The 5A apolipoprotein A-I mimetic peptide displays anti-inflammatory and antioxidant properties in vivo and in vitro
Identifieur interne : 001349 ( Pmc/Curation ); précédent : 001348; suivant : 001350The 5A apolipoprotein A-I mimetic peptide displays anti-inflammatory and antioxidant properties in vivo and in vitro
Auteurs : Fatiha Tabet [Australie] ; Alan T. Remaley [États-Unis] ; Aude I. Segaliny [Australie] ; Jonathan Millet [Australie] ; Ling Yan [Australie] ; Shirley Nakhla [Australie] ; Philip J. Barter [Australie] ; Kerry-Anne Rye [Australie] ; Gilles Lambert [Australie, France]Source :
- Arteriosclerosis, thrombosis, and vascular biology [ 1079-5642 ] ; 2009.
Abstract
The apolipoprotein (apo) A-I mimetic peptide 5A is highly specific for ABCA1-transporter mediated cholesterol efflux. We investigated whether the 5A peptide shares other beneficial features of apoA-I, such as protection against inflammation and oxidation.
New-Zealand White rabbits received an infusion of apoA-I, reconstituted HDL containing apoA-I ((A-I)rHDL) or the 5A peptide complexed with phospholipids (PLPC), prior to inserting a collar around the carotid artery. Human coronary artery endothelial cells (HCAECs) were incubated with (A-I)rHDL or 5A/PLPC prior to TNFa stimulation.
ApoA-I, (A-I)rHDL and 5A/PLPC reduced the collar mediated increase in (i) endothelial expression of cell adhesion molecules VCAM-1 and ICAM-1, (ii) O2− production as well as the expression of the Nox4 catalytic subunits of the NADPH oxidase, and (iii) infiltration of circulating neutrophils into the carotid intima-media. In HCAECs, both 5A/PLPC and (A-I)rHDL inhibited TNFa induced ICAM-1 and VCAM-1 expression as well as the NF-κB signalling cascade and O2− production. The effects of the 5A/PLPC complex were no longer apparent in HCAECs knocked down for ABCA1.
Like apoA-I, the 5A peptide inhibits acute inflammation and oxidative stress in rabbit carotids and HCAECs. In vitro, the 5A peptide exerts these beneficial effects through interaction with ABCA1.
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DOI: 10.1161/ATVBAHA.109.200196
PubMed: 19965776
PubMed Central: 2828392
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Remaley</name><affiliation wicri:level="1"><nlm:aff id="A2">National Heart Lung and Blood Institute, Pulmonary and Vascular Medicine Branch, Lipoprotein Metabolism Section, Bethesda, MD, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>National Heart Lung and Blood Institute, Pulmonary and Vascular Medicine Branch, Lipoprotein Metabolism Section, Bethesda, MD</wicri:regionArea></affiliation></author><author><name sortKey="Segaliny, Aude I" sort="Segaliny, Aude I" uniqKey="Segaliny A" first="Aude I." last="Segaliny">Aude I. 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Remaley</name><affiliation wicri:level="1"><nlm:aff id="A2">National Heart Lung and Blood Institute, Pulmonary and Vascular Medicine Branch, Lipoprotein Metabolism Section, Bethesda, MD, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>National Heart Lung and Blood Institute, Pulmonary and Vascular Medicine Branch, Lipoprotein Metabolism Section, Bethesda, MD</wicri:regionArea></affiliation></author><author><name sortKey="Segaliny, Aude I" sort="Segaliny, Aude I" uniqKey="Segaliny A" first="Aude I." last="Segaliny">Aude I. Segaliny</name><affiliation wicri:level="1"><nlm:aff id="A1">Lipid Research Group, The Heart Research Institute, Sydney, New South Wales, Australia</nlm:aff><country xml:lang="fr">Australie</country><wicri:regionArea>Lipid Research Group, The Heart Research Institute, Sydney, New South Wales</wicri:regionArea></affiliation></author><author><name sortKey="Millet, Jonathan" sort="Millet, Jonathan" uniqKey="Millet