Literature DB >> 8503899

Plasma glutathione peroxidase reduces phosphatidylcholine hydroperoxide.

Y Yamamoto1, Y Nagata, E Niki, K Watanabe, S Yoshimura.   

Abstract

The reducing activity of rat plasma glutathione peroxidase on phosphatidylcholine hydroperoxide (PC-OOH) and cholesteryl ester hydroperoxide (CE-OOH) was examined since these hydroperoxides are the major oxidation products of plasma. PC-OOH was reduced by the enzyme while CE-OOH was not. The reduction of PC-OOH by the enzyme ceased when all thiol was consumed, but the activity was recovered by the addition of glutathione, suggesting glutathione is important to keep the enzyme in the reduced form. These results are consistent with the findings that CE-OOH is present in human and rat plasmas while PC-OOH is undetectable and suggest that one of the physiological roles of the enzyme is to reduce PC-OOH.

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Year:  1993        PMID: 8503899     DOI: 10.1006/bbrc.1993.1600

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  3 in total

1.  Phosphatidylcholine hydroperoxide levels in human plasma are lower than previously reported.

Authors:  Junko Adachi; Naoki Yoshioka; Rika Funae; Yasushi Nagasaki; Takeaki Naito; Yasuhiro Ueno
Journal:  Lipids       Date:  2004-09       Impact factor: 1.880

2.  Human blood cells support the reduction of low-density-lipoprotein-associated cholesteryl ester hydroperoxides by albumin-bound ebselen.

Authors:  J Christison; H Sies; R Stocker
Journal:  Biochem J       Date:  1994-12-01       Impact factor: 3.857

Review 3.  Gene-activation mechanisms in the regression of atherosclerosis, elimination of diabetes type 2, and prevention of dementia.

Authors:  P V Luoma
Journal:  Curr Mol Med       Date:  2011-07       Impact factor: 2.222

  3 in total

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