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http://purl.uniprot.org/citations/19910634http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19910634http://www.w3.org/2000/01/rdf-schema#comment"

Introduction

Apolipoprotein (apo) A-II is the second most abundant high-density lipoprotein (HDL) apolipoprotein. We assessed the mechanism involved in the altered postprandial triglyceride-rich lipoprotein metabolism of female human apoA-II-transgenic mice (hapoA-II-Tg mice), which results in up to an 11-fold increase in plasma triglyceride concentration. The relationships between apoA-II, HDL composition, and lipoprotein lipase (LPL) activity were also analyzed in a group of normolipidemic women.

Methods and results

Triglyceride-rich lipoprotein catabolism was decreased in hapoA-II-Tg mice compared to control mice. This suggests that hapoA-II, which was mainly associated with HDL during fasting and postprandially, impairs triglyceride-rich lipoprotein lipolysis. HDL isolated from hapoA-II-Tg mice impaired bovine LPL activity. Two-dimensional gel electrophoresis, mass spectrometry, and immunonephelometry identified a marked deficiency in the HDL content of apoA-I, apoC-III, and apoE in these mice. In normolipidemic women, apoA-II concentration was directly correlated with plasma triglyceride and inversely correlated with the HDL-apoC-II+apoE/apoC-III ratio [corrected]. HDL-mediated induction of LPL activity was inversely correlated with apoA-II and directly correlated with the HDL-apoC-II+apoE/apoC-III ratio [corrected]. Purified hapoA-II displaced apoC-II, apoC-III, and apoE from human HDL2. Human HDL3 was, compared to HDL2, enriched in apoA-II but poorer in apoC-II, apoC-III, and apoE.

Conclusions

ApoA-II plays a crucial role in triglyceride catabolism by regulating LPL activity, at least in part, through HDL proteome modulation."xsd:string
http://purl.uniprot.org/citations/19910634http://purl.org/dc/terms/identifier"doi:10.1161/atvbaha.109.198226"xsd:string
http://purl.uniprot.org/citations/19910634http://purl.uniprot.org/core/author"Blanco-Vaca F."xsd:string
http://purl.uniprot.org/citations/19910634http://purl.uniprot.org/core/author"Sloan J.H."xsd:string
http://purl.uniprot.org/citations/19910634http://purl.uniprot.org/core/author"Fievet C."xsd:string
http://purl.uniprot.org/citations/19910634http://purl.uniprot.org/core/author"de la Torre C."xsd:string
http://purl.uniprot.org/citations/19910634http://purl.uniprot.org/core/author"Escola-Gil J.C."xsd:string
http://purl.uniprot.org/citations/19910634http://purl.uniprot.org/core/author"Julve J."xsd:string
http://purl.uniprot.org/citations/19910634http://purl.uniprot.org/core/author"Ribas V."xsd:string
http://purl.uniprot.org/citations/19910634http://purl.uniprot.org/core/author"Rotllan N."xsd:string
http://purl.uniprot.org/citations/19910634http://purl.uniprot.org/core/author"Vallez E."xsd:string
http://purl.uniprot.org/citations/19910634http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/19910634http://purl.uniprot.org/core/name"Arterioscler Thromb Vasc Biol"xsd:string
http://purl.uniprot.org/citations/19910634http://purl.uniprot.org/core/pages"232-238"xsd:string
http://purl.uniprot.org/citations/19910634http://purl.uniprot.org/core/title"Human apolipoprotein A-II determines plasma triglycerides by regulating lipoprotein lipase activity and high-density lipoprotein proteome."xsd:string
http://purl.uniprot.org/citations/19910634http://purl.uniprot.org/core/volume"30"xsd:string
http://purl.uniprot.org/citations/19910634http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/19910634
http://purl.uniprot.org/citations/19910634http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/19910634
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