This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsReferences
Alaiz, M., and Barragan, S. 1995. Changes induced in bovine serum albumin following interactions with the lipid peroxidation product E-2-octenal. Chem. Phys. Lipids. 77:217–223.
Amarnath, V., Amarnath, K., Valentine, W. M., Eng, M. A., and Graham, D. G. 1995. Intermediates in the Paal–Knorr synthesis of pyrroles. 4-Oxoaldehydes. Chem. Res. Toxicol. 8:234–238.
Asselin, C., Bouchard, B., Tardif, J. C., and Des Rosiers, C. 2006. Circulating 4-hydroxynonenal-protein thioether adducts assessed by gas chromatography-mass spectrometry are increased with disease progression and aging in spontaneously hypertensive rats. Free Rad. Biol. Med. 41:97–105.
Baker, A., Zidek, L., Wiesler, D., Chmelik, J., Pagel, M., and Novotny, M. V. 1998. Reaction of N-acetylglycyllysine methyl ester with 2-alkenals: an alternative model for covalent modification of proteins. Chem. Res. Toxicol. 11:730–740.
Bateman, R. H., Carruthers, R., Hoyes, J. B., Jones, C., Langridge, J. I., Millar, A., and Vissers, J. P. C. 2002. A novel precursor ion discovery method on a hybrid quadrupole orthogonal acceleration time-of-flight (Q-TOF) mass spectrometer for studying protein phosphorylation. J. Am. Soc. Mass Spectrom. 13:792–803.
Bolgar, M. S., and Gaskell, S. J. 1996. Determination of the sites of 4-hydroxy-2-nonenal adduction to protein by electrospray tandem mass spectrometry. Anal. Chem. 68:2325–2330.
Burcham, P. C., and Pyke, S. M. 2006. Hydralazine inhibits rapid acrolein-induced protein oligomerization: role of aldehyde scavenging and adduct trapping in cross-link blocking and cytoprotection. Mol. Pharmacol. 69:1056–1065.
Conklin, D. J., Prough, R. A., and Bhatnagar, A., 2006. Aldehyde metabolism in the cardiovascular system. Mol. Biosys. 2:1–16.
Domon, B., and Aebersold, R. 2006. Mass spectrometry and protein analysis. Science 312:212–217.
Doorn, J. A., and Petersen, D. R. 2002. Covalent modification of amino acid nucleophiles by the lipid peroxidation products 4-hydroxy-2-nonenal and 4-oxo-2-nonenal. Chem. Res. Toxicol. 15:1445–1450.
Esterbauer, H., Schaur, R. J., and Zollner, H. 1991. Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Rad. Biol. Med. 11:81–128.
Fenaille, F., Guy, P. A., and Tabet, J. C. 2003. Study of protein modification by 4-hydroxy-2-nonenal and other short chain aldehydes analyzed by electrospray ionization tandem mass spectrometry. J. Am. Soc. Mass Spectrom. 14:215–226.
Fenaille, F., Tabet, J. C., and Guy, P. A. 2004. Identification of 4-hydroxy-2-nonenal-modified peptides within unfractionated digests using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Anal. Chem. 76:867–873.
Furuhata, A., Ishii, T., Kumazawa, S., Yamada, T., Nakayama, T., and Uchida, K. 2003. N ɛ-(3-methylpyridinium)lysine, a major antigenic adduct generated in acrolein-modified protein. J. Biol. Chem. 278:48658–48665.
Furuhata, A., Nakamura, M., Osawa, T., and Uchida, K. 2002. Thiolation of protein-bound carcinogenic aldehyde. An electrophilic acrolein–lysine adduct that covalently binds to thiols. J. Biol. Chem. 277:27919–27926.
Ichihashi, K., Osawa, T., Toyokuni, S., and Uchida, K. 2001. Endogenous formation of protein adducts with carcinogenic aldehydes: implications for oxidative stress. J. Biol. Chem. 276:23903–23913.
Isom, A. L., Barnes, S., Wilson, L., Kirk, M., Coward, L., and Darley-Usmar, V. 2004. Modification of cytochrome c by 4-hydroxy-2-nonenal: evidence for histidine, lysine, and arginine–aldehyde adducts. J. Am. Soc. Mass Spectrom. 15:1136–1147.
Han, X., Jin, M., Breuker, K., and McLafferty, F. W. 2006. Extending top-down mass spectrometry to proteins with masses greater than 200 kilodaltons. Science 314:109–112.
