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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
2010-7-2
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pubmed:abstractText |
Guanidinylated neomycin (GNeo) can transport bioactive, high molecular weight cargo into the interior of cells in a process that depends on cell surface heparan sulfate proteoglycans. In this report, we show that GNeo-modified quantum dots bind to cell surface heparan sulfate, undergo endocytosis and eventually reach the lysosomal compartment. An N-hydroxysuccinimide activated ester of GNeo (GNeo-NHS) was prepared and conjugated to two lysosomal enzymes, beta-D-glucuronidase (GUS) and alpha-L-iduronidase. Conjugation did not interfere with enzyme activity and enabled binding of the enzymes to heparin-Sepharose and heparan sulfate on primary human fibroblasts. Cells lacking the corresponding lysosomal enzyme took up sufficient amounts of the conjugated enzymes to restore normal turnover of glycosaminoglycans. The high capacity of proteoglycan-mediated uptake suggests that this method of delivery might be used for enzyme replacement or introduction of foreign enzymes into cells.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/20442709-10872465,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20442709-11042114,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20442709-11149851,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20442709-11336786,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20442709-11562370,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20442709-12612639,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20442709-12782143,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20442709-14523939,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20442709-14531657,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20442709-14992581,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20442709-16043103,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20442709-16333858,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20442709-16945147,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20442709-17209559,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20442709-17311923,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20442709-17460664,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20442709-17635154,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20442709-17763452,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20442709-18025928,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20442709-18045727,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20442709-18460924,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20442709-19805913,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20442709-3315809,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20442709-8993162
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1525-0024
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
18
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1268-74
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pubmed:dateRevised |
2011-8-1
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pubmed:meshHeading |
pubmed-meshheading:20442709-Animals,
pubmed-meshheading:20442709-CHO Cells,
pubmed-meshheading:20442709-Cells, Cultured,
pubmed-meshheading:20442709-Cricetinae,
pubmed-meshheading:20442709-Cricetulus,
pubmed-meshheading:20442709-Endocytosis,
pubmed-meshheading:20442709-Glucuronidase,
pubmed-meshheading:20442709-Glycosaminoglycans,
pubmed-meshheading:20442709-Heparitin Sulfate,
pubmed-meshheading:20442709-Humans,
pubmed-meshheading:20442709-Iduronidase,
pubmed-meshheading:20442709-Lysosomes,
pubmed-meshheading:20442709-Microscopy, Fluorescence,
pubmed-meshheading:20442709-Molecular Structure,
pubmed-meshheading:20442709-Neomycin,
pubmed-meshheading:20442709-Quantum Dots
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pubmed:year |
2010
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pubmed:articleTitle |
Guanidinylated neomycin mediates heparan sulfate-dependent transport of active enzymes to lysosomes.
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pubmed:affiliation |
Department of Cellular and Molecular Medicine, Glycobiology Research and Training Center, University of California-San Diego, La Jolla, California 92093-0687, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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