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Parkinsonism-associated protein DJ-1 is a bona fide deglycase.


Maximus Peto’s Commentary

Here, these researchers report on deglycase activity of DJ-1, which apparently acts to deglycate glyoxal- and methylglyoxal-glycated proteins. I leave readers to decide whether this is new, interesting, and/or relevant for age-related accumulation of AGEs.


Parkinsonism-associated protein DJ-1 is a bona fide deglycase.
Biochem Biophys Res Commun.
 
2017 Jan 29;483(1):387-391.
Richarme G, Dairou J
DOI: 10.1016/j.bbrc.2016.12.134
PubMed publication date (edat): 12/26/2016

Abstract

We discovered recently that Parkinsonism-associated DJ-1 and its bacterial homologs function as protein deglycases that repair glyoxal- and methylglyoxal-glycated proteins. Protein glycation levels are 2- to 10-fold increased in deglycase-depleted cells, and deglycase mutants display up to 500-fold loss of viability in methylglyoxal or glucose-containing media, suggesting that these deglycases play important roles in protecting cells against electrophile and carbonyl stress. Although the deglycase activity of DJ-1 is well supported by extensive biochemical work, Pfaff et al….claimed in a recent study that deglycation of the hemithioacetal formed upon cysteine glycation by methylglyoxal results from a Tris buffer artefact. Here, we show that this is not the case, and that DJ-1 and its homologs are the bona fide deglycases awaited since the Maillard discovery.

PMID: 28013050
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Maximus Peto

Max Peto is a longevity researcher and founder of Long Life Labs. A biochemist by training, he studies the biochemistry of aging and longevity and has worked with research organizations such as SENS Research Foundation, Methuselah Foundation, BioAge Labs, Life Extension Foundation, and Ichor Therapeutics. His work at Long Life Labs is focused on empowering people to understand and manage the most critical factors for better health and longer life.

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