Secondary lipid oxidation products modify and impact the function of proteins. Identifying where and how these products modify a protein's structure would allow for targeted approaches to mitigate or prevent this modification. Here, we purified calpain-2, a neutral calcium dependent cysteine protease, from porcine skeletal muscle and conducted in-vitro experiments using various concentrations of malondialdehyde, 2-hexenal, and 4-hydroxynonenal. We determined these secondary lipid oxidation products differentially impact calpain-2 proteolytic activity and autolysis. We identified modifications of malondialdehyde and hexenal on calpain-2 with LC-MS/MS approaches. We further evaluated the number of adduction sites on the catalytic and regulatory subunits of calpain-2 through MALDI-MS approaches. These data demonstrate that secondary lipid oxidation products can modify and differentially impact calpain-2.
[doi:10.25345/C56M33F0S]
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: in-vitro ; malondialdehyde ; hexenal ; 4-hydroxynonenal ; calpain-2
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Principal Investigators: (in alphabetical order) |
Steven Lonergan, Iowa State University, United States of America |
| Submitting User: | lgjohnson |
Logan G. Johnson, Chaoyu Zhai, Kitty Brown, Jessica E. Prenni, Mahesh N. Nair., Elisabeth Huff-Lonergan, and Steven M. Lonergan.
Secondary Lipid Oxidation Products as Modulators of Calpain-2 Functionality In Vitro.
J. Agric. Food Chem. 2024. doi: 10.1021/acs.jafc.4c00335.
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