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• W2016180547 startingPage "10597" @default.
• W2016180547 abstract "Targeting of drug carriers to cell-surface receptors involved in endocytosis is commonly used for intracellular drug delivery. However, most endocytic receptors mediate uptake via clathrin or caveolar pathways associated with ≤200-nm vesicles, restricting carrier design. We recently showed that endocytosis mediated by intercellular adhesion molecule 1 (ICAM-1), which differs from clathrin- and caveolae-mediated pathways, allows uptake of nano- and microcarriers in cell culture and in vivo due to recruitment of cellular sphingomyelinases to the plasmalemma. This leads to ceramide generation at carrier binding sites and formation of actin stress-fibers, enabling engulfment and uptake of a wide size-range of carriers. Here we adapted this paradigm to enhance uptake of drug carriers targeted to receptors associated with size-restricted pathways. We coated sphingomyelinase onto model (polystyrene) submicro- and microcarriers targeted to clathrin-associated mannose-6-phosphate receptor. In endothelial cells, this provided ceramide enrichment at the cell surface and actin stress-fiber formation, modifying the uptake pathway and enhancing carrier endocytosis without affecting targeting, endosomal transport, cell-associated degradation, or cell viability. This improvement depended on the carrier size and enzyme dose, and similar results were observed for other receptors (transferrin receptor) and cell types (epithelial cells). This phenomenon also enhanced tissue accumulation of carriers after intravenous injection in mice. Hence, it is possible to maintain targeting toward a selected receptor while bypassing natural size restrictions of its associated endocytic route by functionalization of drug carriers with biological elements mimicking the ICAM-1 pathway. This strategy holds considerable promise to enhance flexibility of design of targeted drug delivery systems." @default.
• W2016180547 created "2016-06-24" @default.
• W2016180547 creator A5000819682 @default.
• W2016180547 creator A5023585056 @default.
• W2016180547 creator A5029014892 @default.
• W2016180547 creator A5040577651 @default.
• W2016180547 creator A5068648493 @default.
• W2016180547 date "2013-11-20" @default.
• W2016180547 modified "2023-10-14" @default.
• W2016180547 title "Biological Functionalization of Drug Delivery Carriers To Bypass Size Restrictions of Receptor-Mediated Endocytosis Independently from Receptor Targeting" @default.
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• W2016180547 doi "https://doi.org/10.1021/nn404719c" @default.
• W2016180547 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3901850" @default.
• W2016180547 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24237309" @default.
• W2016180547 hasPublicationYear "2013" @default.
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