The Carboxy-Terminus of Apolipoprotein A-I (ApoA-I) is necessary for the Transport of lipid-free ApoA-I but not pre-lipidated ApoA-I Particles through aortic endothelial Cells
نویسندگان
چکیده
Pascale M. Ohnsorg, Lucia Rohrer, Damir Perisa, Andreas Kateifides, Angeliki Chroni, Dimitris Kardassis, Vassilis I. Zannis, and Arnold von Eckardstein From the Institute of Clinical Chemistry, University Hospital of Zurich, Switzerland; Competence Center for Systems Physiology and Metabolic Diseases, ETH and University of Zurich, Switzerland; Center for Integrative Human Physiology, University of Zurich, Switzerland;Molecular Genetics, Whitaker Cardiovascular Institute, Boston University School of Medicine, Boston, USA; National Centre of Scientific Research “Demokritos”, Institute of Biology, Athens, Greece; and Department of Biochemistry, Division of Basic Sciences, Institute of Molecular Biology & Biotechnology, University of Crete Medical School, Crete, Greece
منابع مشابه
Carboxyl terminus of apolipoprotein A-I (ApoA-I) is necessary for the transport of lipid-free ApoA-I but not prelipidated ApoA-I particles through aortic endothelial cells.
High density lipoproteins (HDL) and apolipoprotein A-I (apoA-I) must leave the circulation and pass the endothelium to exert their atheroprotective actions in the arterial wall. We previously demonstrated that the transendothelial transport of apoA-I involves ATP-binding cassette transporter (ABC) A1 and re-secretion of lipidated particles. Transendothelial transport of HDL is modulated by ABCG...
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Apolipoprotein A-I is the most abundant protein in Cyprinus carpio plasma that plays an important role in lipid transport and protection of the skin by means of its antimicrobial activity. A 527 bp cDNA fragment encoding C terminus part of apoA-I from the skin mucosa of common carp was isolated using RT-PCR. After GenBank database searching, a partial sequence containing a coding sequence (CDS)...
متن کاملMolecular characterization of apolipoprotein A-I from the skin mucosa of Cyprinus carpio
Apolipoprotein A-I is the most abundant protein in Cyprinus carpio plasma that plays an important role in lipid transport and protection of the skin by means of its antimicrobial activity. A 527 bp cDNA fragment encoding C terminus part of apoA-I from the skin mucosa of common carp was isolated using RT-PCR. After GenBank database searching, a partial sequence containing a coding sequence (CDS)...
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Five mutants of apolipoprotein A-I (apoA-I), apoA-I(Delta63-73), apoA-I(Delta140-150), apoA-I(63-73@140-150), apoA-I(R149V), and apoA-I(P143A) were compared with human plasma apoA-I for their ability to promote cholesterol and phospholipid efflux from HepG2 cells. A significantly lower capacity to promote cholesterol and phospholipid efflux was observed with lipid-free apoA-I(Delta63-73), while...
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