Iron-catalyzed oxidation of Trp residues in low-density lipoprotein.
作者： Hsin-Hung Chen , Ching-Yi Chen , Lu-Ping Chow , Chu-Huang Chen , Yuan-Teh Lee
DOI: 10.1515/BC.2011.173
关键词: In vivo 、 Apolipoprotein B 、 Chelation 、 Ascorbic acid 、 In vitro 、 Tryptophan 、 Chemistry 、 Biochemistry 、 Stereochemistry 、 Low-density lipoprotein 、 Mass spectrometry
摘要: The mechanisms of oxidation low-density lipoproteins (LDLs) are not well defined, but epidemiological and experimental studies suggest that iron-catalyzed processes may contribute to atherogenesis. aim this study was test the hypothesis oxidations LDLs in vitro produce diagnostic biomarkers apolipoprotein could be applied vivo. were oxidized presence Fe2+, EDTA, ascorbic acid for up 40 h. Following delipidation trypsin digestion, peptides separated by HPLC, with four peaks detected at 365 nm, whereas none observed from unoxidized LDLs. identified MALDI-QTOF mass spectrometry as IVQILP(W+4) EQNEQVK, IYSL(W+4)EHSTK, FEGLQE(W+4)EGK, YH(W+4)EHTGLTLR, (W+4) rather than W residues protein. gains (+4 increase m/z tryptophan, W) absorbance nm indicate kynurenines, which trypsin-releasable on surface LDL particles. All thus characterized share sequence WE. preferential WE sequences contributions C-proximate glutamate chelation iron species, thereby influencing site selectivities oxidation. These kynurenine-containing might serve iron-mediated
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