Advanced lipid peroxidation end products in oxidative damage to proteins. Potential role in diseases and therapeutic prospects for the inhibitors
Identifieur interne : 000028 ( Pmc/Curation ); précédent : 000027; suivant : 000029Advanced lipid peroxidation end products in oxidative damage to proteins. Potential role in diseases and therapeutic prospects for the inhibitors
Auteurs : A. Negre-Salvayre [France] ; C. Coatrieux [France] ; C. Ingueneau [France] ; R. Salvayre [France]Source :
- British Journal of Pharmacology [ 0007-1188 ] ; 2007.
Abstract
Reactive carbonyl compounds (RCCs) formed during lipid peroxidation and sugar glycoxidation, namely Advanced lipid peroxidation end products (ALEs) and Advanced Glycation end products (AGEs), accumulate with ageing and oxidative stress-related diseases, such as atherosclerosis, diabetes or neurodegenerative diseases. RCCs induce the ‘carbonyl stress' characterized by the formation of adducts and cross-links on proteins, which progressively leads to impaired protein function and damages in all tissues, and pathological consequences including cell dysfunction, inflammatory response and apoptosis. The prevention of carbonyl stress involves the use of free radical scavengers and antioxidants that prevent the generation of lipid peroxidation products, but are inefficient on pre-formed RCCs. Conversely, carbonyl scavengers prevent carbonyl stress by inhibiting the formation of protein cross-links. While a large variety of AGE inhibitors has been developed, only few carbonyl scavengers have been tested on ALE-mediated effects. This review summarizes the signalling properties of ALEs and ALE-precursors, their role in the pathogenesis of oxidative stress-associated diseases, and the different agents efficient in neutralizing ALEs effects
Url:
DOI: 10.1038/sj.bjp.0707395
PubMed: 17643134
PubMed Central: 2199390
Links toward previous steps (curation, corpus...)
- to stream Pmc, to step Corpus: Pour aller vers cette notice dans l'étape Curation :000028
Links to Exploration step
PMC:2199390Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Advanced lipid peroxidation end products in oxidative damage to proteins. Potential role in diseases and therapeutic prospects for the inhibitors</title><author><name sortKey="Negre Salvayre, A" sort="Negre Salvayre, A" uniqKey="Negre Salvayre A" first="A" last="Negre-Salvayre">A. Negre-Salvayre</name><affiliation wicri:level="1"><nlm:aff id="aff1"><institution>INSERM U858, IFR-31 and Biochemistry Department, CHU Rangueil, University Toulouse-3</institution> Toulouse,<country>France</country></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Coatrieux, C" sort="Coatrieux, C" uniqKey="Coatrieux C" first="C" last="Coatrieux">C. Coatrieux</name><affiliation wicri:level="1"><nlm:aff id="aff1"><institution>INSERM U858, IFR-31 and Biochemistry Department, CHU Rangueil, University Toulouse-3</institution> Toulouse,<country>France</country></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Ingueneau, C" sort="Ingueneau, C" uniqKey="Ingueneau C" first="C" last="Ingueneau">C. Ingueneau</name><affiliation wicri:level="1"><nlm:aff id="aff1"><institution>INSERM U858, IFR-31 and Biochemistry Department, CHU Rangueil, University Toulouse-3</institution> Toulouse,<country>France</country></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Salvayre, R" sort="Salvayre, R" uniqKey="Salvayre R" first="R" last="Salvayre">R. Salvayre</name><affiliation wicri:level="1"><nlm:aff id="aff1"><institution>INSERM U858, IFR-31 and Biochemistry Department, CHU Rangueil, University Toulouse-3</institution> Toulouse,<country>France</country></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">17643134</idno><idno type="pmc">2199390</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2199390</idno><idno type="RBID">PMC:2199390</idno><idno type="doi">10.1038/sj.bjp.0707395</idno><date when="2007">2007</date><idno type="wicri:Area/Pmc/Corpus">000028</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000028</idno><idno type="wicri:Area/Pmc/Curation">000028</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000028</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Advanced