Immunochemical characterization of purified human oxidized low-density lipoprotein antibodies

Copyright 2000 Academic Press.

Bibliographische Detailangaben
Veröffentlicht in:Clinical immunology (Orlando, Fla.). - 1999. - 95(2000), 2 vom: 01. Mai, Seite 135-44
1. Verfasser: Virella, G (VerfasserIn)
Weitere Verfasser: Koskinen, S, Krings, G, Onorato, J M, Thorpe, S R, Lopes-Virella, M
Format: Aufsatz
Sprache:English
Veröffentlicht: 2000
Zugriff auf das übergeordnete Werk:Clinical immunology (Orlando, Fla.)
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Antibodies Cardiolipins Epitopes Immunoglobulin Isotypes Lipoproteins, LDL oxidized low density lipoprotein mehr... Malondialdehyde 4Y8F71G49Q
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100 1 |a Virella, G  |e verfasserin  |4 aut 
245 1 0 |a Immunochemical characterization of purified human oxidized low-density lipoprotein antibodies 
264 1 |c 2000 
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500 |a Date Revised 21.11.2013 
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520 |a The goal of this study was to characterize the isotypes and reactivity of human autoantibodies to copper oxidized LDL (oxLDL). Forty-six purified oxLDL antibodies contained immunoglobulins of the three major isotypes, with a predominance of IgG, subclasses 1 and 3. These IgG isotypes are known to interact with FcRgammaI and to activate the complement system and thus are potentially able to activate macrophages and cause foam cell formation. The same purified antibodies were tested for cross-reactivity with malondialdehyde (MDA)-, glycated (Glyc)-, and native (n)LDL and cardiolipin. Absorption with oxLDL resulted in a decrease of reactivity of 77.2 +/- 4.7%. Absorption with MDA-LDL resulted in a wider range of reduction of reactivity values, ranging from 50 to 87%, possibly reflecting differences in the degree of MDA modification. Absorption with Glyc- and nLDL caused a minor decrease in the reactivity of antibodies to oxLDL (5.9 +/- 7.1 and 6.8 +/- 6. 4%, respectively), comparable to the reduction of reactivity (2.1 +/- 4.0%) measured after absorption with transferrin, an irrelevant protein used as a negative control. These results suggest that oxLDL antibodies recognize primarily MDA epitopes. To determine whether purified oxLDL antibodies also recognize other epitopes known to be generated during copper oxidation of LDL, such as 4-hydroxynonenal (HNE)- and N(epsilon)(carboxymethyl)-lysine (CML), two additional sets of experiments were carried out. First, we monitored the formation of CML-, MDA-lysine, and HNE-lysine at different times during copper oxidation of two LDL pools. Both pools showed simultaneous increases in protein modification, as indicated by increasing fluorescence emission at 430 nm, and in immunoreactivity with oxLDL antibodies, coinciding closely with MDA modification of lysine groups. Second, we assessed whether the reactivity of oxLDL antibodies could be blocked by absorption with CML- or HNE-LDL. HNE-LDL did not react with isolated oxLDL antibodies. Highly modified CML-LDL (>90% of lysine residues modified) reduced the reactivity of oxLDL antibodies, but only by 25.5%. Finally, we investigated the possible cross-reactivity of oxLDL antibodies with cardiolipin. Seventeen purified oxLDL antibodies were used in this study, which showed that absorption with oxLDL or nLDL did not affect their reactivity with immobilized cardiolipin 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a Research Support, U.S. Gov't, Non-P.H.S. 
650 4 |a Research Support, U.S. Gov't, P.H.S. 
650 7 |a Antibodies  |2 NLM 
650 7 |a Cardiolipins  |2 NLM 
650 7 |a Epitopes  |2 NLM 
650 7 |a Immunoglobulin Isotypes  |2 NLM 
650 7 |a Lipoproteins, LDL  |2 NLM 
650 7 |a oxidized low density lipoprotein  |2 NLM 
650 7 |a Malondialdehyde  |2 NLM 
650 7 |a 4Y8F71G49Q  |2 NLM 
700 1 |a Koskinen, S  |e verfasserin  |4 aut 
700 1 |a Krings, G  |e verfasserin  |4 aut 
700 1 |a Onorato, J M  |e verfasserin  |4 aut 
700 1 |a Thorpe, S R  |e verfasserin  |4 aut 
700 1 |a Lopes-Virella, M  |e verfasserin  |4 aut 
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