Document Detail


Macrophage proteases can modify low density lipoproteins to increase their uptake by macrophages.
MedLine Citation:
PMID:  2201569     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
When low density lipoprotein (LDL) was incubated with sonicated macrophages at acidic pH, its protein moiety was partially degraded by cathepsins B and D. The reisolated LDL was taken up by intact macrophages up to about 20 times as fast as control LDL. LDL proteolysis and its enhanced uptake could be inhibited almost entirely by the selective protease inhibitors leupeptin and pepstatin. If macrophages in atherosclerotic lesions were to release acidic proteases (either by exocytosis or following cell death) and these were to modify LDL, this may help to explain why so much cholesteryl ester accumulates in these cells.
Authors:
D S Leake; S M Rankin; J Collard
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Publication Detail:
Type:  In Vitro; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  FEBS letters     Volume:  269     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  1990 Aug 
Date Detail:
Created Date:  1990-09-27     Completed Date:  1990-09-27     Revised Date:  2009-09-29    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  209-12     Citation Subset:  IM    
Affiliation:
Division of Biomedical Sciences, King's College London (University of London), UK.
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MeSH Terms
Descriptor/Qualifier:
Animals
Apolipoprotein B-100
Apolipoproteins B / metabolism
Lipoproteins, LDL / metabolism*
Macrophages / enzymology,  metabolism*
Mice
Peptide Hydrolases / metabolism*
Protease Inhibitors / pharmacology
Grant Support
ID/Acronym/Agency:
//Wellcome Trust
Chemical
Reg. No./Substance:
0/Apolipoprotein B-100; 0/Apolipoproteins B; 0/Lipoproteins, LDL; 0/Protease Inhibitors; EC 3.4.-/Peptide Hydrolases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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