| HDL-ApoE content regulates the displacement of hepatic lipase from cell surface proteoglycans. | |
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MedLine Citation:
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PMID: 19528346 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Human hepatic lipase (HL) is an interfacial enzyme that must be liberated from cell surface proteoglycans to hydrolyze lipoprotein triglyceride. Both high-density lipoprotein (HDL) and apolipoprotein (apo)A-I can displace HL from cell surface proteoglycans, much like heparin. HL displacement is inhibited by HDL-apoE content. Postprandial HDL is approximately twofold better at displacing HL than is fasting HDL, but only has approximately one-half the apoE content. Enriching native HDL with triglyceride decreases HDL-apoE content and increases HL displacement. Incubation of HDL with the anti-apoE antibody, 6C5, also increases HL displacement. In contrast, enrichment of synthetic HDL with apoE significantly inhibits HL displacement. HDL from fasted female normolipidemic subjects displaces HL approximately twofold better than HDL from male subjects. HDL from female subjects also has significantly less apoE than HDL from males. Normolipidemic females have increased circulating HDL-bound HL. Hyperlipidemia has little effect on the HL displacement ability of HDL from men, whereas HDL from hypercholesterolemic females exhibits impaired HL displacement. HL displacement from liver heparan sulfate proteoglycans therefore appears to be linked to interlipoprotein apoE exchange. Decreased HL displacement is associated with higher HDL-apoE levels and may therefore affect vascular triglyceride hydrolysis. |
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Authors:
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Elizabeth K Young; Cynthia Chatterjee; Daniel L Sparks |
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Publication Detail:
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Type: Journal Article Date: 2009-06-15 |
Journal Detail:
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Title: The American journal of pathology Volume: 175 ISSN: 1525-2191 ISO Abbreviation: Am. J. Pathol. Publication Date: 2009 Jul |
Date Detail:
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Created Date: 2009-06-26 Completed Date: 2009-07-15 Revised Date: 2010-09-24 |
Medline Journal Info:
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Nlm Unique ID: 0370502 Medline TA: Am J Pathol Country: United States |
Other Details:
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Languages: eng Pagination: 448-57 Citation Subset: AIM; IM |
Affiliation:
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University of Ottawa Heart Institute, 40 Ruskin Street, Ottawa, Ontario, Canada. dsparks@ottawaheart.ca |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Apolipoproteins E
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chemistry,
metabolism* Cell Membrane / chemistry, metabolism* Cholesterol, HDL / chemistry, metabolism* Enzyme-Linked Immunosorbent Assay Female Humans Hypercholesterolemia / metabolism Immunoblotting Lipase / metabolism* Male Proteoglycans / metabolism* Sex Characteristics |
| Chemical | |
Reg. No./Substance:
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0/Apolipoproteins E; 0/Cholesterol, HDL; 0/Proteoglycans; EC 3.1.1.3/Lipase; EC 3.1.1.3/hepatic lipase, human |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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