Dataset Information

Protein lysine modification by a 3-hydroxy-2,5-hexanedione probe and LC-MS/MS detection

ABSTRACT: Protein lysine modification in human plasma by a 3-hydroxy-2,5-hexanedione probe and LC-MS/MS detection of binding sites.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Blood Plasma

SUBMITTER: Johan Palmfeldt

LAB HEAD: Johan Palmfeldt

PROVIDER: PXD006663 | Pride | 2017-08-22

REPOSITORIES: Pride

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Publications

Ketone Body Acetoacetate Buffers Methylglyoxal via a Non-enzymatic Conversion during Diabetic and Dietary Ketosis.

Salomón Trine T Sibbersen Christian C Hansen Jakob J Britz Dieter D Svart Mads Vandsted MV Voss Thomas Schmidt TS Møller Niels N Gregersen Niels N Jørgensen Karl Anker KA Palmfeldt Johan J Poulsen Thomas Bjørnskov TB Johannsen Mogens M

Cell chemical biology 20170801 8

The α-oxoaldehyde methylglyoxal is a ubiquitous and highly reactive metabolite known to be involved in aging- and diabetes-related diseases. If not detoxified by the endogenous glyoxalase system, it exerts its detrimental effects primarily by reacting with biopolymers such as DNA and proteins. We now demonstrate that during ketosis, another metabolic route is operative via direct non-enzymatic aldol reaction between methylglyoxal and the ketone body acetoacetate, leading to 3-hydroxyhexane-2,5-d ...[more]

PMID: 28820963

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