bp(MESH:"Lipid Peroxidation")
PPAR-a is known to regulate lipid oxidation but is not highly expressed in the brain [20]. PubMed:21718217
Identical results were obtained with the antioxidant dithiothreitol (DTT) (data not shown). PubMed:25301065
Consistently, we measured increased lipid peroxidation in both cells and tissues exposed to free heme, which can be rescued by α-tocopherol, an agent able to react with lipid radicals and interrupt the oxidation reaction. PubMed:28400318
FeCl3 treatment resulted in a dose- (Fig. 3) and timedependent (data not shown) increase inRBClipid peroxidation, which correlated closely with hemolysis (Fig. 2B). PubMed:19276082
In contrast, at an equal antioxidant concentration, Trolox completely blocked heme-triggered lipid peroxidation (measured as production of thiobarbituric acid reactive substances (TBARS)) in soybean lecithin micelles (Figure 7g). PubMed:25301065
Free heme is a potent trigger of lipid peroxidation and a promoter of inflammation.4–6 PubMed:26794659
Previously we have shown that heme can enter the lipid moiety of LDL and induce iron-dependent lipid peroxidation.8 PubMed:20378845
Here we demonstrate that lipids isolated from human atheromatous lesions – which are already in an oxidized state – can be further oxidized in the presence of heme, whereas this effect is not observed using lipids isolated from normal vasculature. PubMed:20378845
Thus, it appears that these extracts oxidize ferrohemoglobin to ferrihemoglobin, thereby leading to heme instability and heme-mediated initiation of lipid peroxidation. PubMed:20378845
Besides its physiological importance, heme has a potent oxidative capacity oxidizing lipids (Tappel, 1953, 1955; Vincent et al., 1988) and proteins (Aft and Mueller, 1984; Vincent, 1989), and damaging DNA (Aft and Mueller, 1983). PubMed:24904418
In contrast, at an equal antioxidant concentration, Trolox completely blocked heme-triggered lipid peroxidation (measured as production of thiobarbituric acid reactive substances (TBARS)) in soybean lecithin micelles (Figure 7g). PubMed:25301065
Toxicity of free hemoglobin is also caused by the release of cell-free heme, which produces lipid peroxidation and mitochondrial damage and increases the production of reactive oxygen species. PubMed:27515135
Consistently, we measured increased lipid peroxidation in both cells and tissues exposed to free heme, which can be rescued by α-tocopherol, an agent able to react with lipid radicals and interrupt the oxidation reaction. PubMed:28400318
These radicals may initiate further lipid peroxidation forming alkyl radicals that in the presence of O2 form more peroxyl radicals leading to a facile propagation of free radical reactions. PubMed:24904418
Malondialdehyde (MDA) represents evidence of systemic oxidative stress and inflammation [31], and is commonly used to estimate the level of lipid peroxidation. PubMed:30324533
These radicals may initiate further lipid peroxidation forming alkyl radicals that in the presence of O2 form more peroxyl radicals leading to a facile propagation of free radical reactions. PubMed:24904418
Inhibition of lipid oxidation by either haptoglobin or hemopexin reduced the cytotoxicity (Fig 4B) and HO-1 induction caused by sublethal amounts of pretreated atheromatous lesion lipids (Fig 4C and D). PubMed:20378845
As is true of intact hemoglobin, lipid extracts from atheromatous lesions exposed to heme also underwent lipid peroxidation as reflected by the accumulation of thiobarbituric acid-reactive substances (TBARs) and lipid hydroperoxides (supplemental Fig I). PubMed:20378845
Both BSA and BSA-T attenuated heme/H2O2/NO2 −-induced protein carbonylation and lipid peroxidation. PubMed:30324533
Inhibition of lipid oxidation by either haptoglobin or hemopexin reduced the cytotoxicity (Fig 4B) and HO-1 induction caused by sublethal amounts of pretreated atheromatous lesion lipids (Fig 4C and D). PubMed:20378845
Both ROS and lipid peroxidation were increased in the heart of Hx-/- mice compared to that of wild-type animals (Figure 2C, D). PubMed:28400318
Inhibition of lipid oxidation by either haptoglobin or hemopexin reduced the cytotoxicity (Fig 4B) and HO-1 induction caused by sublethal amounts of pretreated atheromatous lesion lipids (Fig 4C and D). PubMed:20378845
Both BSA and BSA-T attenuated heme/H2O2/NO2 −-induced protein carbonylation and lipid peroxidation. PubMed:30324533
Interestingly enough, lipid peroxidation has been shown to decrease the number of nAChRs in PC12 cells (Guan et al 2000a) PubMed:11230871
FeCl3 treatment resulted in a dose- (Fig. 3) and timedependent (data not shown) increase inRBClipid peroxidation, which correlated closely with hemolysis (Fig. 2B). PubMed:19276082
Inhibition of lipid oxidation by either haptoglobin or hemopexin reduced the cytotoxicity (Fig 4B) and HO-1 induction caused by sublethal amounts of pretreated atheromatous lesion lipids (Fig 4C and D). PubMed:20378845
Previously we have shown that heme can enter the lipid moiety of LDL and induce iron-dependent lipid peroxidation.8 PubMed:20378845
Here we demonstrate that lipids isolated from human atheromatous lesions – which are already in an oxidized state – can be further oxidized in the presence of heme, whereas this effect is not observed using lipids isolated from normal vasculature. PubMed:20378845
Thus, it appears that these extracts oxidize ferrohemoglobin to ferrihemoglobin, thereby leading to heme instability and heme-mediated initiation of lipid peroxidation. PubMed:20378845
Besides its physiological importance, heme has a potent oxidative capacity oxidizing lipids (Tappel, 1953, 1955; Vincent et al., 1988) and proteins (Aft and Mueller, 1984; Vincent, 1989), and damaging DNA (Aft and Mueller, 1983). PubMed:24904418
Free heme is a potent trigger of lipid peroxidation and a promoter of inflammation.4–6 PubMed:26794659
Toxicity of free hemoglobin is also caused by the release of cell-free heme, which produces lipid peroxidation and mitochondrial damage and increases the production of reactive oxygen species. PubMed:27515135
Malondialdehyde (MDA) represents evidence of systemic oxidative stress and inflammation [31], and is commonly used to estimate the level of lipid peroxidation. PubMed:30324533
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If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.