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Magnesium-dependent phosphatase-1 is a protein-fructosamine-6-phosphatase potentially involved in glycation repair.

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Fortpied, Juliette [UCL] Maliekal, Pushpa [UCL] Vertommen, Didier [UCL] Van Schaftingen, Emile [UCL]

Fructosamine-3-kinase (FN3K) is a recently described protein-repair enzyme responsible for the removal of fructosamines, which are the products of a spontaneous reaction of glucose with amines. We show here that, compared with glucose, glucose 6-phosphate (Glu-6-P) reacted 3-6-fold more rapidly with proteins and 8-fold more rapidly with N-alpha-t-Boc-lysine, being therefore a more significant intracellular glycating agent than glucose in skeletal muscle and heart. Fructosamine 6-phosphates, which result from the reaction of amines with Glu-6-P, were not substrates for FN3K. However, a phosphatase that dephosphorylates protein-bound fructosamine 6-phosphates was found to be present in rat tissues. This enzyme was purified to near homogeneity from skeletal muscle and was identified as magnesium-dependent phosphatase-1 (MDP-1), an enzyme of the haloacid dehalogenase family with a putative protein-tyrosine phosphatase function. Human recombinant MDP-1 acted on protein-bound fructosamine 6-phosphates with a catalytic efficiency >10-fold higher than those observed with its next best substrates (arabinose 5-phosphate and free fructoselysine 6-phosphate) and >100-fold higher than with protein-phosphotyrosine. It had no detectable activity on fructosamine 3-phosphates. MDP-1 dephosphorylated up to approximately 75% of the fructosamine 6-phosphates that are present on lysozyme after incubation of this protein with Glu-6-P. Furthermore, lysozyme glycated with Glu-6-P was converted by MDP-1 to a substrate for FN3K. We conclude that MDP-1 may act physiologically in conjunction with FN3K to free proteins from the glycation products derived from Glu-6-P.

Document type Article de périodique (Journal article) – Article de recherche
Access type Accès restreint
Publication date 2006
Journal information "The Journal of biological chemistry" - Vol. 281, no. 27, p. 18378-85 (2006)
Peer reviewed yes
issn 0021-9258
Publication status Publié
Affiliation UCL - MD/BICL - Département de biochimie et de biologie cellulaire
MESH Subject Amino Acid Sequence ; Animals ; Fructosamine - metabolism ; Glucose - metabolism ; Glucose-6-Phosphate - metabolism ; Humans ; Molecular Sequence Data ; Muscle, Skeletal - metabolism ; Myocardium - metabolism ; Organ Specificity ; Phosphoprotein Phosphatases - genetics - metabolism ; Phosphotransferases (Alcohol Group Acceptor) - genetics - metabolism ; Protein Phosphatase 1 ; Rats ; Recombinant Proteins - genetics - metabolism ; Substrate Specificity
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Bibliographic reference Fortpied, Juliette ; Maliekal, Pushpa ; Vertommen, Didier ; Van Schaftingen, Emile. Magnesium-dependent phosphatase-1 is a protein-fructosamine-6-phosphatase potentially involved in glycation repair.. In: The Journal of biological chemistry, Vol. 281, no. 27, p. 18378-85 (2006)
Permanent URL http://hdl.handle.net/2078.1/21967