Serveur d'exploration sur les relations entre la France et l'Australie

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Non-Enzymatic Glycation Impairs the Anti-Inflammatory Properties of Apolipoprotein A-I

Identifieur interne : 001350 ( Pmc/Curation ); précédent : 001349; suivant : 001351

Non-Enzymatic Glycation Impairs the Anti-Inflammatory Properties of Apolipoprotein A-I

Auteurs : Estelle Nobécourt ; Fatiha Tabet ; Gilles Lambert [France] ; Rajesh Puranik [Australie] ; Shisan Bao [Australie] ; Ling Yan ; Michael J. Davies [Australie] ; Bronwyn E. Brown ; Alicia J. Jenkins [Australie] ; Gregory J. Dusting [Australie] ; David J. Bonnet ; Linda K. Curtiss ; Philip J. Barter [Australie] ; Kerry-Anne Rye [Australie]

Source :

RBID : PMC:3038672

Abstract

Objective

To investigate the effects of non-enzymatic glycation on the anti-inflammatory properties of apolipoprotein (apo) A-I.

Methods and Results

Rabbits were infused with saline, lipid-free apoA-I from normal subjects (apoA-IN), lipid-free apoA-I non-enzymatically glycated by incubation with methylglyoxal (apoA-IGlyc in vitro), non-enzymatically glycated lipid-free apoA-I from subjects with diabetes (apoA-IGlyc in vivo), discoidal reconstituted HDL containing phosphatidylcholine and apoA-IN, (A-IN)rHDL, or apoA-IGlyc in vitro, (A-IGlyc in vitro)rHDL. At 24 h post-infusion, acute vascular inflammation was induced by inserting a non-occlusive, periarterial carotid collar. The animals were sacrificed 24 h post-collar insertion. The collars caused intima/media neutrophil infiltration and increased endothelial expression of vascular cell adhesion molecule-1 (VCAM-1) and intercellular adhesion molecule-1 (ICAM-1). ApoA-IN infusion decreased neutrophil infiltration and VCAM-1 and ICAM-1 expression by 89, 90 and 66%, respectively. The apoA-IGlyc in vitro infusion decreased neutrophil infiltration by 53%, but did not reduce VCAM-1 or ICAM-1 expression. ApoA-IGlyc in vivo did not inhibit neutrophil infiltration or adhesion molecule expression. (A-IGlyc in vitro)rHDL also inhibited vascular inflammation less effectively than (A-IN)rHDL. The reduced anti-inflammatory properties of non-enzymatically glycated apoA-I were attributed to a reduced ability to inhibit nuclear factor-κB activation and reactive oxygen species formation.

Conclusion

Non-enzymatic glycation impairs the anti-inflammatory properties of apoA-I.


