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Mol. Cells 2002; 13(1): 107-113

Published online January 1, 1970

© The Korean Society for Molecular and Cellular Biology

Protection by Carnosine-related Dipeptides against Hydrogen Peroxide-mediated Ceruloplasmin Modification

Jung Hoon Kang, Kyung Sik Kim, SooYoung Choi, Hyeok Yil Kwon, Moo Ho Won, Tae-Cheon Kang

Abstract

Carnosine, homocarnosine, and anserine are present in high concentrations in the muscle and brain of many animals and humans. Previous studies showed that these compounds have an antioxidant function. We investigated the protective effects of carnosine and related compounds on the modification of human ceruloplasmin that is induced by H2O2. Carnosine, homocarnosine, and anserine significantly inhibited the fragmentation and inactivation of ceruloplasmin that is induced by H2O2. All three compounds also inhibited the release of copper ion from protein, and the formation of hydroxyl radicals in the ceruloplas-min/H2O2 system. These compounds inhibited the fragmentation of human serum albumin that is in-duced by the copper-catalyzed oxidation system, as well as by the iron-catalyzed oxidation system. These results suggest that carnosine, homocarnosine, and anserine might protect ceruloplasmin against H2O2-mediated oxidative damage through a combination of copper chelation and free radical scavenging.

Keywords Ceruloplasmin, Fragmentation, Carnosine,

Article

Research Article

Mol. Cells 2002; 13(1): 107-113

Published online February 28, 2002

Copyright © The Korean Society for Molecular and Cellular Biology.

Protection by Carnosine-related Dipeptides against Hydrogen Peroxide-mediated Ceruloplasmin Modification

Jung Hoon Kang, Kyung Sik Kim, SooYoung Choi, Hyeok Yil Kwon, Moo Ho Won, Tae-Cheon Kang

Abstract

Carnosine, homocarnosine, and anserine are present in high concentrations in the muscle and brain of many animals and humans. Previous studies showed that these compounds have an antioxidant function. We investigated the protective effects of carnosine and related compounds on the modification of human ceruloplasmin that is induced by H2O2. Carnosine, homocarnosine, and anserine significantly inhibited the fragmentation and inactivation of ceruloplasmin that is induced by H2O2. All three compounds also inhibited the release of copper ion from protein, and the formation of hydroxyl radicals in the ceruloplas-min/H2O2 system. These compounds inhibited the fragmentation of human serum albumin that is in-duced by the copper-catalyzed oxidation system, as well as by the iron-catalyzed oxidation system. These results suggest that carnosine, homocarnosine, and anserine might protect ceruloplasmin against H2O2-mediated oxidative damage through a combination of copper chelation and free radical scavenging.

Keywords: Ceruloplasmin, Fragmentation, Carnosine,

Mol. Cells
May 31, 2023 Vol.46 No.5, pp. 259~328
COVER PICTURE
The alpha-helices in the lamin filaments are depicted as coils, with different subdomains distinguished by various colors. Coil 1a is represented by magenta, coil 1b by yellow, L2 by green, coil 2a by white, coil 2b by brown, stutter by cyan, coil 2c by dark blue, and the lamin Ig-like domain by grey. In the background, cells are displayed, with the cytosol depicted in green and the nucleus in blue (Ahn et al., pp. 309-318).

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