lipid peroxidation end products in oxidative damage to proteins. Potential role in diseases and therapeutic prospects for the inhibitors</title><author><name sortKey="Negre Salvayre, A" sort="Negre Salvayre, A" uniqKey="Negre Salvayre A" first="A" last="Negre-Salvayre">A. Negre-Salvayre</name><affiliation wicri:level="1"><nlm:aff id="aff1"><institution>INSERM U858, IFR-31 and Biochemistry Department, CHU Rangueil, University Toulouse-3</institution> Toulouse,<country>France</country></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Coatrieux, C" sort="Coatrieux, C" uniqKey="Coatrieux C" first="C" last="Coatrieux">C. Coatrieux</name><affiliation wicri:level="1"><nlm:aff id="aff1"><institution>INSERM U858, IFR-31 and Biochemistry Department, CHU Rangueil, University Toulouse-3</institution> Toulouse,<country>France</country></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Ingueneau, C" sort="Ingueneau, C" uniqKey="Ingueneau C" first="C" last="Ingueneau">C. Ingueneau</name><affiliation wicri:level="1"><nlm:aff id="aff1"><institution>INSERM U858, IFR-31 and Biochemistry Department, CHU Rangueil, University Toulouse-3</institution> Toulouse,<country>France</country></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Salvayre, R" sort="Salvayre, R" uniqKey="Salvayre R" first="R" last="Salvayre">R. Salvayre</name><affiliation wicri:level="1"><nlm:aff id="aff1"><institution>INSERM U858, IFR-31 and Biochemistry Department, CHU Rangueil, University Toulouse-3</institution> Toulouse,<country>France</country></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author></analytic><series><title level="j">British Journal of Pharmacology</title><idno type="ISSN">0007-1188</idno><idno type="eISSN">1476-5381</idno><imprint><date when="2007">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Reactive carbonyl compounds (RCCs) formed during lipid peroxidation and sugar glycoxidation, namely Advanced lipid peroxidation end products (ALEs) and Advanced Glycation end products (AGEs), accumulate with ageing and oxidative stress-related diseases, such as atherosclerosis, diabetes or neurodegenerative diseases. RCCs induce the ‘carbonyl stress' characterized by the formation of adducts and cross-links on proteins, which progressively leads to impaired protein function and damages in all tissues, and pathological consequences including cell dysfunction, inflammatory response and apoptosis. The prevention of carbonyl stress involves the use of free radical scavengers and antioxidants that prevent the generation of lipid peroxidation products, but are inefficient on pre-formed RCCs. Conversely, carbonyl scavengers prevent carbonyl stress by inhibiting the formation of protein cross-links. While a large variety of AGE inhibitors has been developed, only few carbonyl scavengers have been tested on ALE-mediated effects. This review summarizes the signalling properties of ALEs and ALE-precursors, their role in the pathogenesis of oxidative stress-associated diseases, and the different agents efficient in neutralizing ALEs effects <italic>in vitro</italic> and <italic>in vivo</italic>. The generation of drugs sharing both antioxidant and carbonyl scavenger properties represents a new therapeutic challenge in the treatment of carbonyl stress-associated diseases.</p></div></front></TEI><pmc article-type="review-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<pmc-comment> Original-type: rv</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Br J Pharmacol</journal-id><journal-title>British Journal of Pharmacology</journal-title><issn pub-type="ppub">0007-1188</issn><issn pub-type="epub">1476-5381</issn><publisher><publisher-name>Nature Publishing Group</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">17643134</article-id><article-id pub-id-type="pmc">2199390</article-id><article-id pub-id-type="pii">0707395</article-id><article-id pub-id-type="doi">10.1038/sj.bjp.0707395</article-id><article-categories><subj-group subj-group-type="heading"><subject>Reviews</subject><subj-group><subject>Review