Url:
DOI: 10.1161/ATVBAHA.109.201715
PubMed: 20110571
PubMed Central: 3038672

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PMC:3038672

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Estelle Nobécourt
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Fatiha Tabet
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Gilles Lambert
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Rajesh Puranik
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Shisan Bao
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Ling Yan
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Michael J. Davies
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Bronwyn E. Brown
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David J. Bonnet
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Linda K. Curtiss
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Philip J. Barter
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Kerry-Anne Rye
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</affiliation>
<affiliation wicri:level="4">
<nlm:aff id="A3">Faculty of Medicine, University of Sydney, NSW, Australia, 2006</nlm:aff>
<orgName type="university">Université de Sydney</orgName>
<country>Australie</country>
<placeName>
<settlement type="city">Sydney</settlement>
<region type="état">Nouvelle-Galles du Sud</region>
</placeName>
</affiliation>
<affiliation wicri:level="4">
<nlm:aff id="A6">Department of Medicine, University of Melbourne, Victoria, Australia, 3010</nlm:aff>
<orgName type="university">Université de Melbourne</orgName>
<country>Australie</country>
<placeName>
<settlement type="city">Melbourne</settlement>
<region type="état">Victoria (État)</region>
</placeName>
</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="2010">2010</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc>
<textClass></textClass>
</profileDesc>
</teiHeader>
<front>
<div type="abstract" xml:lang="en">
<sec id="S1">
<title>Objective</title>
<p id="P2">To investigate the effects of non-enzymatic glycation on the anti-inflammatory properties of apolipoprotein (apo) A-I.</p>
</sec>
<sec sec-type="methods" id="S2">
<title>Methods and Results</title>
<p id="P3">Rabbits were infused with saline, lipid-free apoA-I from normal subjects (apoA-I
<sub>
<italic>N</italic>
</sub>
), lipid-free apoA-I non-enzymatically glycated by incubation with methylglyoxal (apoA-I
<italic>
<sub>Glyc in vitro</sub>
</italic>
), non-enzymatically glycated lipid-free apoA-I from subjects with diabetes (apoA-I
<sub>
<italic>Glyc in vivo</italic>
</sub>
), discoidal reconstituted HDL containing phosphatidylcholine and apoA-I
<italic>
<sub>N</sub>
</italic>
, (A-I
<sub>
<italic>N</italic>
</sub>
)rHDL, or apoA-I
<sub>
<italic>Glyc in vitro</italic>
</sub>
, (A-I
<sub>
<italic>Glyc in vitro</italic>
</sub>
)rHDL. At 24 h post-infusion, acute vascular inflammation was induced by inserting a non-occlusive, periarterial carotid collar. The animals were sacrificed 24 h post-collar insertion. The collars caused intima/media neutrophil infiltration and increased endothelial expression of vascular cell adhesion molecule-1 (VCAM-1) and intercellular adhesion molecule-1 (ICAM-1). ApoA-I
<sub>
<italic>N</italic>
</sub>
infusion decreased neutrophil infiltration and VCAM-1 and ICAM-1 expression by 89, 90 and 66%, respectively. The apoA-I
<sub>
<italic>Glyc in vitro</italic>
</sub>
infusion decreased neutrophil infiltration by 53%, but did not reduce VCAM-1 or ICAM-1 expression. ApoA-I
<sub>
<italic>Glyc in vivo</italic>
</sub>
did not inhibit neutrophil infiltration or adhesion molecule expression. (A-I
<sub>
<italic>Glyc in vitro</italic>
</sub>
)rHDL also inhibited vascular inflammation less effectively than (A-I
<sub>
<italic>N</italic>
</sub>
)rHDL. The reduced anti-inflammatory properties of non-enzymatically glycated apoA-I were attributed to a reduced ability to inhibit nuclear factor-κB activation and reactive oxygen species formation.</p>
</sec>
<sec id="S3">
<title>Conclusion</title>
<p id="P4">Non-enzymatic glycation impairs the anti-inflammatory properties of apoA-I.</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">20110571</article-id>
<article-id pub-id-type="pmc">3038672</article-id>
<article-id pub-id-type="doi">10.1161/ATVBAHA.109.201715</article-id>
<article-id pub-id-type="manuscript">NIHMS267616</article-id>
<article-categories>
<subj-group subj-group-type="heading">
<subject>Article</subject>
</subj-group>
</article-categories>
<title-group>
<article-title>Non-Enzymatic Glycation Impairs the Anti-Inflammatory Properties of Apolipoprotein A-I</article-title>
</title-group>
<contrib-group>
<contrib contrib-type="author">
<name>
<surname>Nobécourt</surname>
<given-names>Estelle</given-names>
</name>
<xref ref-type="aff" rid="A1">1</xref>
<xref ref-type="author-notes" rid="FN1">*</xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Tabet</surname>
<given-names>Fatiha</given-names>
</name>
<xref ref-type="aff" rid="A1">1</xref>
<xref ref-type="author-notes" rid="FN1">*</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="A2">2</xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Puranik</surname>
<given-names>Rajesh</given-names>
</name>
<xref ref-type="aff" rid="A1">1</xref>
<xref ref-type="aff" rid="A3">3</xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Bao</surname>
<given-names>Shisan</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>Yan</surname>
<given-names>Ling</given-names>
</name>
