| Cell-surface proteoglycans as molecular portals for cationic peptide and polymer entry into cells. | |
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MedLine Citation:
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PMID: 17635149 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Polycationic macromolecules and cationic peptides acting as PTDs (protein transduction domains) and CPPs (cell-penetrating peptides) represent important classes of agents used for the import and delivery of a wide range of molecular cargoes into cells. Their entry into cells is typically initiated through interaction with cell-surface HS (heparan sulfate) molecules via electrostatic interactions, followed by endocytosis of the resulting complexes. However, the endocytic mechanism employed (clathrin-mediated endocytosis, caveolar uptake or macropinocytosis), defining the migration of these peptides into cells, depends on parameters such as the nature of the cationic agent itself and complex formation with cargo, as well as the nature and distribution of proteoglycans expressed on the cell surface. Moreover, a survey of the literature suggests that endocytic pathways should not be considered as mutually exclusive, as more than one entry mechanism may be operational for a given cationic complex in a particular cell type. Specifically, the observed import may best be explained by the distribution and uptake of cell-surface HSPGs (heparan sulfate proteoglycans), such as syndecans and glypicans, which have been shown to mediate the uptake of many ligands besides cationic polymers. A brief overview of the roles of HSPGs in ligand internalization is presented, as well as mechanistic hypotheses based on the known properties of these cell-surface markers. The identification and investigation of interactions made by glycosaminoglycans and core proteins of HSPGs with PTDs and cationic polymers will be crucial in defining their uptake by cells. |
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Authors:
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G M K Poon; J Gariépy |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Review |
Journal Detail:
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Title: Biochemical Society transactions Volume: 35 ISSN: 0300-5127 ISO Abbreviation: Biochem. Soc. Trans. Publication Date: 2007 Aug |
Date Detail:
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Created Date: 2007-07-19 Completed Date: 2007-10-11 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 7506897 Medline TA: Biochem Soc Trans Country: England |
Other Details:
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Languages: eng Pagination: 788-93 Citation Subset: IM |
Affiliation:
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Division of Cancer Genomics and Proteomics, Ontario Cancer Institute, University Health Network, Ontario, Canada M5G 2M9. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Antimicrobial Cationic Peptides / metabolism* Humans Membrane Glycoproteins / physiology* Polymers / metabolism* Protein Sorting Signals / physiology Protein Transport / physiology* Proteoglycans / physiology* |
| Chemical | |
Reg. No./Substance:
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0/Antimicrobial Cationic Peptides; 0/Membrane Glycoproteins; 0/Polymers; 0/Protein Sorting Signals; 0/Proteoglycans |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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