Antibacterial Activity of l-5-Alkylthiomethylhydantoin-S-oxides |
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Authors: | Yuzo Miura Satoshi Hobara Satoshi Tahara Junya Mizutani |
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Institution: | Department of Agricultural Chemistry, Faculty of Agriculture, Hokkaido University, Sapporo |
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Abstract: | Cell-surface expression of the discoidin domain receptor (DDR) tyrosine kinase family in high molecular mass form was controlled sensitively by the glucose concentration through a post-translational N-glycosylation process. Cycloheximide time-course experiments revealed that the high-molecular-mass forms of DDR1 and DDR2 were significantly less stable than control receptor tyrosine kinases. Site-directed mutational analysis of the consensus N-glycosylation sites of the DDRs revealed that mutations of asparagine 213 of DDR2 and asparagine 211 of DDR1, a conserved N-glycosylation site among vertebrate DDRs, inhibited the generation of the high-molecular-mass isoform. Taken together, these results suggest a mechanism to control the activity of the DDR family by regulating its cell-surface expression. Due to low stability, the steady-state population of functional DDR proteins in the cell surface depends sensitively on its maturation process via post-translational N-glycosylation, which is controlled by the glucose supply and the presence of a conserved N-glycosylation site. |
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Keywords: | discoidin domain receptor glucose protein stability N-glycosylation asparagine |
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