Evidence against a role for the parkinsonism-associated protein DJ-1 in methylglyoxal detoxification

• Verfasst von: Pfaff, Daniel [VerfasserIn]
• Verfasst von: Fleming, Thomas [VerfasserIn]
• Verfasst von: Nawroth, Peter Paul [VerfasserIn]
• Verfasst von: Teleman, Aurelio A. [VerfasserIn]
• Titel: Evidence against a role for the parkinsonism-associated protein DJ-1 in methylglyoxal detoxification
• Verf.angabe: Daniel H. Pfaff, Thomas Fleming, Peter Nawroth and Aurelio A. Teleman
• Jahr: 2017
• Jahr des Originals: 2016
• Umfang: 6 S.
• Fussnoten: Published November 30, 2016 ; Gesehen am 22.08.2018
• Titel Quelle: Enthalten in: The journal of biological chemistry
• Ort Quelle: Bethesda, Md. : Soc., 1905
• Jahr Quelle: 2017
• Band/Heft Quelle: 292(2017), 2, Seite 685-690
• ISSN Quelle: 1083-351X
• DOI: doi:10.1074/jbc.M116.743823
• Datenträger: Online-Ressource
• Sprache: eng
• Bibliogr. Hinweis: Kommentar in: Pfaff, Daniel, 1984 - : Reply to Richarme: Evidence against a role of DJ-1 in methylglyoxal detoxification
• Sach-SW: development
• Sach-SW: Drosophila
• Sach-SW: glucose metabolism
• Sach-SW: glycation
• Sach-SW: metabolism
• K10plus-PPN: 1580304419

Abstract

Methylglyoxal (MG) is a reactive metabolite that forms adducts on cysteine, lysine and arginine residues of proteins, thereby affecting their function. Methylglyoxal is detoxified by the Glyoxalase system, consisting of two enzymes, Glo1 and Glo2, that act sequentially to convert MG into d-lactate. Recently, the Parkinsonism-associated protein DJ-1 was described in vitro to have glyoxalase activity, thereby detoxifying the MG metabolite, or deglycase activity, thereby removing the adduct formed by MG on proteins. Since Drosophila is an established model system to study signaling, neurodegeneration, and metabolic regulation in vivo, we asked whether DJ-1 contributes to MG detoxification in vivo. Using both DJ-1 knockdown in Drosophila cells in culture, and DJ-1β knock-out flies, we could detect no contribution of DJ-1 to survival to MG challenge or to accumulation of MG protein adducts. Furthermore, we provide data suggesting that the previously reported deglycation activity of DJ-1 can be ascribed to a TRIS buffer artifact.