TY - JOUR
T1 - Mass spectrometric characterizations of protein carbonylation
T2 - Comparison between three different conditions, oxidation by CuII/ascorbic acid, adduction of methyl glyoxal, and adduction of 4-hydroxy-2(E)-nonenal
AU - Kazuki, Maeda
AU - Funatsu, Hiroyuki
AU - Miyazawa, Yuki
AU - Misawa, Yasushi
AU - Goto, Takaaki
AU - Lee, Seon Hwa
AU - Oe, Tomoyuki
N1 - Funding Information:
This work was supported in part by a Grant-in-Aid for Challenging Exploratory Research (to T.O., No. 23659016 for 2011–2012) and Grants-in-Aid for Scientific Research (C) (to T.G., No. 40344684 for 2012–2014; to S.H.L., No. 22590130 for 2010–2012 and No. 25460186 for 2013–2015) from the Japan Society for the Promotion of Science. The authors also thank Professor Ian A. Blair (University of Pennsylvania, Philadelphia, PA, USA) for donating a used LCQ Deca.
PY - 2014/11/15
Y1 - 2014/11/15
N2 - Oxidative stress can cause various protein modifications, mainly carbonylation. There are three major chemical ways to introduce hydrazine reactive carbonyls: (i) direct oxidation by reactive oxygen species (ROS), (ii) adduction of sugars or sugar-related aldehydes, and (iii) adduction of lipid-related aldehydes. Here, we performed a comparative study of three representative conditions: CuII/ascorbic acid (AA) (ROS), methylglyoxal (sugar-related), and 4-hydroxy-2(E)-nonenal (HNE) (lipid-related). Insulin β chain and Girard's reagent P were used as the model protein and hydrazine reagent, respectively. LC/MS analyses of reactions with HNE or CuII/AA-treated linoleic acid revealed that protein carbonylation under oxidative stress is the most efficient in the presence of polyunsaturated fatty acids.
AB - Oxidative stress can cause various protein modifications, mainly carbonylation. There are three major chemical ways to introduce hydrazine reactive carbonyls: (i) direct oxidation by reactive oxygen species (ROS), (ii) adduction of sugars or sugar-related aldehydes, and (iii) adduction of lipid-related aldehydes. Here, we performed a comparative study of three representative conditions: CuII/ascorbic acid (AA) (ROS), methylglyoxal (sugar-related), and 4-hydroxy-2(E)-nonenal (HNE) (lipid-related). Insulin β chain and Girard's reagent P were used as the model protein and hydrazine reagent, respectively. LC/MS analyses of reactions with HNE or CuII/AA-treated linoleic acid revealed that protein carbonylation under oxidative stress is the most efficient in the presence of polyunsaturated fatty acids.
KW - 4-Hydroxy-2(E)-nonenal
KW - Carbonylation
KW - Methylglyoxal
KW - Oxidative stress
KW - Protein
KW - Reactive oxygen species
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U2 - 10.1016/j.ijms.2014.09.012
DO - 10.1016/j.ijms.2014.09.012
M3 - Article
AN - SCOPUS:84908003863
VL - 373
SP - 72
EP - 80
JO - International Journal of Mass Spectrometry and Ion Physics
JF - International Journal of Mass Spectrometry and Ion Physics
SN - 1387-3806
ER -