pubmed-article:6950395 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:6950395 | lifeskim:mentions | umls-concept:C0025914 | lld:lifeskim |
pubmed-article:6950395 | lifeskim:mentions | umls-concept:C0026809 | lld:lifeskim |
pubmed-article:6950395 | lifeskim:mentions | umls-concept:C0024432 | lld:lifeskim |
pubmed-article:6950395 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:6950395 | lifeskim:mentions | umls-concept:C0003595 | lld:lifeskim |
pubmed-article:6950395 | pubmed:issue | 12 | lld:pubmed |
pubmed-article:6950395 | pubmed:dateCreated | 1982-5-21 | lld:pubmed |
pubmed-article:6950395 | pubmed:abstractText | Monolayers of mouse peritoneal macrophages were shown to synthesize and secrete a protein that resembles apoprotein E (apoE), a normal constituent of plasma lipoproteins. Synthesis and secretion were studied by incubation of macrophages with L-[35S]methionine and analysis of the 35S-labeled proteins secreted into the culture medium. The 35S-labeled protein resembling apoE showed the following properties: (i) it floated in the ultracentrifuge at a density less than 1.215 g/ml, indicating that it was associated with lipid; (ii) by NaDodSO4/polyacrylamide gel electrophoresis, its Mr of 35,000 was identical to that of authentic apoE obtained from mouse plasma very low density lipoprotein; (iii) its isoelectric point of 5.4 was the same as that of authentic mouse apoE; (iv) it comigrated with authentic mouse apoE after two-dimensional isoelectric focusing/NaDodSO4/polyacrylamide gel electrophoresis; and (v) it was quantitatively precipitated by a monospecific antibody directed against rat apoE. Synthesis and secretion of the apoE-like protein was stimulated 3- to 8-fold when the macrophages were loaded with cholesterol by incubation with either acetylated low density lipoprotein (acetyl-LDL) or beta-migrating very low density lipoprotein from cholesterol-fed rabbits. When the cells were incubated with acetyl-LDL, the apoE-like protein composed approximately 2% of the total 35S-labeled protein synthesized by the cells and approximately 10% of the total 35S-labeled protein secreted into the medium. The current findings suggest a role for apoE in the plasma transport of cholesterol excreted from cholesterol-loaded macrophages. | lld:pubmed |
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pubmed-article:6950395 | pubmed:language | eng | lld:pubmed |
pubmed-article:6950395 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6950395 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:6950395 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:6950395 | pubmed:month | Dec | lld:pubmed |
pubmed-article:6950395 | pubmed:issn | 0027-8424 | lld:pubmed |
pubmed-article:6950395 | pubmed:author | pubmed-author:BrownM SMS | lld:pubmed |
pubmed-article:6950395 | pubmed:author | pubmed-author:GoldsteinJ... | lld:pubmed |
pubmed-article:6950395 | pubmed:author | pubmed-author:HavelR JRJ | lld:pubmed |
pubmed-article:6950395 | pubmed:author | pubmed-author:BasuS KSK | lld:pubmed |
pubmed-article:6950395 | pubmed:author | pubmed-author:HoY KYK | lld:pubmed |
pubmed-article:6950395 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:6950395 | pubmed:volume | 78 | lld:pubmed |
pubmed-article:6950395 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:6950395 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:6950395 | pubmed:pagination | 7545-9 | lld:pubmed |
pubmed-article:6950395 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:6950395 | pubmed:year | 1981 | lld:pubmed |
pubmed-article:6950395 | pubmed:articleTitle | Mouse macrophages synthesize and secrete a protein resembling apolipoprotein E. | lld:pubmed |
pubmed-article:6950395 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:6950395 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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