| Apolipoprotein modulation of streptococcal serum opacity factor activity against human plasma high-density lipoproteins. | |
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MedLine Citation:
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PMID: 19618959 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Human plasma HDL are the target of streptococcal serum opacity factor (SOF), a virulence factor that clouds human plasma. Recombinant (r) SOF transfers cholesteryl esters (CE) from approximately 400,000 HDL particles to a CE-rich microemulsion (CERM), forms a cholesterol-poor HDL-like particle (neo HDL), and releases lipid-free (LF) apo A-I. Whereas the rSOF reaction requires labile apo A-I, the modulation effects of other apos are not known. We compared the products and rates of the rSOF reaction against human HDL and HDL from mice overexpressing apos A-I and A-II. Kinetic studies showed that the reactivity of various HDL species is apo-specific. LpA-I reacts faster than LpA-I/A-II. Adding apos A-I and A-II inhibited the SOF reaction, an effect that was more profound for apo A-II. The rate of SOF-mediated CERM formation was slower against HDL from mice expressing human apos A-I and A-II than against WT mice HDL and slowest against HDL from apo A-II overexpressing mice. The lower reactivity of SOF against HDL containing human apos is due to the higher hydropathy of human apo A-I, particularly its C-terminus relative to mouse apo A-I, and the higher lipophilicity of human apo A-II. The SOF-catalyzed reaction is the first to target HDL rather than its transporters and receptors in a way that enhances reverse cholesterol transport (RCT). Thus, effects of apos on the SOF reaction are highly relevant. Our studies show that the "humanized" apo A-I-expressing mouse is a good animal model for studies of rSOF effects on RCT in vivo. |
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Authors:
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Corina Rosales; Baiba K Gillard; Harry S Courtney; Francisco Blanco-Vaca; Henry J Pownall |
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Publication Detail:
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Type: Comparative Study; Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S. |
Journal Detail:
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Title: Biochemistry Volume: 48 ISSN: 1520-4995 ISO Abbreviation: Biochemistry Publication Date: 2009 Aug |
Date Detail:
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Created Date: 2009-08-18 Completed Date: 2009-09-25 Revised Date: 2012-05-04 |
Medline Journal Info:
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Nlm Unique ID: 0370623 Medline TA: Biochemistry Country: United States |
Other Details:
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Languages: eng Pagination: 8070-6 Citation Subset: IM |
Affiliation:
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Section of Atherosclerosis and Vascular Medicine, Department of Medicine, Baylor College of Medicine, Houston, Texas 77030, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Apolipoprotein A-I / biosynthesis, genetics, metabolism, physiology* Apolipoprotein A-II / biosynthesis, genetics, physiology*, secretion Catalysis Cholesterol Ester Transfer Proteins / antagonists & inhibitors, chemistry, physiology Cholesterol Esters / metabolism Emulsions Humans Lipoproteins, HDL / antagonists & inhibitors*, blood Mice Mice, Transgenic Nephelometry and Turbidimetry Peptide Fragments / biosynthesis, genetics, physiology Peptide Hydrolases / blood*, genetics, physiology Protein Binding Recombinant Proteins / blood, chemistry, genetics Streptococcus pyogenes / chemistry, physiology* |
| Grant Support | |
ID/Acronym/Agency:
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HL 30914/HL/NHLBI NIH HHS; HL056865/HL/NHLBI NIH HHS; R01 HL030914-22S1/HL/NHLBI NIH HHS; R01 HL056865/HL/NHLBI NIH HHS; R01 HL056865-09A2/HL/NHLBI NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/APOA1 protein, human; 0/APOA2 protein, human; 0/Apolipoprotein A-I; 0/Apolipoprotein A-II; 0/Cholesterol Ester Transfer Proteins; 0/Cholesterol Esters; 0/Emulsions; 0/Lipoproteins, HDL; 0/Peptide Fragments; 0/Recombinant Proteins; 0/opacity factor; EC 3.4.-/Peptide Hydrolases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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