https://orcid.org/0000-0002-6925-1268
Abstract
Aim: Advanced glycation end products (AGE) are the biomarkers of aging and diabetes which are formed via reactions between glycating agents and biomacromolecules. However, no proteomic study has been reported to systematically investigate the protein substrates of AGEs. Results: In this paper, we used an aniline-based probe to capture the glyoxal-imine intermediate which is the transition sate of glyoxal-derived AGEs. Combined with the tandem orthogonal proteolysis activity-based protein profiling strategy, we successfully identified 962 lysines modified by glyoxal. Conclusion: Enzymes in glycolysis are heavily modified by glyoxal and our biochemical experiments showed that glyoxal can significantly inhibit the activity of GAPDH and glycolysis. These data indicated that AGEs modifications may contribute to pathological processes through impairing the glycolytic process.
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Supplementary data
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Acknowledgments
The authors thank the Computing Platform of the Center for Life Science for supporting the proteomic data analysis.
Financial & competing interests disclosure
This work was supported by Ministry of Science and Technology of China (2016YFA0501500), National Science Foundation of China (21472008, 81490741 and 21778004), and a “1000 Talents Plan” Young Investigator Award (C.W.). The authors have no other relevant affiliations or financial involvement with any organization or entity with a financial interest in or financial conflict with the subject matter or materials discussed in the manuscript apart from those disclosed.
No writing assistance was utilized in the production of this manuscript.