Sources and role of iron in lipid peroxidation

Minotti, Giorgio

doi:10.1021/tx00032a001

Cited by 144 publications

(109 citation statements)

References 106 publications

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“…Uteroferrin functions to transport iron to the fetus (Roberts & Bazer 1988), which is considered essential for normal fetal development. However, iron-containing proteins catalyze lipid peroxidation in the presence of H 2 O 2 and ascorbic acid (Minotti 1993, Vallet 1995. Lipid peroxidation has been associated with cell death and has been shown to restrict intrauterine growth of mammalian fetuses (Karowicz-Bilinska 2004).…”

Section: Discussionmentioning

confidence: 99%

Global characterization of porcine intrauterine proteins during early pregnancy

Kayser¹,

Kim²,

Cerny³

et al. 2006

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Total protein secreted in the intrauterine lumen increases between day 10 and 13 post-estrus in both cyclic and pregnant gilts. The objective of this experiment was to identify those intrauterine proteins whose secretion changes during this time period. Sixteen mature gilts were either mated (day 0) or remained cyclic and were slaughtered at either day 10 or day 13 (n 5 4 per status by day). At slaughter, each uterine horn was flushed with 20 ml Minimal Essential Medium. Flushings were dialyzed extensively against distilled water. A 0.5 ml aliquot of each was lyophilized, subjected to two-dimensional PAGE, and protein spots were identified following Coomassie staining of each gel. Densitometry was used to compare relative amounts of each spot. After statistical analysis, spots that differed due to either day, status, or day by status interaction were excised and digested in-gel with trypsin. The resulting peptides were analyzed by tandem mass spectrometry (MS/MS). Using MS/MS data, protein identification for each spot was attempted. There were 280 matching spots, of which 132 were significantly (P < 0.05 or 0.01) affected by pregnancy status, day, or the day by status interaction. Most (73%) spots increased from day 10 to day 13 with no effect of pregnancy. Several spots were identified as proteases or their inhibitors. Others potentially modify glycolipids and/or glycoproteins. These results indicate that the concentrations of many proteins within the intrauterine environment during early pregnancy are independent of the conceptus and could play roles in regulating the endometrial or conceptus glycocalyx.

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Section: Discussionmentioning

confidence: 99%

Global characterization of porcine intrauterine proteins during early pregnancy

Kayser¹,

Kim²,

Cerny³

et al. 2006

Reproduction

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“…The ability of antioxidants to chelate Fe 2+ ions was determined by a photocolorimetric method (Minotti, 1993). In this assay, the compounds bind Fe 2+ ion, released by iron (II) sulfate.…”

Section: Methodsmentioning

confidence: 99%

The Effect of Some Polyphenols on Minced Pork during Refrigeration Compared with Ascorbic Acid

Predescu¹,

Papuc²,

Petcu³

et al. 2018

BUASVMCN-FST

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Quality of meat and meat products by two oxidative processes is affected. The two processes are lipid peroxidation and myoglobin oxidation. To delay oxidative processes, in meat and meat products are added compounds with antioxidant activity.The aim of this study was to evaluate the antioxidant activity of (±)-catechin, quercetin, and gallic acid, on oxidative processes in minced pork, comparatively with ascorbic acid in the same concentration. The ability of antioxidants to reduce DPPH• and to chelate Fe (II) were determinated. Minced pork samples separately with the chemicals were treated. The treated samples with antioxidants were preserved for seven days at refrigeration temperature. Myoglobin, oxymyoglobin, metmyoglobin concentrations, peroxide value, conjugated dienes and trienes levels and TBARS value were determined. Polyphenols have showed important hydrogen radical donator and iron chelator activity, higher as ascorbic acid activities. All antioxidants were effective in myoglobin oxidation and lipid peroxidation inhibition on minced pork, but the three polyphenols ((±)-catechin, quercetin, and gallic acid) protected better myoglobin than ascorbic acid as showed the results.

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“…It has been reported that when cardiomyocytes are exposed to doxorubicin, activation of the nuclear transcription factor NFkB and apoptosis occurred after redox cycling and formation of superoxide anion radicals and hydrogen peroxides [72]. Moreover, it has been shown that iron (Fe(II)) plays a key role in lipid peroxidation [73]. Because cells have very little or no free iron available to catalyse free radical reactions [74], it is conceivable that doxorubicin and doxorubicinol mediate iron release from ferritin and other cellular stores [73,75].…”

Section: Pharmacology and Toxicity Of Doxorubicinmentioning

confidence: 99%

“…Moreover, it has been shown that iron (Fe(II)) plays a key role in lipid peroxidation [73]. Because cells have very little or no free iron available to catalyse free radical reactions [74], it is conceivable that doxorubicin and doxorubicinol mediate iron release from ferritin and other cellular stores [73,75]. Toxic effects on a number of mitochondrial functions have been reported for metabolites of doxorubicin [76,77].…”

Section: Pharmacology and Toxicity Of Doxorubicinmentioning

confidence: 99%