| pubmed-article:16002991 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16002991 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:16002991 | lifeskim:mentions | umls-concept:C0007292 | lld:lifeskim |
| pubmed-article:16002991 | lifeskim:mentions | umls-concept:C1160185 | lld:lifeskim |
| pubmed-article:16002991 | lifeskim:mentions | umls-concept:C1269765 | lld:lifeskim |
| pubmed-article:16002991 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:16002991 | pubmed:dateCreated | 2005-7-8 | lld:pubmed |
| pubmed-article:16002991 | pubmed:abstractText | Previously, we have reported that cationized-proteins covalently modified with polyethylenimine (PEI) (direct PEI-cationization) efficiently enter cells and function in the cytosol [Futami et al. (2005) J. Biosci. Bioeng. 99, 95-103]. However, it may be more convenient if a protein could be delivered into cells just by mixing the protein with a PEI-cationized carrier protein having a specific affinity (indirect PEI-cationization). Thus, we prepared PEI-cationized avidin (PEI-avidin), streptavidin (PEI-streptavidin), and protein G (PEI-protein G), and examined whether they could deliver biotinylated proteins and antibodies into living cells. PEI-avidin (and/or PEI-streptavidin) carried biotinylated GFPs into various mammalian cells very efficiently. A GFP variant containing a nuclear localization signal was found to arrive even in the nucleus. The addition of a biotinylated RNase A derivative mixed with PEI-streptavidin to a culture medium of 3T3-SV-40 cells resulted in remarkable cell growth inhibition, suggesting that the biotinylated RNase A derivative entered cells and digested intracellular RNA molecules. Furthermore, the addition of a fluorescein-labeled anti-S100C (beta-actin binding protein) antibody mixed with PEI-protein G to human fibroblasts resulted in the appearance of a fluorescence image of actin-like filamentous structures in the cells. These results indicate that indirect PEI-cationization using non-covalent interaction is as effective as the direct PEI-cationization for the transduction of proteins into living cells and for expression of their functions in the cytosol. Thus, PEI-cationized proteins having a specific affinity for certain molecules such as PEI-streptavidin, PEI-avidin and PEI-protein G are concluded to be widely applicable protein transduction carrier molecules. | lld:pubmed |
| pubmed-article:16002991 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16002991 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16002991 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16002991 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16002991 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16002991 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16002991 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16002991 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16002991 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16002991 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16002991 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16002991 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16002991 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:16002991 | pubmed:issn | 0021-924X | lld:pubmed |
| pubmed-article:16002991 | pubmed:author | pubmed-author:NambaMasayosh... | lld:pubmed |
| pubmed-article:16002991 | pubmed:author | pubmed-author:MaedaTakashiT | lld:pubmed |
| pubmed-article:16002991 | pubmed:author | pubmed-author:KitazoeMidori... | lld:pubmed |
| pubmed-article:16002991 | pubmed:author | pubmed-author:TadaHirokoH | lld:pubmed |
| pubmed-article:16002991 | pubmed:author | pubmed-author:YamadaHidenor... | lld:pubmed |
| pubmed-article:16002991 | pubmed:author | pubmed-author:SenoMasaharuM | lld:pubmed |
| pubmed-article:16002991 | pubmed:author | pubmed-author:SakaguchiMasa... | lld:pubmed |
| pubmed-article:16002991 | pubmed:author | pubmed-author:MiyazakiMasah... | lld:pubmed |
| pubmed-article:16002991 | pubmed:author | pubmed-author:NishikawaMits... | lld:pubmed |
| pubmed-article:16002991 | pubmed:author | pubmed-author:HuhNam-hoNH | lld:pubmed |
| pubmed-article:16002991 | pubmed:author | pubmed-author:MaedaYoshitak... | lld:pubmed |
| pubmed-article:16002991 | pubmed:author | pubmed-author:FutamiJunichi... | lld:pubmed |
| pubmed-article:16002991 | pubmed:author | pubmed-author:KosakaMegumiM | lld:pubmed |
| pubmed-article:16002991 | pubmed:author | pubmed-author:MurataHitoshi... | lld:pubmed |
| pubmed-article:16002991 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16002991 | pubmed:volume | 137 | lld:pubmed |
| pubmed-article:16002991 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16002991 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16002991 | pubmed:pagination | 693-701 | lld:pubmed |
| pubmed-article:16002991 | pubmed:dateRevised | 2007-12-19 | lld:pubmed |
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| pubmed-article:16002991 | pubmed:meshHeading | pubmed-meshheading:16002991... | lld:pubmed |
| pubmed-article:16002991 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16002991 | pubmed:articleTitle | Protein transduction assisted by polyethylenimine-cationized carrier proteins. | lld:pubmed |
| pubmed-article:16002991 | pubmed:affiliation | Department of Bioscience and Biotechnology, Faculty of Engineering, Graduate School of Natural Science and Technology, Okayama University, Okayama 700-8530, Japan. | lld:pubmed |
| pubmed-article:16002991 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16002991 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:16002991 | pubmed:publicationType | Evaluation Studies | lld:pubmed |
