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The Role of Parkinsonism Associated Protein HsDJ-1 in Deglycation Activity

Undergraduate #167
Discipline: Chemistry and Chemical Sciences
Subcategory: Biochemistry (not Cell and Molecular Biology and Genetics)

Jatauria Lathan - Dillard University
Co-Author(s): Dr. Jiusheng Lin and Dr. Mark Wilson,University of Nebraska- Lincoln, Lincoln, Nebraska



HsDJ-1 is a 20 kDa neuroprotective, oxidative stress response protein that plays a key role in shielding cells against reactive oxygen species and mitochondrial damage. It contains an oxidation sensitive cysteine (C106), a highly conserved residue which is essential for DJ-1 to confer cellular protection. The oxidation of C106 is proposed to play an essential role in allowing DJ-1 to function as a redox sensor, although it may also provide a catalytic nucleophile for several proposed but unverified enzymatic activities of DJ-1. It has been recently reported that HsDJ-1 functions as a protein deglycase, removing the early glycation products formed when methylglyoxal (MG) reacts with proteins and nucleic acids. This hypothesis is important, as it would ascribe a long-sought enzymatic function to DJ1 and may help explain the protein’s involvement in several human disease states. HsDJ-1, HsDJ-1(O) HsDJ- 1 E18N, HsDJ-1 C106S, and HsDJ-1 E18D proteins were purified and utilized to test glycation activity. The glycation of N-acetyl- cysteine (NacCys) by methylglyoxal (MG) to form a hemithioacetal and its deglycation by DJ-1 was measured to quantify the enzymatic activity of DJ-1.

Not Submitted

Funder Acknowledgement(s): This work was supported by NSF grant DBI-1461240 and the Nebraska Redox Biology Center REU program.

Faculty Advisor: Dr. Ruby Broadway, rbroadway@dillard.edu

Role: My role in this research project was to purify the proteins that were used in the experiment as well as measure and record data obtained from enzymatic activity.

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This material is based upon work supported by the National Science Foundation (NSF) under Grant No. DUE-1930047. Any opinions, findings, interpretations, conclusions or recommendations expressed in this material are those of its authors and do not represent the views of the AAAS Board of Directors, the Council of AAAS, AAAS’ membership or the National Science Foundation.

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