Linked Life Data

7989348

Source:http://linkedlifedata.com/resource/pubmed/id/7989348

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
50
pubmed:dateCreated
1995-1-12
pubmed:abstractText
It has previously been shown that lipoprotein lipase can mediate uptake of remnant lipoprotein particles via binding to the low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor (LRP). Binding of lipoprotein lipase, and of triglyceride-rich lipoproteins associated with the lipase, to LRP depends on an intact carboxyl-terminal folding domain of the lipase (Nykjaer, A., Bengtsson-Olivecrona, G., Lookene, A., Moestrup, S. K., Petersen, C. M., Weber, W., Beisiegel, W., and Gliemann, J. (1993) J. Biol. Chem. 268, 15048-15055). Here we show that the site for binding to the receptor is within residues 380-425 of the bovine and residues 378-423 of the human lipoprotein lipase. We demonstrate that a carboxyl-terminal fragment of human lipoprotein lipase (residues 378-448), expressed as fusion protein in Escherichia coli, binds to purified and cellular LRP but not to lipoproteins. Binding of the fragment to purified LRP was blocked by heparin. In addition, the fragment inhibited the binding of lipase and the lipase-mediated binding of lipoproteins to the purified receptor. The fragment exhibited reduced binding to proteoglycan-deficient cells. Moreover, the fragment inhibited the uptake of lipoproteins in cells mediated by the lipase via binding to heparan sulfate proteoglycans and LRP. We conclude that the fragment contains the site for binding to LRP and a candidate site for interaction with heparan sulfate proteoglycans, whereas binding to lipoproteins is inefficient. The fragment can therefore inhibit the lipase-mediated lipoprotein uptake, a process that may promote the development of atherosclerosis when occurring in cells of the arterial wall.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
31747-55
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:7989348-Amino Acid Sequence, pubmed-meshheading:7989348-Animals, pubmed-meshheading:7989348-Base Sequence, pubmed-meshheading:7989348-Biological Transport, pubmed-meshheading:7989348-Cells, Cultured, pubmed-meshheading:7989348-DNA Primers, pubmed-meshheading:7989348-Humans, pubmed-meshheading:7989348-Lipoprotein Lipase, pubmed-meshheading:7989348-Lipoproteins, pubmed-meshheading:7989348-Lipoproteins, VLDL, pubmed-meshheading:7989348-Low Density Lipoprotein Receptor-Related Protein-1, pubmed-meshheading:7989348-Molecular Sequence Data, pubmed-meshheading:7989348-Peptide Fragments, pubmed-meshheading:7989348-Protein Binding, pubmed-meshheading:7989348-Receptors, Immunologic, pubmed-meshheading:7989348-Recombinant Fusion Proteins, pubmed-meshheading:7989348-Sequence Alignment, pubmed-meshheading:7989348-Sequence Homology, Amino Acid
pubmed:year
1994
pubmed:articleTitle
A carboxyl-terminal fragment of lipoprotein lipase binds to the low density lipoprotein receptor-related protein and inhibits lipase-mediated uptake of lipoprotein in cells.
pubmed:affiliation
Department of Medical Biochemistry, University of Aarhus, Denmark.
pubmed:publicationType
Journal Article, Comparative Study, In Vitro, Research Support, Non-U.S. Gov't