Riboflavin nutritional status and flavoprotein enzymes in streptozotocin-diabetic rats
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Cited by (16)
The role of PDI as a survival factor in cardiomyocyte ischemia
2011, Methods in EnzymologyCitation Excerpt :As diabetes has been described to induce a pathologic state called diabetic cardiomyopathy (Hayat et al., 2004; Kannel et al., 1974; Rubler et al., 1972) in which ER stress plays a pivotal role, in this paragraph, we focus on the evaluation of PDI expression and redox state in the diabetic heart. Several pieces of evidence showed that the intracellular level of small molecules as FAD is lower in both diabetic animal models and diabetic patients (Banhegyi et al., 1998, Reddi, 1986) and that the activity of some FAD-containing enzymes, as Ero1, is significantly lower in experimental diabetes (Nardai et al., 2003). In streptozotocin-induced diabetic rats, despite of the oxidative changes of the extracellular space, the redox environment of liver microsomal vesicles was shifted to a more reduced state with an increase of total thiol content and an increase of protein-thiol/disulfide ratio (Nardai et al., 2005).
ACP1 genotype, glutathione reductase activity, and riboflavin uptake affect cardiovascular risk in the obese
2009, Metabolism: Clinical and ExperimentalCitation Excerpt :However, riboflavin deficiency has been shown to be highly prevalent among diabetic rats and mice. Eighty-three percent of genetically diabetic KK mice were found to be deficient in riboflavin on a normal diet, showing significantly reduced GR activity [42], whereas 100% of streptozotocin-diabetic rats showed riboflavin deficiency and reduced GR activity [43]. It has been shown that riboflavin supplementation of 1.6 mg/d may significantly reduce levels of homocysteine in homozygote carriers of the 677C3T polymorphism of the MTHFR gene by as much as 40% in those patients with lower riboflavin status at baseline and by 22% overall [44].
Diabetic changes in the redox status of the microsomal protein folding machinery
2005, Biochemical and Biophysical Research CommunicationsCitation Excerpt :In addition to dehydroascorbic acid, FAD also participates in the redox changes of the ER [50,51]. Earlier data showed that the level of FAD and the activity of FAD-enzymes are both decreased in diabetes [52]. Here, we showed FAD was unable to sufficiently re-oxidize protein thiols in diabetic microsomes despite of the potent oxidation of ER proteins by extramicrosomal FAD [51].
Antioxidant systems and erythrocyte life-span in mammals
1993, Comparative Biochemistry and Physiology -- Part B: Biochemistry and