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J. Biol. Chem., Vol. 279, Issue 45, 46606-46613, November 5, 2004

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Tissue Distribution and Evolution of Fructosamine 3-Kinase and Fructosamine 3-Kinase-related Protein^*

Jérôme Delplanque, Ghislain Delpierre¶, Fred R. Opperdoes||, and Emile Van Schaftingen**

From the Laboratory of Physiological Chemistry and the ^||Research Unit for Tropical Diseases, Christian de Duve Institute of Cellular Pathology and Université Catholique de Louvain, Avenue Hippocrate 75, B-1200 Brussels, Belgium

Fructosamine 3-kinase (FN3K) and FN3K-related protein (FN3K-RP) catalyze the phosphorylation of the Amadori products ribulosamines, psicosamines, and, in the case of FN3K, fructosamines. BLAST searches in chordate genomes revealed two genes encoding proteins homologous to FN3K or FN3K-RP in various mammals and in chicken but only one gene, encoding a protein more similar to FN3K-RP than to FN3K, in fishes and the sea squirt Ciona intestinalis. This suggests that a gene duplication event occurred after the fish radiation and that the FN3K gene evolved more rapidly than the FN3K-RP gene. In agreement with this distribution, only one enzyme, phosphorylating ribulosamines and psicosamines but not fructosamines, was found in the tissues from a fish (Clarias gariepinus), whereas two enzymes with specificities similar to either FN3K or FN3K-RP were found in mouse, rat, and chicken tissues. FN3K is particularly active in brain, heart, kidney, and skeletal muscle. Its activity is also relatively elevated in erythrocytes from man, rat, and mouse but barely detectable in erythrocytes from chicken and pig, which correlates well with the low intracellular concentration of glucose in erythrocytes from these species. This is in keeping with the specific role of FN3K to repair protein damage caused by glucose. FN3K-RP was more evenly distributed in tissues, except for skeletal muscle where its activity was particularly low. This may be related to low activity of the pentose phosphate pathway in this tissue, as suggested by assays of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase. This finding, together with the high affinity of FN3K-RP for ribulosamines, suggests that this enzyme may serve to repair damage caused by the powerful glycating agent, ribose 5-phosphate.

Received for publication, July 8, 2004 , and in revised form, August 24, 2004.

^* This work was supported by the Directorate General for Higher Education and Scientific Research, French Community of Belgium, the European Foundation for the Study of Diabetes, the Fund for Medical Scientific Research, and the Interuniversity Attraction Poles Programme-Belgian Science Policy. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Fellow of the Christian de Duve Institute of Cellular Pathology.

^¶ Chargé de Recherche of the Belgian Fonds National de la Recherche Scientifique.

^** To whom correspondence should be addressed: Laboratory of Physiological Chemistry, Avenue Hippocrate, 75, B-1200 Brussels, Belgium. Tel.: 32-2-764-75-64; Fax: 32-2-764-75-98; E-mail: vanschaftingen{at}bchm.ucl.ac.be.

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