Hansen, B. T., Jones, J. A., Mason, D. E., and Liebler, D. C. 2001. SALSA: a pattern recognition algorithm to detect electrophile-adducted peptides by automated evaluation of CID spectra in LC-MS-MS analyses. Anal. Chem. 73:1676–1683.
Hansen, B. T., Davey, S. W., Ham, A. J., and Liebler, D. C. 2005. P-Mod: an algorithm and software to map modifications to peptide sequences using tandem MS data. J. Proteome Res. 4:358–368.
Ji, C., Kozak, K. R., and Marnett, L. J. 2004. IkappaB kinase, a molecular target for inhibition by 4-hydroxy-2-nonenal. J. Biol. Chem. 276:18233–18228.
Lee, S. H., and Blair, I. A. 2000. Characterization of 4-oxo-2-nonenal as a novel product of lipid peroxidation. Chem. Res. Toxicol. 13:698–702.
Lin, D., Lee, H. G., Liu, Q., Perry, G., Smith, M. A., and Sayre, L. M. 2005. 4-Oxo-2-nonenal is both more neurotoxic and more protein reactive than 4-hydroxy-2-nonenal. Chem. Res. Toxicol. 18:1219–1231.
Liu, Z., Minkler, P. E., and Sayre, L. M. 2003. Mass spectroscopic characterization of protein modification by 4-hydroxy-2-(E)-nonenal and 4-oxo-2-(E)-nonenal. Chem. Res. Toxicol. 16:901–911.
Miyagi, M., and Rao, K. C. S. 2007. Proteolytic 18O-labeling strategies for quantitative proteomics. Mass Spectrom. Rev. 26:121–136.
Nielsen, J. E., and Vriend, G. 2001. Optimizing the hydrogen-bond network in Poisson–Boltzmann equation-based pK(a) calculations. Proteins 43:403–412.
Oe, T., Lee, S. H., Silva Elipe, M. V., Arison, B. H., and Blair, I. A. 2003a. A novel lipid hydroperoxide-derived modification to arginine. Chem. Res. Toxicol. 16:1598–1605.
Oe, T., Arora, J. S., Lee, S. H., and Blair, I. A. 2003b. A novel lipid hydroperoxide-derived cyclic covalent modification to histone H4. J. Biol. Chem. 278:42098–42105.
Robino, G., Zamara, E., Novo, E., Dianzani, M. U., Parola, M. 2001. 4-hydroxy-2,3-alkenals as signal molecules modulating proliferative and adaptative cell responses. Biofactors 15:103–106.
Ruef, J., Rao, G. N., Li, F., Bode, C., Patterson, C., Bhatnagar, A., and Runge, M. S. 1998. Induction of rat aortic smooth muscle cell growth by the lipid peroxidation product 4-hydroxy-2-nonenal. Circulation 97:1071–1078.
Salomon, R. G., Kaur, K., Podrez, E., Hoff, H. F., Krushinsky, A. V., and Sayre, L. M. 2000. HNE-derived 2-pentylpyrroles are generated during oxidation of LDL, are more prevalent in blood plasma from patients with renal disease or atherosclerosis, and are present in atherosclerotic plaques. Chem. Res. Toxicol. 13:557–564.
Sampey, B. P., Carbone, D. L., Doorn, J. A., Drechsel, D. A. and Peterson, D. R. 2007. 4-Hydroxy-2-nonenal adduction of extracelluar signal-regulated kinase (ERK) and the inhibition of hepatocyte Erk-Est-like Protein-1-activating Protein-1 signal transduction. Mol. Pharmacol. 71:871–883.
Sayre, L. M., Arora, P. K., Iyer, R. S., and Salomon, R. G. 1993. Pyrrole formation from 4-hydroxynonenal and primary amines. Chem. Res. Toxicol. 6:19–22.
Sayre, L. M., Sha, W., Xu, G., Kaur, K., Nadkarni, D., Subbanagounder, G., and Salomon, R. G. 1996. Immunochemical evidence supporting 2-pentylpyrrole formation on proteins exposed to 4-hydroxy-2-nonenal. Chem. Res. Toxicol. 9:1194–1201.
