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Heparan sulfate proteoglycan as a plasma membrane carrier
Abstract
The plasma membrane defines the border of living cells and provides a barrier to extracellular components. Advances in molecular biology have resulted in the development of novel therapeutic strategies (e.g. gene therapy and cellular protein delivery) which rely on the entry of charged macromolecules into the intracellular compartment. Recent reports demonstrate an intriguing role for heparan sulfate proteoglycans in cellular internalization of viruses, basic peptides and polycation-nucleic-acid complexes and the possibility that they have important implications for gene transfer and protein delivery to mammalian cells. This review focuses on heparan sulfate proteoglycan as a plasma membrane carrier.
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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 [64]
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 [5]
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 [63]
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Metadata
- Authors
- Belting, M.
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2003-03
- Volume
- 28
- Issue
- 3
- Pages
- 145-151
- ISSN
- 0968-0004
- Cited by
- 273
- References
- 1
- Language
- en
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