4.5 Article

Human DJ-1 and its homologs are novel glyoxalases

期刊

HUMAN MOLECULAR GENETICS
卷 21, 期 14, 页码 3215-3225

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OXFORD UNIV PRESS
DOI: 10.1093/hmg/dds155

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资金

  1. Korea Institute of Planning and Evaluation for Technology in food, agriculture, forestry and fisheries
  2. Inha University
  3. National Research Foundation of Korea (NRF) [2011-0007189]
  4. Institute of Planning & Evaluation for Technology in Food, Agriculture, Forestry & Fisheries (iPET), Republic of Korea [IPET110056-3] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
  5. National Research Foundation of Korea [2011-0007189] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)

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Human DJ-1 is a genetic cause of early-onset Parkinsons disease (PD), although its biochemical function is unknown. We report here that human DJ-1 and its homologs of the mouse and Caenorhabditis elegans are novel types of glyoxalase, converting glyoxal or methylglyoxal to glycolic or lactic acid, respectively, in the absence of glutathione. Purified DJ-1 proteins exhibit typical MichaelisMenten kinetics, which were abolished completely in the mutants of essential catalytic residues, consisting of cysteine and glutamic acid. The presence of DJ-1 protected mouse embryonic fibroblast and dopaminergically derived SH-SY5Y cells from treatments of glyoxals. Likewise, C. elegans lacking cDJR-1.1, a DJ-1 homolog expressed primarily in the intestine, protected worms from glyoxal-induced death. Sub-lethal doses of glyoxals caused significant degeneration of the dopaminergic neurons in C. elegans lacking cDJR-1.2, another DJ-1 homolog expressed primarily in the head region, including neurons. Our findings that DJ-1 serves as scavengers for reactive carbonyl species may provide a new insight into the causation of PD.

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