J" first="Jonathan" last="Millet">Jonathan Millet</name><affiliation wicri:level="1"><nlm:aff id="A1">Lipid Research Group, The Heart Research Institute, Sydney, New South Wales, Australia</nlm:aff><country xml:lang="fr">Australie</country><wicri:regionArea>Lipid Research Group, The Heart Research Institute, Sydney, New South Wales</wicri:regionArea></affiliation></author><author><name sortKey="Yan, Ling" sort="Yan, Ling" uniqKey="Yan L" first="Ling" last="Yan">Ling Yan</name><affiliation wicri:level="1"><nlm:aff id="A1">Lipid Research Group, The Heart Research Institute, Sydney, New South Wales, Australia</nlm:aff><country xml:lang="fr">Australie</country><wicri:regionArea>Lipid Research Group, The Heart Research Institute, Sydney, New South Wales</wicri:regionArea></affiliation></author><author><name sortKey="Nakhla, Shirley" sort="Nakhla, Shirley" uniqKey="Nakhla S" first="Shirley" last="Nakhla">Shirley Nakhla</name><affiliation wicri:level="1"><nlm:aff id="A1">Lipid Research Group, The Heart Research Institute, Sydney, New South Wales, Australia</nlm:aff><country xml:lang="fr">Australie</country><wicri:regionArea>Lipid Research Group, The Heart Research Institute, Sydney, New South Wales</wicri:regionArea></affiliation></author><author><name sortKey="Barter, Philip J" sort="Barter, Philip J" uniqKey="Barter P" first="Philip J." last="Barter">Philip J. Barter</name><affiliation wicri:level="1"><nlm:aff id="A1">Lipid Research Group, The Heart Research Institute, Sydney, New South Wales, Australia</nlm:aff><country xml:lang="fr">Australie</country><wicri:regionArea>Lipid Research Group, The Heart Research Institute, Sydney, New South Wales</wicri:regionArea></affiliation><affiliation wicri:level="1"><nlm:aff id="A4">Faculty of Medicine, University of Sydney, New South Wales, Australia</nlm:aff><country xml:lang="fr">Australie</country><wicri:regionArea>Faculty of Medicine, University of Sydney, New South Wales</wicri:regionArea></affiliation></author><author><name sortKey="Rye, Kerry Anne" sort="Rye, Kerry Anne" uniqKey="Rye K" first="Kerry-Anne" last="Rye">Kerry-Anne Rye</name><affiliation wicri:level="1"><nlm:aff id="A1">Lipid Research Group, The Heart Research Institute, Sydney, New South Wales, Australia</nlm:aff><country xml:lang="fr">Australie</country><wicri:regionArea>Lipid Research Group, The Heart Research Institute, Sydney, New South Wales</wicri:regionArea></affiliation><affiliation wicri:level="1"><nlm:aff id="A3">Department of Medicine, University of Melbourne, Melbourne, Victoria, Australia</nlm:aff><country xml:lang="fr">Australie</country><wicri:regionArea>Department of Medicine, University of Melbourne, Melbourne, Victoria</wicri:regionArea></affiliation><affiliation wicri:level="1"><nlm:aff id="A4">Faculty of Medicine, University of Sydney, New South Wales, Australia</nlm:aff><country xml:lang="fr">Australie</country><wicri:regionArea>Faculty of Medicine, University of Sydney, New South Wales</wicri:regionArea></affiliation></author><author><name sortKey="Lambert, Gilles" sort="Lambert, Gilles" uniqKey="Lambert G" first="Gilles" last="Lambert">Gilles Lambert</name><affiliation wicri:level="1"><nlm:aff id="A1">Lipid Research Group, The Heart Research Institute, Sydney, New South Wales, Australia</nlm:aff><country xml:lang="fr">Australie</country><wicri:regionArea>Lipid Research Group, The Heart Research Institute, Sydney, New South Wales</wicri:regionArea></affiliation><affiliation wicri:level="1"><nlm:aff id="A5">Université de Nantes, Faculté de Médecine, Nantes, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>Université de Nantes, Faculté de Médecine, Nantes</wicri:regionArea></affiliation></author></analytic><series><title level="j">Arteriosclerosis, thrombosis, and vascular biology</title><idno type="ISSN">1079-5642</idno><idno type="eISSN">1524-4636</idno><imprint><date when="2009">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><sec id="S1"><title>Objectives</title><p id="P1">The apolipoprotein (apo) A-I mimetic peptide 5A is highly specific for ABCA1-transporter mediated cholesterol efflux. We investigated whether the 5A peptide shares other beneficial features of apoA-I, such as protection against inflammation and oxidation.