<xref ref-type="aff" rid="A1">1</xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Davies</surname>
<given-names>Michael J.</given-names>
</name>
<xref ref-type="aff" rid="A3">3</xref>
<xref ref-type="aff" rid="A5">5</xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Brown</surname>
<given-names>Bronwyn E.</given-names>
</name>
<xref ref-type="aff" rid="A5">5</xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Jenkins</surname>
<given-names>Alicia J</given-names>
</name>
<xref ref-type="aff" rid="A6">6</xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Dusting</surname>
<given-names>Gregory J.</given-names>
</name>
<xref ref-type="aff" rid="A7">7</xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Bonnet</surname>
<given-names>David J.</given-names>
</name>
<xref ref-type="aff" rid="A8">8</xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Curtiss</surname>
<given-names>Linda K.</given-names>
</name>
<xref ref-type="aff" rid="A8">8</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="A3">3</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="A6">6</xref>
</contrib>
</contrib-group>
<aff id="A1">
<label>1</label>
Lipid Research Group, The Heart Research Institute, Sydney, NSW, Australia, 2042</aff>
<aff id="A2">
<label>2</label>
Université de Nantes, Faculté de Médecine, Nantes, France, 44000</aff>
<aff id="A3">
<label>3</label>
Faculty of Medicine, University of Sydney, NSW, Australia, 2006</aff>
<aff id="A4">
<label>4</label>
Department of Pathology, University of Sydney, NSW, Australia, 2006</aff>
<aff id="A5">
<label>5</label>
Free Radical Group, The Heart Research Institute, Sydney, NSW, Australia, 2042</aff>
<aff id="A6">
<label>6</label>
Department of Medicine, University of Melbourne, Victoria, Australia, 3010</aff>
<aff id="A7">
<label>7</label>
O’Brien Institute and Department of Surgery, University of Melbourne, Victoria, Australia, 3010</aff>
<aff id="A8">
<label>8</label>
Department of Immunology, The Scripps Research Institute, La Jolla, CA, USA, 92037</aff>
<author-notes>
<corresp id="cor1">
<italic>Corresponding author:</italic>
Kerry-Anne Rye, Lipid Research Group, The Heart Research Institute, 7 Eliza St, Newtown, NSW, Australia, 2042. Tel: +61 2 8208 8900; Fax: +61 2 9565 5584.
<email>k.rye@hri.org.au</email>
or
<email>karye@ozemail.com.au</email>
</corresp>
<fn id="FN1" fn-type="equal">
<label>*</label>
<p id="P1">both authors contributed equally to the work</p>
</fn>
</author-notes>
<pub-date pub-type="nihms-submitted">
<day>4</day>
<month>2</month>
<year>2011</year>
</pub-date>
<pub-date pub-type="epub">
<day>28</day>
<month>1</month>
<year>2010</year>
</pub-date>
<pub-date pub-type="ppub">
<month>4</month>
<year>2010</year>
</pub-date>
<pub-date pub-type="pmc-release">
<day>1</day>
<month>4</month>
<year>2011</year>
</pub-date>
<volume>30</volume>
<issue>4</issue>
<fpage>766</fpage>
<lpage>772</lpage>
<abstract>
<sec id="S1">
<title>Objective</title>
<p id="P2">To investigate the effects of non-enzymatic glycation on the anti-inflammatory properties of apolipoprotein (apo) A-I.</p>
</sec>
<sec sec-type="methods" id="S2">
<title>Methods and Results</title>
<p id="P3">Rabbits were infused with saline, lipid-free apoA-I from normal subjects (apoA-I
<sub>
<italic>N</italic>
</sub>
), lipid-free apoA-I non-enzymatically glycated by incubation with methylglyoxal (apoA-I
<italic>
<sub>Glyc in vitro</sub>
</italic>
), non-enzymatically glycated lipid-free apoA-I from subjects with diabetes (apoA-I
<sub>
<italic>Glyc in vivo</italic>
</sub>
), discoidal reconstituted HDL containing phosphatidylcholine and apoA-I
<italic>
<sub>N</sub>
</italic>
, (A-I
<sub>
<italic>N</italic>
</sub>
)rHDL, or apoA-I
<sub>
<italic>Glyc in vitro</italic>
</sub>
, (A-I
<sub>
<italic>Glyc in vitro</italic>
</sub>
)rHDL. At 24 h post-infusion, acute vascular inflammation was induced by inserting a non-occlusive, periarterial carotid collar. The animals were sacrificed 24 h post-collar insertion. The collars caused intima/media neutrophil infiltration and increased endothelial expression of vascular cell adhesion molecule-1 (VCAM-1) and intercellular adhesion molecule-1 (ICAM-1). ApoA-I
<sub>
<italic>N</italic>
</sub>
infusion decreased neutrophil infiltration and VCAM-1 and ICAM-1 expression by 89, 90 and 66%, respectively. The apoA-I
<sub>
<italic>Glyc in vitro</italic>
</sub>
infusion decreased neutrophil infiltration by 53%, but did not reduce VCAM-1 or ICAM-1 expression. ApoA-I
<sub>
<italic>Glyc in vivo</italic>
</sub>
did not inhibit neutrophil infiltration or adhesion molecule expression. (A-I
<sub>
<italic>Glyc in vitro</italic>
</sub>
)rHDL also inhibited vascular inflammation less effectively than (A-I
<sub>
<italic>N</italic>
</sub>
)rHDL. The reduced anti-inflammatory properties of non-enzymatically glycated apoA-I were attributed to a reduced ability to inhibit nuclear factor-κB activation and reactive oxygen species formation.</p>
</sec>
<sec id="S3">
<title>Conclusion</title>
<p id="P4">Non-enzymatic glycation impairs the anti-inflammatory properties of apoA-I.</p>
</sec>
</abstract>
<kwd-group>
<kwd>apoA-I</kwd>
<kwd>inflammation</kwd>
<kwd>HDL</kwd>
<kwd>adhesion molecules</kwd>
<kwd>neutrophils</kwd>
<kwd>NF-κB</kwd>
<kwd>reactive oxygen species</kwd>
</kwd-group>
<contract-num rid="HL1">P01 HL088093-01A1 ||HL</contract-num>
<contract-sponsor id="HL1">National Heart, Lung, and Blood Institute : NHLBI</contract-sponsor>
</article-meta>
</front>
</pmc>
</record>

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