Oxidative modification of low-density lipoprotein: lipid peroxidation by myeloperoxidase in the presence of nitrite
Gespeichert in:
Verfasser / Beitragende:
[Tilo Kraemer, Inthanongsack Prakosay, Rahul A. Date, Helmut Sies, Tankred Schewe]
Ort, Verlag, Jahr:
2004
Enthalten in:
Biological Chemistry, 385/9(2004-09-01), 809-818
Format:
Artikel (online)
Online Zugang:
| LEADER | caa a22 4500 | ||
|---|---|---|---|
| 001 | 37888400X | ||
| 003 | CHVBK | ||
| 005 | 20180305123438.0 | ||
| 007 | cr unu---uuuuu | ||
| 008 | 161128e20040901xx s 000 0 eng | ||
| 024 | 7 | 0 | |a 10.1515/BC.2004.106 |2 doi |
| 035 | |a (NATIONALLICENCE)gruyter-10.1515/BC.2004.106 | ||
| 245 | 0 | 0 | |a Oxidative modification of low-density lipoprotein: lipid peroxidation by myeloperoxidase in the presence of nitrite |h [Elektronische Daten] |c [Tilo Kraemer, Inthanongsack Prakosay, Rahul A. Date, Helmut Sies, Tankred Schewe] |
| 520 | 3 | |a Oxidative modification of low-density lipoprotein (LDL) is a pivotal process in early atherogenesis and can be brought about by myeloperoxidase (MPO), which is capable of reacting with nitrite, a NO metabolite. We studied MPO-mediated formation of conjugated dienes in isolated human LDL in dependence on the concentrations of nitrite and chloride. This reaction was strongly stimulated by low concentrations (5-50 µM) of nitrite which corresponds to the reported concentration in the arterial vessel wall. Under these conditions no protein tyrosine nitration occurred; this reaction required much higher nitrite concentrations (100 µM—1 mM). Chloride neither supported lipid peroxidation alone nor was its presence mandatory for the effect of nitrite. We propose a prominent role of lipid peroxidation for the proatherogenic action of the MPO/nitrite system, whereas peroxynitrite may be competent for protein tyrosine nitration of LDL. Monomeric and oligomeric flavan-3-ols present in cocoa products effectively counteracted, at micromolar concentrations, the MPO/nitrite-mediated lipid peroxidation of LDL. Flavan-3-ols also suppressed protein tyrosine nitration induced by MPO/nitrite or peroxynitrite as well as Cu2+-mediated lipid peroxidation of LDL. This multi-site protection by (-)-epicatechin or other flavan-3-ols against proatherogenic modification of LDL may contribute to the purported beneficial effects of dietary flavan-3-ols for the cardiovascular system. | |
| 540 | |a © Walter de Gruyter | ||
| 690 | 7 | |a Biochemistry |2 nationallicence | |
| 690 | 7 | |a Molecular biology |2 nationallicence | |
| 690 | 7 | |a Cellular biology |2 nationallicence | |
| 690 | 7 | |a antioxidant |2 nationallicence | |
| 690 | 7 | |a atherosclerosis |2 nationallicence | |
| 690 | 7 | |a cocoa |2 nationallicence | |
| 690 | 7 | |a epicatechin |2 nationallicence | |
| 690 | 7 | |a flavonoids |2 nationallicence | |
| 690 | 7 | |a LDL oxidation |2 nationallicence | |
| 690 | 7 | |a procyanidins |2 nationallicence | |
| 700 | 1 | |a Kraemer |D Tilo |u Institut für Biochemie und Molekularbiologie I, Heinrich-Heine-Universität Düsseldorf, P.O. Box 10 10 07, D-40001 Düsseldorf, Germany |4 aut | |
| 700 | 1 | |a Prakosay |D Inthanongsack |u Institut für Biochemie und Molekularbiologie I, Heinrich-Heine-Universität Düsseldorf, P.O. Box 10 10 07, D-40001 Düsseldorf, Germany |4 aut | |
| 700 | 1 | |a Date |D Rahul A. |u Institut für Biochemie und Molekularbiologie I, Heinrich-Heine-Universität Düsseldorf, P.O. Box 10 10 07, D-40001 Düsseldorf, Germany |4 aut | |
| 700 | 1 | |a Sies |D Helmut |u Institut für Biochemie und Molekularbiologie I, Heinrich-Heine-Universität Düsseldorf, P.O. Box 10 10 07, D-40001 Düsseldorf, Germany |4 aut | |
| 700 | 1 | |a Schewe |D Tankred |u Institut für Biochemie und Molekularbiologie I, Heinrich-Heine-Universität Düsseldorf, P.O. Box 10 10 07, D-40001 Düsseldorf, Germany |4 aut | |
| 773 | 0 | |t Biological Chemistry |d Walter de Gruyter |g 385/9(2004-09-01), 809-818 |x 1431-6730 |q 385:9<809 |1 2004 |2 385 |o bchm | |
| 856 | 4 | 0 | |u https://doi.org/10.1515/BC.2004.106 |q text/html |z Onlinezugriff via DOI |
| 908 | |D 1 |a research article |2 jats | ||
| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1515/BC.2004.106 |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Kraemer |D Tilo |u Institut für Biochemie und Molekularbiologie I, Heinrich-Heine-Universität Düsseldorf, P.O. Box 10 10 07, D-40001 Düsseldorf, Germany |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Prakosay |D Inthanongsack |u Institut für Biochemie und Molekularbiologie I, Heinrich-Heine-Universität Düsseldorf, P.O. Box 10 10 07, D-40001 Düsseldorf, Germany |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Date |D Rahul A. |u Institut für Biochemie und Molekularbiologie I, Heinrich-Heine-Universität Düsseldorf, P.O. Box 10 10 07, D-40001 Düsseldorf, Germany |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Sies |D Helmut |u Institut für Biochemie und Molekularbiologie I, Heinrich-Heine-Universität Düsseldorf, P.O. Box 10 10 07, D-40001 Düsseldorf, Germany |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Schewe |D Tankred |u Institut für Biochemie und Molekularbiologie I, Heinrich-Heine-Universität Düsseldorf, P.O. Box 10 10 07, D-40001 Düsseldorf, Germany |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t Biological Chemistry |d Walter de Gruyter |g 385/9(2004-09-01), 809-818 |x 1431-6730 |q 385:9<809 |1 2004 |2 385 |o bchm | ||
| 900 | 7 | |b CC0 |u http://creativecommons.org/publicdomain/zero/1.0 |2 nationallicence | |
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 949 | |B NATIONALLICENCE |F NATIONALLICENCE |b NL-gruyter | ||