</p></sec><sec sec-type="methods" id="S2"><title>Methods</title><p id="P2">New-Zealand White rabbits received an infusion of apoA-I, reconstituted HDL containing apoA-I ((A-I)rHDL) or the 5A peptide complexed with phospholipids (PLPC), prior to inserting a collar around the carotid artery. Human coronary artery endothelial cells (HCAECs) were incubated with (A-I)rHDL or 5A/PLPC prior to TNFa stimulation.</p></sec><sec id="S3"><title>Results</title><p id="P3">ApoA-I, (A-I)rHDL and 5A/PLPC reduced the collar mediated increase in (i) endothelial expression of cell adhesion molecules VCAM-1 and ICAM-1, (ii) O<sub>2</sub><sup>−</sup> production as well as the expression of the Nox4 catalytic subunits of the NADPH oxidase, and (iii) infiltration of circulating neutrophils into the carotid intima-media. In HCAECs, both 5A/PLPC and (A-I)rHDL inhibited TNFa induced ICAM-1 and VCAM-1 expression as well as the NF-κB signalling cascade and O<sub>2</sub><sup>−</sup> production. The effects of the 5A/PLPC complex were no longer apparent in HCAECs knocked down for ABCA1.</p></sec><sec id="S4"><title>Conclusion</title><p id="P4">Like apoA-I, the 5A peptide inhibits acute inflammation and oxidative stress in rabbit carotids and HCAECs. In vitro, the 5A peptide exerts these beneficial effects through interaction with ABCA1.</p></sec></div></front></TEI><pmc article-type="research-article" xml:lang="EN"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<pmc-dir>properties manuscript</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-journal-id">9505803</journal-id><journal-id journal-id-type="pubmed-jr-id">8623</journal-id><journal-id journal-id-type="nlm-ta">Arterioscler Thromb Vasc Biol</journal-id><journal-title>Arteriosclerosis, thrombosis, and vascular biology</journal-title><issn pub-type="ppub">1079-5642</issn><issn pub-type="epub">1524-4636</issn></journal-meta><article-meta><article-id pub-id-type="pmid">19965776</article-id><article-id pub-id-type="pmc">2828392</article-id><article-id pub-id-type="doi">10.1161/ATVBAHA.109.200196</article-id><article-id pub-id-type="manuscript">NIHMS172804</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>The 5A apolipoprotein A-I mimetic peptide displays anti-inflammatory and antioxidant properties in vivo and in vitro</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Tabet</surname><given-names>Fatiha</given-names></name><xref ref-type="aff" rid="A1">1</xref></contrib><contrib contrib-type="author"><name><surname>Remaley</surname><given-names>Alan T.</given-names></name><xref ref-type="aff" rid="A2">2</xref></contrib><contrib contrib-type="author"><name><surname>Segaliny</surname><given-names>Aude I.</given-names></name><xref ref-type="aff" rid="A1">1</xref></contrib><contrib contrib-type="author"><name><surname>Millet</surname><given-names>Jonathan</given-names></name><xref ref-type="aff" rid="A1">1</xref></contrib><contrib contrib-type="author"><name><surname>Yan</surname><given-names>Ling</given-names></name><xref ref-type="aff" rid="A1">1</xref></contrib><contrib contrib-type="author"><name><surname>Nakhla</surname><given-names>Shirley</given-names></name><xref ref-type="aff" rid="A1">1</xref></contrib><contrib contrib-type="author"><name><surname>Barter</surname><given-names>Philip J.