Effects of deferrioxamine on iron-catalyzed lipid peroxidation.

Effects of deferrioxamine on iron-catalyzed lipid peroxidation.
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去铁敏对铁催化脂质过氧化的影响。

DOI:
10.1016/0003-9861(92)90513-v
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发表时间:
1992
影响因子:
3.9
通讯作者:
Aust,SD
Aust,SD
中科院分区:
生物学3区
文献类型:
--
作者:
Miller,DM;Spear,NH;Aust,SD

文献摘要

被引文献

相似文献

研究了甲磺酸去铁胺B与铁结合的动力学及其对铁催化的脂质过氧化的影响。去铁胺对Fe(III)的相对结合率为:ADP>AMP>柠檬酸>组氨酸>EDTA。除ADP:Fe(III)外,除ADP:Fe(III)外,在Fe(III)中加入5倍摩尔量的去铁胺并不能完全结合(10分钟内)所测试的任何Fe(III)络合物。去铁胺与Fe(III)的结合速率在低pH和竞争螯合剂浓度与铁的比例较高时较大。去铁胺与Fe(III)的结合相对缓慢,也影响了脂质过氧化,这是一个铁依赖的过程。在依赖抗坏血酸和ADP:Fe(III)的脂质过氧化体系中加入去铁胺,可抑制或刺激丙二醛的形成(即脂质过氧化),这取决于去铁胺与铁的比例。与Fe(III)相反,上述螯合剂中的去铁胺与Fe(II)的结合速度较快且完全(在1min内),并导致Fe(II)氧化为Fe(III)。加入去铁胺可刺激依赖于Fe(II)自氧化的脂质过氧化。过氧化氢酶的加入抑制了该体系中丙二醛的生成,用过氧化氢代替去铁胺,可获得类似程度的脂质过氧化。综上所述,这些结果表明去铁胺与Fe(III)结合的动力学是一个缓慢的、可变的过程,而Fe(II)结合的速度要快得多。去铁胺与两种价态的铁的结合可能会对铁催化的过程产生不同的影响,如通过与Fe(III)的缓慢结合或Fe(II)与伴随的Fe(II)氧化的快速结合而引起的脂质过氧化。
The kinetics of iron binding by deferrioxamine B mesylate and the ramifications of this process upon ironcatalyzed lipid peroxidation were assessed. The relative rates of Fe(III) binding by deferrioxamine varied for the chelators tested as follows: ADP > AMP > citrate > histidine > EDTA. The addition of a fivefold molar excess of deferrioxamine to that of Fe(III) did not result in complete binding (within 10 min) for any of the Fe(III) chelates tested except ADP:Fe(III). The rates of Fe(III) binding by deferrioxamine were greater at lower pH and when the competing chelator concentration was high in relationship to iron. The relatively slow binding of Fe(III) by deferrioxamine also affected lipid peroxidation, an iron-dependent process. The addition of deferrioxamine to an ascorbate- and ADP:Fe(III)-dependent lipid peroxidation system resulted in a time-dependent inhibitionorstimulation of malondialdehyde formation (i.e., lipid peroxidation), depending on the ratio of deferrioxamine to iron. Converse to Fe(III), the rates of Fe(II) binding by deferrioxamine from the chelators tested above were rapid and complete (within 1 min), and resulted in the oxidation of Fe(II) to Fe(III). Lipid peroxidation dependent on Fe(II) autoxidation was stimulated by the addition of deferrioxamine. Malondialdehyde formation in this system was inhibited by the addition of catalase, and a similar extent of lipid peroxidation was achieved by substituting hydrogen peroxide for deferrioxamine. Collectively, these results suggest that the kinetics of Fe(III) binding by deferrioxamine is a slow, variable process, whereas Fe(II) binding is considerably faster. The binding of either valence of iron by deferrioxamine may result in variable effects on iron-catalyzed processes, such as lipid peroxidation, either via slow binding of Fe(III) or the rapid binding of Fe(II) with concomitant Fe(II) oxidation.