Article</subject></subj-group></subj-group></article-categories><title-group><article-title>Advanced lipid peroxidation end products in oxidative damage to proteins. Potential role in diseases and therapeutic prospects for the inhibitors</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Negre-Salvayre</surname><given-names>A</given-names></name><xref ref-type="aff" rid="aff1">1</xref><xref ref-type="corresp" rid="caf1">*</xref></contrib><contrib contrib-type="author"><name><surname>Coatrieux</surname><given-names>C</given-names></name><xref ref-type="aff" rid="aff1">1</xref></contrib><contrib contrib-type="author"><name><surname>Ingueneau</surname><given-names>C</given-names></name><xref ref-type="aff" rid="aff1">1</xref></contrib><contrib contrib-type="author"><name><surname>Salvayre</surname><given-names>R</given-names></name><xref ref-type="aff" rid="aff1">1</xref></contrib></contrib-group><aff id="aff1"><label>1</label><institution>INSERM U858, IFR-31 and Biochemistry Department, CHU Rangueil, University Toulouse-3</institution> Toulouse,<country>France</country></aff><author-notes><corresp id="caf1"><label>*</label>Author for correspondence: <email xlink:href="mailto:anesalv@toulouse.inserm.fr">anesalv@toulouse.inserm.fr</email></corresp></author-notes><pub-date pub-type="epub"><day>23</day><month>07</month><year>2007</year></pub-date><pub-date pub-type="collection"><day>07</day><month>01</month><year>2008</year></pub-date><pub-date pub-type="ppub"><month>1</month><year>2008</year></pub-date><volume>153</volume><issue>1</issue><fpage>6</fpage><lpage>20</lpage><history><date date-type="received"><day>29</day><month>03</month><year>2007</year></date><date date-type="rev-recd"><day>01</day><month>06</month><year>2007</year></date><date date-type="accepted"><day>11</day><month>06</month><year>2007</year></date></history><copyright-statement>Copyright 2008, Nature Publishing Group</copyright-statement><copyright-year>2008</copyright-year><permissions><copyright-holder>Nature Publishing Group</copyright-holder></permissions><abstract><p>Reactive carbonyl compounds (RCCs) formed during lipid peroxidation and sugar glycoxidation, namely Advanced lipid peroxidation end products (ALEs) and Advanced Glycation end products (AGEs), accumulate with ageing and oxidative stress-related diseases, such as atherosclerosis, diabetes or neurodegenerative diseases. RCCs induce the ‘carbonyl stress' characterized by the formation of adducts and cross-links on proteins, which progressively leads to impaired protein function and damages in all tissues, and pathological consequences including cell dysfunction, inflammatory response and apoptosis. The prevention of carbonyl stress involves the use of free radical scavengers and antioxidants that prevent the generation of lipid peroxidation products, but are inefficient on pre-formed RCCs. Conversely, carbonyl scavengers prevent carbonyl stress by inhibiting the formation of protein cross-links. While a large variety of AGE inhibitors has been developed, only few carbonyl scavengers have been tested on ALE-mediated effects. This review summarizes the signalling properties of ALEs and ALE-precursors, their role in the pathogenesis of oxidative stress-associated diseases, and the different agents efficient in neutralizing ALEs effects <italic>in vitro</italic> and <italic>in vivo</italic>. The generation of drugs sharing both antioxidant and carbonyl scavenger properties represents a new therapeutic challenge in the treatment of carbonyl stress-associated diseases.</p></abstract><kwd-group><kwd>ALE</kwd><kwd>atherosclerosis</kwd><kwd>cancer</kwd><kwd>carbonyl scavenger</kwd><kwd>carbonyl stress</kwd><kwd>diabetes</kwd><kwd>4-hydroxynonenal</kwd><kwd>inflammation</kwd><kwd>lipid peroxidation</kwd><kwd>neurodegenerative diseases</kwd></kwd-group></article-meta></front><floats-wrap><fig id="fig1"><label>Figure 1</label><caption><p>Chemical formulae of some aldehydic compounds derived from lipid peroxidation, including saturated aldehydes, unsaturated aldehydes, 4-hydroxy-2-alkenals and dicarbonyls. These reactive carbonyl compounds are also advanced lipid peroxidation end product precursors.