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Although activating mutations of fibroblast growth factor receptor 3 (FGFR3) are frequent in bladder tumors, little information is available on their specific effects in urothelial cells or the basis for the observed mutation spectrum. We investigated the phenotypic and signaling consequences of three FGFR3 mutations (S249C, Y375C, and K652E) in(More)
Known glycoproteins were used to determine the differences occurring in the binding specificities of the three variants of the K88 lectin in an approach essentially based on lectin blotting. During the screening, it was demonstrated that each variant of the K88 lectin biotinylated via its amino groups (NbioK88) exhibited a characteristic binding to the(More)
After the demonstration that neither N-glycans nor neuraminic acid are involved in the binding of K88 lectins to the B beta and gamma chains of porcine fibrinogen and that their recognition was due to O-glycans (L'Hôte C, Berger S, Bourgerie S, Duval-Ifiah Y, Julien R, Karamanos Y. Infect Immun 1995; 63: 1927-1932) it clearly appeared that these lectins(More)
A monoester lipase (MEL) activity (EC 3.1.1.3) is described in human red blood cells (RBC). The lipase acts as a cell-bound enzyme and is able to exert its catalytic activity in vitro toward an exogenously added emulsified substrate. The enzyme activity, which appears to be confined to the cell membrane, is inhibited by Triton X-100. The MEL activity of(More)
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