Professor Akira Kurosaka
■ Area and Subject Taught: Cell Biology
■ Research Theme(s): Functional Analysis of Glycosyltransferases in Neural Differentiation
■ Academic Degrees: Doctor of Pharmacology, Kyoto University
■ Keywords for Research Field: Neural Differentiation, Sugar Chains, Glycosyltransferases
[Research Overview]
The genome sequences of several important organisms have been determined, but functions of proteins encoded by the genome still remain to be elucidated. Polypeptide chains synthesized using the information of the genome sequences, in general, become functional proteins after having a range of posttranslational modifications, such as glycosylation. We have successfully cloned a brainspecific glycosyltransferase (Figure), which catalyzes the initial reaction of mucin-carbohydrate biosynthesis by transferring N-acethylgalactosamine to a hydroxyl amino acid in polypeptides. We have also found that the brain-specific isozyme is important for the development of neurons since its suppression gives rise to morphological abnormality and apoptotic cell death in the brain of zebrafish. It should be noted that this isozyme is found in the critical region of Williams-Beuren syndrome, an inheritable disease, which is characterized by metal retardation.
[Notable Publications and Works in the Last Three Years]
- Yamauchi K. and Kurosaka A. (2009) Inhibition of glycogen synthase kinase-3 enhances the expression of alkaline phosphatase and insulin-like growth factor-1 in human primary dermal papilla cell culture and maintains mouse hair bulbs in organ culture. Arch. Dermatol. Res, 301, 357-365.
- S., Takada, S., and Kurosaka, A. (2008) Studies on apoptosis caused by the suppression of UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase 16. ActaHumanistatica et Scientifica Universitatis Sangio Kyotiensis, 37, 59-70．
- M., Saeki, A., Elhammer, Å.P., and Kurosaka, A. (2007) Function of conserved aromatic residues in the Gal/GalNAc-glycosyltransferase motif of UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase 1. FEBS J., 274, 6037-6045.