Molecular mechanism of recombinant liver fatty acid binding protein's antioxidant activity

Yan, J., Gong, Y. W., She, Y. M., Wang, G. Q., Roberts, M. S. and Burczynski, F. J. (2009) Molecular mechanism of recombinant liver fatty acid binding protein's antioxidant activity. Journal of Lipid Research, 50 12: 2445-2454. doi:10.1194/jlr.M900177-JLR200

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Author Yan, J.
Gong, Y. W.
She, Y. M.
Wang, G. Q.
Roberts, M. S.
Burczynski, F. J.
Title Molecular mechanism of recombinant liver fatty acid binding protein's antioxidant activity
Journal name Journal of Lipid Research   Check publisher's open access policy
ISSN 0022-2275
1539-7262
Publication date 2009-05-27
Sub-type Article (original research)
DOI 10.1194/jlr.M900177-JLR200
Open Access Status File (Publisher version)
Volume 50
Issue 12
Start page 2445
End page 2454
Total pages 10
Editor Dennis, Edward A.
Place of publication United States
Publisher American Society for Biochemistry and Molecular Biology
Collection year 2010
Language eng
Subject C1
110106 Medical Biochemistry: Proteins and Peptides (incl. Medical Proteomics)
92 Health
Formatted abstract
Hepatocytes expressing liver fatty acid binding protein (L-FABP) are known to be more resistant to oxidative stress than those devoid of this protein. The mechanism for the observed antioxidant activity is not known. We examined the antioxidant mechanism of a recombinant rat L-FABP in the presence of a hydrophilic (AAPH) or lipophilic (AMVN) free radical generator. Recombinant L-FABP amino acid sequence and its amino acid oxidative products following oxidation were identified by MALDI quadrupole time-of-flight MS after being digested by endoproteinase Glu-C. L-FABP was observed to have better antioxidative activity when free radicals were generated by the hydrophilic generator than by the lipophilic generator. Oxidative modification of L-FABP included up to five methionine oxidative peptide products with a total of ~80 Da mass shift compared with native L-FABP. Protection against lipid peroxidation of L-FABP after binding with palmitate or {alpha}-bromo-palmitate by the AAPH or AMVN free radical generators indicated that ligand binding can partially block antioxidant activity. We conclude that the mechanism of L-FABP's antioxidant activity is through inactivation of the free radicals by L-FABP's methionine and cysteine amino acids. Moreover, exposure of the L-FABP binding site further promotes its antioxidant activity. In this manner, L-FABP serves as a hepatocellular antioxidant.
Keyword Hepatocyte
Oxidative stress
Free radical
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: 2010 Higher Education Research Data Collection
School of Medicine Publications
 
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Created: Sun, 29 Nov 2009, 00:03:02 EST