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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2010-3-1
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pubmed:abstractText |
Human apolipoprotein A-IV (apoA-IV) is involved in chylomicron assembly and secretion, and in reverse cholesterol transport. Several apoA-IV isoforms exist, the most common in Caucasian populations being apoA-IV-1a (T347S) and apoA-IV-2 (Q360H). The objective of the present study was to investigate the impact of these common aminoacid substitutions on the ability of apoA-IV to bind lipids, to promote cell cholesterol efflux via ABCA1, and to maintain endothelial homeostasis. Recombinant forms of wild-type apoA-IV, apoA-IV Q360H, and apoA-IV T347S were produced in Escherichia coli. ApoA-IV Q360H and apoA-IV T347S showed a slightly higher alpha-helical content compared to wild-type apoA-IV, and associated with phospholipids faster than wild-type apoA-IV. The capacity to promote ABCA1-mediated cholesterol efflux was significantly greater for the apoA-IV T347S than the other apoA-IV isoforms. No differences were observed in the ability of apoA-IV isoforms to inhibit the production of VCAM-1 and IL-6 in TNFalpha-stimulated endothelial cells. In conclusion, the apoA-IV T347S common variant has increased lipid binding properties and cholesterol efflux capacity, while the apoA-IV Q360H variant has only slightly increased lipid binding properties. The two common aminoacid substitutions have no effect on the ability of apoA-IV to maintain endothelial homeostasis.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Inflammatory Agents...,
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoproteins A,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamine,
http://linkedlifedata.com/resource/pubmed/chemical/Histidine,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-6,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, HDL,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/Threonine,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/Vascular Cell Adhesion Molecule-1,
http://linkedlifedata.com/resource/pubmed/chemical/apolipoprotein A-IV
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1090-2104
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pubmed:author |
pubmed-author:BarbiroliAlbertoA,
pubmed-author:BerniniFrancoF,
pubmed-author:BonomiFrancescoF,
pubmed-author:CalabresiLauraL,
pubmed-author:FavariEldaE,
pubmed-author:FranceschiniGuidoG,
pubmed-author:GomaraschiMonicaM,
pubmed-author:IamettiStefaniaS,
pubmed-author:PozziSilviaS,
pubmed-author:PuttWendy EWE,
pubmed-author:TalmudPhilippa JPJ
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pubmed:copyrightInfo |
Copyright 2010 Elsevier Inc. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
26
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pubmed:volume |
393
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
126-30
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pubmed:meshHeading |
pubmed-meshheading:20117098-Amino Acid Substitution,
pubmed-meshheading:20117098-Animals,
pubmed-meshheading:20117098-Anti-Inflammatory Agents, Non-Steroidal,
pubmed-meshheading:20117098-Apolipoproteins A,
pubmed-meshheading:20117098-Cell Line,
pubmed-meshheading:20117098-Cholesterol,
pubmed-meshheading:20117098-Endothelium, Vascular,
pubmed-meshheading:20117098-Glutamine,
pubmed-meshheading:20117098-Histidine,
pubmed-meshheading:20117098-Homeostasis,
pubmed-meshheading:20117098-Humans,
pubmed-meshheading:20117098-Inflammation,
pubmed-meshheading:20117098-Interleukin-6,
pubmed-meshheading:20117098-Lipid Metabolism,
pubmed-meshheading:20117098-Lipoproteins, HDL,
pubmed-meshheading:20117098-Mice,
pubmed-meshheading:20117098-Protein Structure, Secondary,
pubmed-meshheading:20117098-Serine,
pubmed-meshheading:20117098-Threonine,
pubmed-meshheading:20117098-Tumor Necrosis Factor-alpha,
pubmed-meshheading:20117098-Vascular Cell Adhesion Molecule-1
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pubmed:year |
2010
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pubmed:articleTitle |
Structure and function of the apoA-IV T347S and Q360H common variants.
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pubmed:affiliation |
Center E. Grossi Paoletti, Department of Pharmacological Sciences, Università degli Studi di Milano, 20133 Milano, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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