrane proteoglycans undergo clustering and constitutive endocytosis (4, 22, 62, 63), lipoproteins bound to the proteoglycans could “piggy-back” into the cell.”
From Liver heparan sulfate proteoglycans mediate clearance of triglyceride-rich lipoproteins independently of LDL receptor family members (2007) · cites this paper as [4]
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Libeu, C. P., Lund-Katz, S., Phillips, M. C., Wehrli, S., Hernáiz, M. J., Capila, I., Linhardt, R. J., Raffaı̈, R. L., Newhouse, Y. M., Zhou, F., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104746200 · Cited by 113
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Foley, E. M., Gordts, P. L. S. M., Stanford, K. I., Gonzales, J. C., Lawrence, R., Stoddard, N., & Esko, J. D. (2013) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/atvbaha.113.301637 · Cited by 77
Shuvaev, V. V., Laffont, I., & Siest, G. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01285-5 · Cited by 27
Metadata
- Authors
- Jon Williams, K., & Fuki, I. V.
- Venue
- Current Opinion in Lipidology
- Published
- 1997-10
- Volume
- 8
- Issue
- 5
- Pages
- 253-262
- ISSN
- 0957-9672
- Cited by
- 113
- References
- 0
- Language
- en
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