</given-names></name><xref ref-type="aff" rid="A1">1</xref><xref ref-type="aff" rid="A4">4</xref></contrib><contrib contrib-type="author"><name><surname>Rye</surname><given-names>Kerry-Anne</given-names></name><xref ref-type="aff" rid="A1">1</xref><xref ref-type="aff" rid="A3">3</xref><xref ref-type="aff" rid="A4">4</xref></contrib><contrib contrib-type="author"><name><surname>Lambert</surname><given-names>Gilles</given-names></name><xref ref-type="aff" rid="A1">1</xref><xref ref-type="aff" rid="A5">5</xref></contrib></contrib-group><aff id="A1"><label>1</label>Lipid Research Group, The Heart Research Institute, Sydney, New South Wales, Australia</aff><aff id="A2"><label>2</label>National Heart Lung and Blood Institute, Pulmonary and Vascular Medicine Branch, Lipoprotein Metabolism Section, Bethesda, MD, USA</aff><aff id="A3"><label>3</label>Department of Medicine, University of Melbourne, Melbourne, Victoria, Australia</aff><aff id="A4"><label>4</label>Faculty of Medicine, University of Sydney, New South Wales, Australia</aff><aff id="A5"><label>5</label>Université de Nantes, Faculté de Médecine, Nantes, France</aff><author-notes><corresp id="CR1"><bold>Correspondence</bold>: A/Prof Gilles Lambert, The Heart Research Institute, 114, Pyrmont Bridge Road, Camperdown, NSW 2050, Australia, Tel: +61 2 8208 8900; Fax: +61 2 9565 5584, <email>lambertg@hri.org.au</email></corresp></author-notes><pub-date pub-type="nihms-submitted"><day>3</day><month>2</month><year>2010</year></pub-date><pub-date pub-type="epub"><day>3</day><month>12</month><year>2009</year></pub-date><pub-date pub-type="ppub"><month>2</month><year>2010</year></pub-date><pub-date pub-type="pmc-release"><day>1</day><month>2</month><year>2011</year></pub-date><volume>30</volume><issue>2</issue><fpage>246</fpage><lpage>252</lpage><abstract><sec id="S1"><title>Objectives</title><p id="P1">The apolipoprotein (apo) A-I mimetic peptide 5A is highly specific for ABCA1-transporter mediated cholesterol efflux. We investigated whether the 5A peptide shares other beneficial features of apoA-I, such as protection against inflammation and oxidation.</p></sec><sec sec-type="methods" id="S2"><title>Methods</title><p id="P2">New-Zealand White rabbits received an infusion of apoA-I, reconstituted HDL containing apoA-I ((A-I)rHDL) or the 5A peptide complexed with phospholipids (PLPC), prior to inserting a collar around the carotid artery. Human coronary artery endothelial cells (HCAECs) were incubated with (A-I)rHDL or 5A/PLPC prior to TNFa stimulation.</p></sec><sec id="S3"><title>Results</title><p id="P3">ApoA-I, (A-I)rHDL and 5A/PLPC reduced the collar mediated increase in (i) endothelial expression of cell adhesion molecules VCAM-1 and ICAM-1, (ii) O<sub>2</sub><sup>−</sup> production as well as the expression of the Nox4 catalytic subunits of the NADPH oxidase, and (iii) infiltration of circulating neutrophils into the carotid intima-media. In HCAECs, both 5A/PLPC and (A-I)rHDL inhibited TNFa induced ICAM-1 and VCAM-1 expression as well as the NF-κB signalling cascade and O<sub>2</sub><sup>−</sup> production. The effects of the 5A/PLPC complex were no longer apparent in HCAECs knocked down for ABCA1.</p></sec><sec id="S4"><title>Conclusion</title><p id="P4">Like apoA-I, the 5A peptide inhibits acute inflammation and oxidative stress in rabbit carotids and HCAECs. In vitro, the 5A peptide exerts these beneficial effects through interaction with ABCA1.</p></sec></abstract><kwd-group><kwd>HDL</kwd><kwd>apoA-I</kwd><kwd>mimetic peptide</kwd><kwd>inflammation</kwd><kwd>oxidation</kwd></kwd-group><contract-num rid="CL1">ZIA CL010303-09
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