| pubmed-article:18367474 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18367474 | lifeskim:mentions | umls-concept:C0178719 | lld:lifeskim |
| pubmed-article:18367474 | lifeskim:mentions | umls-concept:C0597361 | lld:lifeskim |
| pubmed-article:18367474 | lifeskim:mentions | umls-concept:C0079925 | lld:lifeskim |
| pubmed-article:18367474 | lifeskim:mentions | umls-concept:C0011209 | lld:lifeskim |
| pubmed-article:18367474 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:18367474 | pubmed:dateCreated | 2008-5-7 | lld:pubmed |
| pubmed-article:18367474 | pubmed:abstractText | We describe the synthesis and characterization of a 5' conjugate between a 2'-O-Me phosphorothioate antisense oligonucleotide and a bivalent RGD (arginine-glycine-aspartic acid) peptide that is a high-affinity ligand for the alphavbeta3 integrin. We used alphavbeta3-positive melanoma cells transfected with a reporter comprised of the firefly luciferase gene interrupted by an abnormally spliced intron. Intranuclear delivery of a specific antisense oligonucleotide (termed 623) corrects splicing and allows luciferase expression in these cells. The RGD-623 conjugate or a cationic lipid-623 complex produced significant increases in luciferase expression, while 'free' 623 did not. However, the kinetics of luciferase expression was distinct; the RGD-623 conjugate produced a gradual increase followed by a gradual decline, while the cationic lipid-623 complex caused a rapid increase followed by a monotonic decline. The subcellular distribution of the oligonucleotide delivered using cationic lipids included both cytoplasmic vesicles and the nucleus, while the RGD-623 conjugate was primarily found in cytoplasmic vesicles that partially co-localized with a marker for caveolae. Both the cellular uptake and the biological effect of the RGD-623 conjugate were blocked by excess RGD peptide. These observations suggest that the bivalent RGD peptide-oligonucleotide conjugate enters cells via a process of receptor-mediated endocytosis mediated by the alphavbeta3 integrin. | lld:pubmed |
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| pubmed-article:18367474 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18367474 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18367474 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18367474 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18367474 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:18367474 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18367474 | pubmed:month | May | lld:pubmed |
| pubmed-article:18367474 | pubmed:issn | 1362-4962 | lld:pubmed |
| pubmed-article:18367474 | pubmed:author | pubmed-author:FisherMichael... | lld:pubmed |
| pubmed-article:18367474 | pubmed:author | pubmed-author:JulianoRudy... | lld:pubmed |
| pubmed-article:18367474 | pubmed:author | pubmed-author:ChenXiaoyuanX | lld:pubmed |
| pubmed-article:18367474 | pubmed:author | pubmed-author:KangHyunminH | lld:pubmed |
| pubmed-article:18367474 | pubmed:author | pubmed-author:TrejoJoannJ | lld:pubmed |
| pubmed-article:18367474 | pubmed:author | pubmed-author:DixitVidulaV | lld:pubmed |
| pubmed-article:18367474 | pubmed:author | pubmed-author:LiZi-BoZB | lld:pubmed |
| pubmed-article:18367474 | pubmed:author | pubmed-author:AlamMd... | lld:pubmed |
| pubmed-article:18367474 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18367474 | pubmed:volume | 36 | lld:pubmed |
| pubmed-article:18367474 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18367474 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18367474 | pubmed:pagination | 2764-76 | lld:pubmed |
| pubmed-article:18367474 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:18367474 | pubmed:meshHeading | pubmed-meshheading:18367474... | lld:pubmed |
| pubmed-article:18367474 | pubmed:meshHeading | pubmed-meshheading:18367474... | lld:pubmed |
