論文 - 詳細
| RRC ID | 58962 |
|---|---|
| 著者 | Miura K, Hakamata W, Tanaka A, Hirano T, Nishio T. |
| タイトル | Discovery of human Golgi β-galactosidase with no identified glycosidase using a QMC substrate design platform for exo-glycosidase. |
| ジャーナル | Bioorg Med Chem |
| Abstract |
Post-translational modifications (PTMs) of proteins play important roles in the physiology of eukaryotes. In the PTMs, non-reversible glycosylations are classified as N-glycosylations and O-glycosylations, and are catalyzed by various glycosidases and glycosyltransferases. However, β-glycosidases are not known to play a role in N- and O-glycan processing, although both glycans provide partial structures as substrates for β-galactosidase and β-N-acetylglucosaminidase in the Golgi apparatus of human cells. We explored human Golgi β-galactosidase using fluorescent substrates based on a quinone methide cleavage (QMC) substrate design platform that was previously developed to image exo-type glycosidases in living cells. As a result, we discovered a novel Golgi β-galactosidase in human cells. It is possible to predict a novel and important function in glycan processing of this β-galactosidase, because various β-galactosyl linkages in N- and O-glycans exist in Golgi apparatus. In addition, these results show that the QMC platform is excellent for imaging exo-type glycosidases. |
| 巻・号 | 24(6) |
| ページ | 1369-75 |
| 公開日 | 2016-3-15 |
| DOI | 10.1016/j.bmc.2016.02.010 |
| PII | S0968-0896(16)30090-6 |
| PMID | 26875935 |
| MeSH | Cell Line, Tumor Fluorescence Glycoside Hydrolases / chemistry Glycoside Hydrolases / metabolism* Golgi Apparatus / enzymology* HeLa Cells Humans Indolequinones / chemistry Indolequinones / metabolism* Molecular Structure beta-Galactosidase / chemistry* beta-Galactosidase / metabolism* |
| IF | 3.073 |
| 引用数 | 3 |
| オルトメトリクス指標 |
オルトメトリクス指標項目
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| 最多言及媒体 | Patent(IFI CLAIMS) |
| 各媒体での言及数の合計 | 5 |
| 過去6か月間でのオルトメトリクス指標の変動値 | 0.0 |
| リソース情報 | |
| ヒト・動物細胞 | HeLa(RCB0007) SK-N-SH(RCB0426) |