| pubmed-article:3301616 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3301616 | lifeskim:mentions | umls-concept:C0225336 | lld:lifeskim |
| pubmed-article:3301616 | lifeskim:mentions | umls-concept:C0022801 | lld:lifeskim |
| pubmed-article:3301616 | lifeskim:mentions | umls-concept:C1882726 | lld:lifeskim |
| pubmed-article:3301616 | lifeskim:mentions | umls-concept:C0017968 | lld:lifeskim |
| pubmed-article:3301616 | lifeskim:mentions | umls-concept:C1704243 | lld:lifeskim |
| pubmed-article:3301616 | lifeskim:mentions | umls-concept:C1516240 | lld:lifeskim |
| pubmed-article:3301616 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:3301616 | pubmed:dateCreated | 1987-8-28 | lld:pubmed |
| pubmed-article:3301616 | pubmed:abstractText | The capacity of rat liver Kupffer and endothelial cells to endocytose glycoproteins with N-acetylglucosamine- or mannose-terminated oligosaccharide chains was studied. For this purpose, agalactoorosomucoid, ahexosaminoorosomucoid and horseradish peroxidase were used as ligands. A reliable determination of the amount of ligand endocytosed in vivo or in vitro was made possible by using the recently developed cold pronase method for the isolation and purification of Kupffer and endothelial cells. Both cell types participated in the uptake of the ligands in vivo as well as in vitro, but their endocytic capacity was several times greater in vivo than in vitro. Under both conditions, endothelial cells possessed a greater capacity to endocytose the ligands than did Kupffer cells. Since the total number of endothelial cells in the liver is at least twice the number of Kupffer cells, the contribution of endothelial cells to the liver uptake of N-acetylglucosamine-terminated glycoproteins in vivo was estimated to be 3 to 7 times higher than that of the Kupffer cells. In vitro experiments showed that the uptake of the glycoproteins followed saturation kinetics and was strongly inhibited at 4 degrees C and in the presence of mannan. Ultrastructural investigations revealed that horseradish peroxidase was taken up by all Kupffer and endothelial cells. These results emphasize the important role liver endothelial cells play in the clearance of specific glycoproteins from the circulation. | lld:pubmed |
| pubmed-article:3301616 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3301616 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3301616 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3301616 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3301616 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3301616 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3301616 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3301616 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3301616 | pubmed:issn | 0270-9139 | lld:pubmed |
| pubmed-article:3301616 | pubmed:author | pubmed-author:KnookD LDL | lld:pubmed |
| pubmed-article:3301616 | pubmed:author | pubmed-author:BrouwerAA | lld:pubmed |
| pubmed-article:3301616 | pubmed:author | pubmed-author:de LeeuwA MAM | lld:pubmed |
| pubmed-article:3301616 | pubmed:author | pubmed-author:Praaning-van... | lld:pubmed |
| pubmed-article:3301616 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3301616 | pubmed:volume | 7 | lld:pubmed |
| pubmed-article:3301616 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3301616 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3301616 | pubmed:pagination | 672-9 | lld:pubmed |
| pubmed-article:3301616 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:3301616 | pubmed:meshHeading | pubmed-meshheading:3301616-... | lld:pubmed |
| pubmed-article:3301616 | pubmed:meshHeading | pubmed-meshheading:3301616-... | lld:pubmed |
| pubmed-article:3301616 | pubmed:meshHeading | pubmed-meshheading:3301616-... | lld:pubmed |
| pubmed-article:3301616 | pubmed:meshHeading | pubmed-meshheading:3301616-... | lld:pubmed |
| pubmed-article:3301616 | pubmed:meshHeading | pubmed-meshheading:3301616-... | lld:pubmed |
| pubmed-article:3301616 | pubmed:meshHeading | pubmed-meshheading:3301616-... | lld:pubmed |
| pubmed-article:3301616 | pubmed:meshHeading | pubmed-meshheading:3301616-... | lld:pubmed |
| pubmed-article:3301616 | pubmed:meshHeading | pubmed-meshheading:3301616-... | lld:pubmed |
| pubmed-article:3301616 | pubmed:meshHeading | pubmed-meshheading:3301616-... | lld:pubmed |
| pubmed-article:3301616 | pubmed:meshHeading | pubmed-meshheading:3301616-... | lld:pubmed |
| pubmed-article:3301616 | pubmed:meshHeading | pubmed-meshheading:3301616-... | lld:pubmed |
| pubmed-article:3301616 | pubmed:meshHeading | pubmed-meshheading:3301616-... | lld:pubmed |
| pubmed-article:3301616 | pubmed:articleTitle | Rat liver endothelial cells have a greater capacity than Kupffer cells to endocytose N-acetylglucosamine- and mannose-terminated glycoproteins. | lld:pubmed |
| pubmed-article:3301616 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3301616 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3301616 | lld:pubmed |
