Enzymatic repair of oxidative damage to human apolipoprotein A‐I

Sigalov, Alexander B.; Stern, Lawrence J.

doi:10.1016/s0014-5793(98)00908-9

Cited by 46 publications

(41 citation statements)

References 19 publications

(18 reference statements)

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“…This observation further supports the anti-oxidative properties of Met in proteins and peptides, as discussed by others [12,38,39]. Recently it has been shown that oxidized Met""# and Met"%) in lipid-free as well as in lipid-associated apo A-I can be reduced to Met in itro by peptide Met(SO) reductase [40], suggesting that the enzymic reduction of oxidized apo A-I could restore its biological activity.…”

Section: Discussionsupporting

confidence: 86%

Reagent or myeloperoxidase-generated hypochlorite affects discrete regions in lipid-free and lipid-associated human apolipoprotein A-I

Bergt

OETTL²,

Keller

et al. 2000

Biochem. J.

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Section: Discussionsupporting

confidence: 86%

Reagent or myeloperoxidase-generated hypochlorite affects discrete regions in lipid-free and lipid-associated human apolipoprotein A-I

Bergt

OETTL²,

Keller

et al. 2000

Biochem. J.

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“…Several protein substrates for PMSR have been investigated in animal and microbial systems. These include the ␣-1-proteinase inhibitor (Abrams et al, 1981), calmodulin (Sun et al, 1999), apolipoprotein A1 (Sigalov and Stern, 1998), and ␣/␤-spore proteins (Hayes et al, 1998). We found that both plant PMSR isoforms were able to repair the bovine oxidized ␣-1-proteinase inhibitor protein at rates comparable to those reported in the literature for non-plant PMSRs.…”

Section: Discussionmentioning

confidence: 99%

Differential Regulation of Plastidial and Cytosolic Isoforms of Peptide Methionine Sulfoxide Reductase in Arabidopsis

et al. 2000

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We report the characterization of two members of a gene family from Arabidopsis that encode, respectively, cytosolic (cPMSR) and plastid-targeted (pPMSR) isoforms of the oxidative-stress-repair enzyme peptide methionine sulfoxide reductase. Overexpression of these proteins in Escherichia coli confirmed that each had PMSR enzyme activity with a synthetic substrate,N-acetyl-[3H]-methionine sulfoxide, or a biological substrate, α-1 proteinase inhibitor. The pPMSR was imported into intact chloroplasts in vitro with concomitant cleavage of its approximately 5-kD N-terminal signal peptide. The two PMSR isoforms exhibited divergent pH optima, tissue localization, and responses to developmental and environmental effects. Analysis of the Arabidopsis database indicated that there are probably at least twop-pmsr-like genes and three c-pmsr-like genes in the Arabidopsis genome. Expression of thep-pmsr genes and their protein products was restricted to photosynthetic tissues and was strongly induced following illumination of etiolated seedlings. In contrast, thec-pmsr genes were expressed at moderate levels in all tissues and were only weakly affected by light. Exposure to a variety of biotic and abiotic stresses showed relatively little effect onpmsr gene expression, with the exception of leaves subjected to a long-term exposure to the cauliflower mosaic virus. These leaves showed a strong induction of the c-pmsrgene after 2 to 3 weeks of chronic pathogen infection. These data suggest novel roles for PMSR in photosynthetic tissues and in pathogen defense responses in plants.

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“…In vitro, the above reaction is slow, although it is accelerated by unknown factor(s) in liver (154), and a slow reduction could still be important under circumstances such as in an atherosclerotic vessel where the average residence time of lipoproteins is long. Peptide methionine sulfoxide reductase acts on methionine sulfoxides in lipid-free and lipid-associated apolipoprotein A-I, suggestive of enzymatic repair of the oxidized protein (850), although it remains unclear whether the cellular sulfoxide reductase can act on extracellular apolipoprotein(s).…”

Section: Throughout the Cellmentioning

confidence: 99%

Role of Oxidative Modifications in Atherosclerosis

Stocker¹,

Keaney²

2004

Physiological Reviews

2,244

1,756

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This review focuses on the role of oxidative processes in atherosclerosis and its resultant cardiovascular events. There is now a consensus that atherosclerosis represents a state of heightened oxidative stress characterized by lipid and protein oxidation in the vascular wall. The oxidative modification hypothesis of atherosclerosis predicts that low-density lipoprotein (LDL) oxidation is an early event in atherosclerosis and that oxidized LDL contributes to atherogenesis. In support of this hypothesis, oxidized LDL can support foam cell formation in vitro, the lipid in human lesions is substantially oxidized, there is evidence for the presence of oxidized LDL in vivo, oxidized LDL has a number of potentially proatherogenic activities, and several structurally unrelated antioxidants inhibit atherosclerosis in animals. An emerging consensus also underscores the importance in vascular disease of oxidative events in addition to LDL oxidation. These include the production of reactive oxygen and nitrogen species by vascular cells, as well as oxidative modifications contributing to important clinical manifestations of coronary artery disease such as endothelial dysfunction and plaque disruption. Despite these abundant data however, fundamental problems remain with implicating oxidative modification as a (requisite) pathophysiologically important cause for atherosclerosis. These include the poor performance of antioxidant strategies in limiting either atherosclerosis or cardiovascular events from atherosclerosis, and observations in animals that suggest dissociation between atherosclerosis and lipoprotein oxidation. Indeed, it remains to be established that oxidative events are a cause rather than an injurious response to atherogenesis. In this context, inflammation needs to be considered as a primary process of atherosclerosis, and oxidative stress as a secondary event. To address this issue, we have proposed an “oxidative response to inflammation” model as a means of reconciling the response-to-injury and oxidative modification hypotheses of atherosclerosis.

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Enzymatic repair of oxidative damage to human apolipoprotein A‐I

Cited by 46 publications

References 19 publications

Reagent or myeloperoxidase-generated hypochlorite affects discrete regions in lipid-free and lipid-associated human apolipoprotein A-I

Reagent or myeloperoxidase-generated hypochlorite affects discrete regions in lipid-free and lipid-associated human apolipoprotein A-I

Differential Regulation of Plastidial and Cytosolic Isoforms of Peptide Methionine Sulfoxide Reductase in Arabidopsis

Role of Oxidative Modifications in Atherosclerosis

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