| pubmed-article:6130761 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6130761 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:6130761 | lifeskim:mentions | umls-concept:C0227525 | lld:lifeskim |
| pubmed-article:6130761 | lifeskim:mentions | umls-concept:C0023820 | lld:lifeskim |
| pubmed-article:6130761 | lifeskim:mentions | umls-concept:C0006772 | lld:lifeskim |
| pubmed-article:6130761 | lifeskim:mentions | umls-concept:C1709694 | lld:lifeskim |
| pubmed-article:6130761 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:6130761 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:6130761 | pubmed:dateCreated | 1983-3-11 | lld:pubmed |
| pubmed-article:6130761 | pubmed:abstractText | 1. Modified lipoproteins have been implicated to play a significant role in the pathogenesis of atherosclerosis. In view of this we studied the fate and mechanism of uptake in vivo of acetylated human low-density lipoprotein (acetyl-LDL). Injected intravenously into rats, acetyl-LDL is rapidly cleared from the blood. At 10min after intravenous injection, 83% of the injected dose is recovered in liver. Separation of the liver into a parenchymal and non-parenchymal cell fraction indicates that the non-parenchymal cells contain a 30-50-fold higher amount of radioactivity per mg of cell protein than the parenchymal cells. 2. When incubated in vitro, freshly isolated non-parenchymal cells show a cell-association of acetyl-LDL that is 13-fold higher per mg of cell protein than with parenchymal cells, and the degradation of acetyl-LDL is 50-fold higher. The degradation of acetyl-LDL by both cell types is blocked by chloroquine (10-50mum) and NH(4)Cl (10mm), indicating that it occurs in the lysosomes. Competition experiments indicate the presence of a specific acetyl-LDL receptor and degradation pathway, which is different from that for native LDL. 3. Degradation of acetyl-LDL by non-parenchymal cells is completely blocked by trifluoperazine, penfluridol and chlorpromazine with a relative effectivity that corresponds to their effectivity as calmodulin inhibitors. The high-affinity degradation of human LDL is also blocked by trifluoperazine (100mum). The inhibition of the processing of acetyl-LDL occurs at a site after the binding-internalization process and before intralysosomal degradation. It is suggested that calmodulin, or a target with a similar sensitivity to calmodulin inhibitors, is involved in the transport of the endocytosed acetyl-LDL to or into the lysosomes. 4. It is concluded that the liver, and in particular non-parenchymal liver cells, are in vivo the major site for acetyl-LDL uptake. This efficient uptake and degradation mechanism for acetyl-LDL in the liver might form in vivo the major protection system against the potential pathogenic action of modified lipoproteins. | lld:pubmed |
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| pubmed-article:6130761 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:6130761 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:6130761 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6130761 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:6130761 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:6130761 | pubmed:author | pubmed-author:Van BerkelT... | lld:pubmed |
| pubmed-article:6130761 | pubmed:author | pubmed-author:KruijtJ KJK | lld:pubmed |
| pubmed-article:6130761 | pubmed:author | pubmed-author:HarkeyJJ | lld:pubmed |
| pubmed-article:6130761 | pubmed:author | pubmed-author:NagelkerkeJ... | lld:pubmed |
| pubmed-article:6130761 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6130761 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:6130761 | pubmed:volume | 208 | lld:pubmed |
| pubmed-article:6130761 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6130761 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6130761 | pubmed:pagination | 493-503 | lld:pubmed |
| pubmed-article:6130761 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:6130761 | pubmed:year | 1982 | lld:pubmed |
| pubmed-article:6130761 | pubmed:articleTitle | Processing of acetylated human low-density lipoprotein by parenchymal and non-parenchymal liver cells. Involvement of calmodulin? | lld:pubmed |
| pubmed-article:6130761 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6130761 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:6130761 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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