| Serum opacity factor enhances HDL-mediated cholesterol efflux, esterification and anti inflammatory effects. | |
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MedLine Citation:
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PMID: 20972840 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Serum opacity factor (SOF) is a streptococcal protein that disrupts the structure of human high density lipoproteins (HDL) releasing lipid-free apo A-I while forming a large cholesteryl ester-rich particle and a small neo HDL. Given its low cholesterol and high phospholipid contents, we tested the hypotheses that neo HDL is a better substrate for cholesterol esterification via lecithin:cholesterol acyltransferase (LCAT), better than HDL as an acceptor of THP-1 macrophage cholesterol efflux, and improves reduction of oxidized LDL-induced production of inflammatory markers. We observed that both cholesterol efflux and esterification were improved by recombinant (r)SOF treatment of whole plasma and that the underlying cause of the improved cholesterol esterification in plasma and macrophage cholesterol efflux to rSOF-treated plasma was due to the rSOF-mediated conversion of HDL to neo HDL. Moreover, the reduction of secretion of TNF-α and IL-6 by THP-1 cells by neo HDL was twice that of HDL. Studies in BHK cells overexpressing cholesterol transporters showed that efflux to neo HDL occurred primarily via ABCA1 not ABCG1. Thus, rSOF improves two steps in reverse cholesterol transport with a concomitant reduction in the release of macrophage markers of inflammation. We conclude that rSOF catalyzes a novel reaction that might be developed as a new therapy that prevents or reverses atherosclerosis via improved reverse cholesterol transport. |
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Authors:
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Urbain Tchoua; Corina Rosales; Daming Tang; Baiba K Gillard; Ashley Vaughan; Hu Yu Lin; Harry S Courtney; Henry J Pownall |
Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S. Date: 2010-10-24 |
Journal Detail:
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Title: Lipids Volume: 45 ISSN: 1558-9307 ISO Abbreviation: Lipids Publication Date: 2010 Dec |
Date Detail:
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Created Date: 2010-11-24 Completed Date: 2011-03-10 Revised Date: 2012-05-04 |
Medline Journal Info:
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Nlm Unique ID: 0060450 Medline TA: Lipids Country: Germany |
Other Details:
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Languages: eng Pagination: 1117-26 Citation Subset: IM |
Affiliation:
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Department of Medicine, Baylor College of Medicine, MSA601, One Baylor Plaza, Houston, TX 77030, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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ATP-Binding Cassette Transporters
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metabolism Animals Anti-Inflammatory Agents / metabolism* Cells, Cultured Cholesterol / metabolism* Cholesterol, HDL / metabolism* Cricetinae Esterification Humans Inflammation / metabolism Macrophages / metabolism Peptide Hydrolases / metabolism* Phosphatidylcholine-Sterol O-Acyltransferase / metabolism |
| Grant Support | |
ID/Acronym/Agency:
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HL-30914/HL/NHLBI NIH HHS; HL-56865/HL/NHLBI NIH HHS; R01 HL030914-22/HL/NHLBI NIH HHS; R01 HL056865/HL/NHLBI NIH HHS; R01 HL056865-10/HL/NHLBI NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/ATP binding cassette transporter 1; 0/ATP-Binding Cassette Transporters; 0/Anti-Inflammatory Agents; 0/Cholesterol, HDL; 0/opacity factor; 57-88-5/Cholesterol; EC 2.3.1.43/Phosphatidylcholine-Sterol O-Acyltransferase; EC 3.4.-/Peptide Hydrolases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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