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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1992-5-14
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pubmed:abstractText |
We investigated the effects of polymyxin B (PMB), an antibiotic that binds to endotoxins, on the uptake and degradation of low density lipoproteins (LDLs) in HepG2 cells, a highly differentiated human hepatoma cell line. The results showed that PMB very effectively enhanced the binding, internalization, and degradation of LDL in HepG2 cells. The PMB-mediated enhancement of LDL uptake was not dependent on the LDL receptor-mediated pathway, as blockage of the LDL receptor by use of a monoclonal anti-LDL receptor antibody had no effect on the PMB-mediated cellular processing of LDL and PMB-mediated enhancement of LDL uptake did not cause an increase in cholesterol esterification. In addition, chloroquine and colchicine, which inhibit lysosomal degradation and cellular endocytosis, respectively, diminished PMB-enhanced degradation of LDL, indicating that PMB mediates uptake through a pathway similar to the LDL receptor-mediated pathway. The PMB-mediated uptake of LDL was sensitive to treatment with phospholipase C and pronase and was dependent on the presence of Ca2+. PMB caused similar changes in human skin fibroblasts, bovine smooth muscle cells, and bovine endothelial cells, which suggests that PMB-enhanced LDL uptake is a general cellular phenomenon. Our results thus indicate that PMB increases cellular catabolism of LDL through an endocytotic pathway not involving the LDL receptors.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Chloroquine,
http://linkedlifedata.com/resource/pubmed/chemical/Colchicine,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, LDL,
http://linkedlifedata.com/resource/pubmed/chemical/Polymyxin B,
http://linkedlifedata.com/resource/pubmed/chemical/Pronase,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, LDL,
http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1049-8834
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
503-11
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:1313696-Animals,
pubmed-meshheading:1313696-Calcium,
pubmed-meshheading:1313696-Carcinoma, Hepatocellular,
pubmed-meshheading:1313696-Cattle,
pubmed-meshheading:1313696-Cells, Cultured,
pubmed-meshheading:1313696-Chloroquine,
pubmed-meshheading:1313696-Colchicine,
pubmed-meshheading:1313696-Endothelium, Vascular,
pubmed-meshheading:1313696-Fibroblasts,
pubmed-meshheading:1313696-Humans,
pubmed-meshheading:1313696-Lipoproteins, LDL,
pubmed-meshheading:1313696-Liver,
pubmed-meshheading:1313696-Liver Neoplasms,
pubmed-meshheading:1313696-Muscle, Smooth,
pubmed-meshheading:1313696-Polymyxin B,
pubmed-meshheading:1313696-Pronase,
pubmed-meshheading:1313696-Receptors, LDL,
pubmed-meshheading:1313696-Tumor Cells, Cultured,
pubmed-meshheading:1313696-Type C Phospholipases
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pubmed:year |
1992
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pubmed:articleTitle |
Polymyxin B enhances low density lipoprotein catabolism in hepatic and extrahepatic cells.
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pubmed:affiliation |
Department of Internal Medicine, Lund University, Malmö General Hospital, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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