</p></caption><graphic mime-subtype="eps" xlink:href="0707395f1"></graphic></fig><fig id="fig2"><label>Figure 2</label><caption><p>Schematic steps of lipid peroxidation leading to the formation of secondary products and ALEs (<xref ref-type="other" rid="bib154">Uchida, 2000</xref>; <xref ref-type="other" rid="bib1">Aldini <italic>et al</italic>., 2006</xref>; <xref ref-type="other" rid="bib132">Shibamoto, 2006</xref>). RCCs are able to react with proteins and other biological molecules, thereby forming ALEs. Stable products (such as alkanes) do not react with proteins. ALEs, advanced lipid peroxidation end products; RCCs, reactive carbonyl compounds.</p></caption><graphic mime-subtype="eps" xlink:href="0707395f2"></graphic></fig><fig id="fig3"><label>Figure 3</label><caption><p>Metabolic pathways leading to the formation of methylglyoxal (MGO) and of MGO adducts (<xref ref-type="other" rid="bib117">Ramasamy <italic>et al</italic>., 2006</xref>). In addition to lipid peroxidation and glycoxidation, MGO can be formed as a by-product of glucose, glycerolipids and amino acids.</p></caption><graphic mime-subtype="eps" xlink:href="0707395f3"></graphic></fig><fig id="fig4"><label>Figure 4</label><caption><p>Schematic reactions of 4-HNE with proteins leading to the formation of 4-HNE-protein adducts. (1) Schiff base formation on primary amine (for example, lysin) leading to more complex compounds, such as pyrrole-Lys adducts and fluorescent cross-links. (2) Michael addition of 4-HNE on amino groups (Lys and His) or thiols (Cys or GSH), followed by cyclization and hemi-acetal or hemi-thioacetal formation (<xref ref-type="other" rid="bib126">Sayre <italic>et al</italic>., 1993</xref>; <xref ref-type="other" rid="bib154">Uchida 2000</xref>; <xref ref-type="other" rid="bib26">Carini <italic>et al</italic>., 2004</xref>). 4-HNE, 4-hydroxynonenal; Lys, lysine; His, histidine; Cys, cysteine; GSH, glutathione.</p></caption><graphic mime-subtype="eps" xlink:href="0707395f4"></graphic></fig><fig id="fig5"><label>Figure 5</label><caption><p>Modification of LDL and formation of foam cells. ROS induce the oxidation of PUFA in LDLs. Lipid peroxidation leads to the formation of aldehydic compounds such as 4-HNE and MDA. These RCCs are able to react with lysin residues of apoB leading to modified apoB. The affinity of modified LDL for the apoB/E receptor decreases when apoB modification increases. Modified oxidized LDL are deviated towards the scavenger receptor pathway of macrophages, which are loaded with cholesterol esters and are transformed into foam cells, the signature of the initial step of atherosclerosis (<xref ref-type="other" rid="bib20">Brown and Goldstein, 1983</xref>; <xref ref-type="other" rid="bib141">Steinberg <italic>et al</italic>., 1989</xref>, <xref ref-type="other" rid="bib140">1997</xref>; <xref ref-type="other" rid="bib48">Esterbauer <italic>et al</italic>., 1990</xref>, <xref ref-type="other" rid="bib49">1991</xref>). LDL, low-density lipoprotein, ROS, reactive oxygen species; PUFAs, polyunsaturated fatty acids; 4-HNE, 4-hydroxynonenal; MDA, malondialdehyde; RCCs, reactive carbonyl compounds.</p></caption><graphic mime-subtype="eps" xlink:href="0707395f5"></graphic></fig></floats-wrap></pmc></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Sante/explor/ParkinsonFranceV1/Data/Pmc/Curation
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000028 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Pmc/Curation/biblio.hfd -nk 000028 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Wicri/Sante
|area= ParkinsonFranceV1
|flux= Pmc
|étape= Curation
|type= RBID
|clé= PMC:2199390
|texte= Advanced lipid peroxidation end products in oxidative damage to proteins. Potential role in diseases and therapeutic prospects for the inhibitors
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Pmc/Curation/RBID.i -Sk "pubmed:17643134" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Pmc/Curation/biblio.hfd \
| NlmPubMed2Wicri -a ParkinsonFranceV1
| This area was generated with Dilib version V0.6.29. |  |