pubmed-article:16609691 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16609691 | lifeskim:mentions | umls-concept:C0032105 | lld:lifeskim |
pubmed-article:16609691 | lifeskim:mentions | umls-concept:C2717940 | lld:lifeskim |
pubmed-article:16609691 | lifeskim:mentions | umls-concept:C1327616 | lld:lifeskim |
pubmed-article:16609691 | lifeskim:mentions | umls-concept:C0070882 | lld:lifeskim |
pubmed-article:16609691 | lifeskim:mentions | umls-concept:C0120285 | lld:lifeskim |
pubmed-article:16609691 | lifeskim:mentions | umls-concept:C1959616 | lld:lifeskim |
pubmed-article:16609691 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
pubmed-article:16609691 | lifeskim:mentions | umls-concept:C1455838 | lld:lifeskim |
pubmed-article:16609691 | lifeskim:mentions | umls-concept:C1705822 | lld:lifeskim |
pubmed-article:16609691 | lifeskim:mentions | umls-concept:C0348011 | lld:lifeskim |
pubmed-article:16609691 | lifeskim:mentions | umls-concept:C0870432 | lld:lifeskim |
pubmed-article:16609691 | lifeskim:mentions | umls-concept:C1708111 | lld:lifeskim |
pubmed-article:16609691 | lifeskim:mentions | umls-concept:C1705417 | lld:lifeskim |
pubmed-article:16609691 | lifeskim:mentions | umls-concept:C1555465 | lld:lifeskim |
pubmed-article:16609691 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:16609691 | pubmed:dateCreated | 2006-4-12 | lld:pubmed |
pubmed-article:16609691 | pubmed:abstractText | Phospholipid transfer protein (PLTP) is a serum glycoprotein with a central role in high-density lipoprotein metabolism. We created a fusion protein in which enhanced green fluorescent protein (EGFP) was fused to the carboxyl-terminus of PLTP. Stably transfected HepG2 cells, which overexpress this fusion protein, were generated. PLTP-EGFP was translocated into the ER and fluoresced within the biosynthetic pathway, showing a marked concentration in the Golgi complex. The transfected cells secreted into the growth medium phospholipid transfer activity 7-fold higher than that of the mock-transfected controls. The medium of the PLTP-EGFP - expressing cells displayed EGFP fluorescence, demonstrating that both the PLTP and the EGFP moieties had attained a biologically active conformation. However, the specific activity of PLTP-EGFP in the medium was markedly reduced as compared with that of endogenous PLTP. This suggests that the EGFP attached to the carboxyl-terminal tail of PLTP interferes with the interaction of PLTP with its substrates or with the lipid transfer process itself. Fluorescently tagged PLTP is a useful tool for elucidating the intracellular functions of PLTP and the interaction of exogenously added PLTP with cells, and will provide a means of monitoring the distribution of exogenously added PLTP between serum lipoprotein subspecies. | lld:pubmed |
pubmed-article:16609691 | pubmed:language | eng | lld:pubmed |
pubmed-article:16609691 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16609691 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:16609691 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16609691 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16609691 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16609691 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16609691 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16609691 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16609691 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:16609691 | pubmed:month | Apr | lld:pubmed |
pubmed-article:16609691 | pubmed:issn | 0829-8211 | lld:pubmed |
pubmed-article:16609691 | pubmed:author | pubmed-author:JauhiainenMat... | lld:pubmed |
pubmed-article:16609691 | pubmed:author | pubmed-author:EhnholmChrist... | lld:pubmed |
pubmed-article:16609691 | pubmed:author | pubmed-author:OlkkonenVesa... | lld:pubmed |
pubmed-article:16609691 | pubmed:author | pubmed-author:SigginsSarahS | lld:pubmed |
pubmed-article:16609691 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:16609691 | pubmed:volume | 84 | lld:pubmed |
pubmed-article:16609691 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:16609691 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:16609691 | pubmed:pagination | 117-25 | lld:pubmed |
pubmed-article:16609691 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:16609691 | pubmed:meshHeading | pubmed-meshheading:16609691... | lld:pubmed |
pubmed-article:16609691 | pubmed:meshHeading | pubmed-meshheading:16609691... | lld:pubmed |
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pubmed-article:16609691 | pubmed:meshHeading | pubmed-meshheading:16609691... | lld:pubmed |
pubmed-article:16609691 | pubmed:meshHeading | pubmed-meshheading:16609691... | lld:pubmed |
pubmed-article:16609691 | pubmed:meshHeading | pubmed-meshheading:16609691... | lld:pubmed |
pubmed-article:16609691 | pubmed:meshHeading | pubmed-meshheading:16609691... | lld:pubmed |
pubmed-article:16609691 | pubmed:year | 2006 | lld:pubmed |
pubmed-article:16609691 | pubmed:articleTitle | Plasma phospholipid transfer protein fused with green fluorescent protein is secreted by HepG2 cells and displays phosphatidylcholine transfer activity. | lld:pubmed |
pubmed-article:16609691 | pubmed:affiliation | Department of Molecular Medicine, National Public HealthInstitute, Biomedicum, Helsinki, Finland. | lld:pubmed |
pubmed-article:16609691 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:16609691 | pubmed:publicationType | In Vitro | lld:pubmed |
pubmed-article:16609691 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16609691 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16609691 | lld:pubmed |