Shao, B., Fu, X., McDonald, T. O., Green, P. S., Uchida, K., O'Brien, K. D., Oram, J. F., and Heinecke, J. W. 2005. Acrolein impairs ATP binding cassette transporter A1-dependent cholesterol export from cells through site-specific modification of apolipoprotein A-I. J. Biol. Chem. 280:36386–36396.
Spiteller, P., Kern, W., Reiner, J., and Spiteller, G. 2001. Aldehydic lipid peroxidation products derived from linoleic acid. Biochim. Biophys. Acta 1531:188–208.
Szapacs, M. E., Riggins, J. N., Zimmerman, L. J., and Liebler, D. C. 2006. Covalent adduction of human serum albumin by 4-hydroxy-2-nonenal: kinetic analysis of competing alkylation reactions. Biochemistry 45:10521–10528.
Uchida, K., Kanematsu, M., Morimitsu, Y., Osawa, T., Noguchi, N., and Niki, E. 1998a. Acrolein is a product of lipid peroxidation reaction. Formation of free acrolein and its conjugate with lysine residues in oxidized low density lipoproteins. J. Biol. Chem. 273:16058–16066.
Uchida, K., Kanematsu, M., Sakai, K., Matsuda, T., Hattori, N., Mizuno, Y., Suzuki, D., Miyata, T., Noguchi, N., Niki, E., and Osawa, T. 1998b. Protein-bound acrolein: potential markers for oxidative stress. Proc. Natl. Acad. Sci. USA. 95:4882–4887.
Uchida, K., and Stadtman, E. R. 1992. Selective cleavage of thioether linkage in proteins modified with 4-hydroxynonenal. Proc. Natl. Acad. Sci. USA. 89:5611–5615.
Uchida, K., and Stadtman, E. R. 1993. Covalent attachment of 4-hydroxynonenal to glyceraldehyde-3-phosphate dehydrogenase. A possible involvement of intra- and intermolecular cross-linking reaction. J. Biol. Chem. 268:6388–6393.
Veronneau, M., Comte, B., and Des Rosiers, C. 2002. Quantitative gas chromatographic-mass spectrometric assay of 4-hydroxynonenal bound to thiol proteins in ischemic/reperfused rat hearts. Free Rad. Biol. Med. 33:1380–1388.
Xu, G., Liu, Y., Kansal, M. M., and Sayre, L. M. 1999. Rapid cross-linking of proteins by 4-ketoaldehydes and 4-hydroxy-2-alkenals does not arise from the lysine-derived monoalkylpyrroles. Chem. Res. Toxicol. 12:855–861.
Xu, G., and Sayre, L. M. 1998. Structural characterization of a 4-hydroxy-2-alkenal-derived fluorophore that contributes to lipoperoxidation-dependent protein cross-linking in aging and degenerative disease. Chem. Res. Toxicol. 11:247–251.
Xu, G., and Sayre, L. M. 1999. Structural elucidation of a 2:2 4-ketoaldehyde-amine adduct as a model for lysine-directed cross-linking of proteins by 4-ketoaldehydes. Chem. Res. Toxicol. 12:862–868.
Zaugg, R. H., Walder, J. A., and Klotz, I. M. 1977. Schiff base adducts of hemoglobin. Modifications that inhibit erythrocyte sickling. J. Biol. Chem. 252:8542–8548.
Zhang, W. H., Liu, J., Xu, G., Yuan, Q., and Sayre, L. M. 2003. Model studies on protein side chain modification by 4-oxo-2-nonenal. Chem. Res. Toxicol. 16:512–523.
Acknowledgements
Supported in part by PO1 ES11860 and ES12062. The authors wish to thank David Hoetker for his expert technical assistance with ESI-MS analyses. JC and BGH contributed jointly as first authors in the preparation of this article.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2008 Springer Science+Business Media, LLC
About this chapter
Cite this chapter
Cai, J., Hill, B., Bhatnagar, A., Pierce, W., Prough, R. (2008). Bioactivation and Protein Modification Reactions of Unsaturated Aldehydes. In: Elfarra, A. (eds) Advances in Bioactivation Research. Biotechnology: Pharmaceutical Aspects, vol IX. Springer, New York, NY. https://doi.org/10.1007/978-0-387-77300-1_9
Download citation
DOI: https://doi.org/10.1007/978-0-387-77300-1_9
Published:
Publisher Name: Springer, New York, NY
Print ISBN: 978-0-387-77299-8
Online ISBN: 978-0-387-77300-1
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)