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N-Glycosylation plays a role in protein folding of human UGT1A9
https://doi.org/10.24517/00015326
https://doi.org/10.24517/00015326c2f1196a-e8df-4649-a42f-78b68f2462c1
| 名前 / ファイル | ライセンス | アクション |
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PH-PR-NAKAJIMA-M-1165.pdf (592.9 kB)
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| Item type | 学術雑誌論文 / Journal Article(1) | |||||||
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| 公開日 | 2017-10-04 | |||||||
| タイトル | ||||||||
| タイトル | N-Glycosylation plays a role in protein folding of human UGT1A9 | |||||||
| 言語 | ||||||||
| 言語 | eng | |||||||
| 資源タイプ | ||||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||||
| 資源タイプ | journal article | |||||||
| ID登録 | ||||||||
| ID登録 | 10.24517/00015326 | |||||||
| ID登録タイプ | JaLC | |||||||
| 著者 |
Nakajima, Miki
× Nakajima, Miki× Koga, Toshihisa× Sakai, Haruko× Yamanaka, Hiroyuki× Fujiwara, Ryoichi× Yokoi, Tsuyoshi |
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| 著者別表示 |
中嶋, 美紀
× 中嶋, 美紀
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| 提供者所属 | ||||||||
| 内容記述タイプ | Other | |||||||
| 内容記述 | 金沢大学ナノ生命科学研究所 / 金沢大学医薬保健研究域薬学系 | |||||||
| 書誌情報 |
Biochemical Pharmacology 巻 79, 号 8, p. 1165-1172, 発行日 2010-04-01 |
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| ISSN | ||||||||
| 収録物識別子タイプ | ISSN | |||||||
| 収録物識別子 | 0006-2952 | |||||||
| NCID | ||||||||
| 収録物識別子タイプ | NCID | |||||||
| 収録物識別子 | AA00564486 | |||||||
| DOI | ||||||||
| 関連タイプ | isVersionOf | |||||||
| 識別子タイプ | DOI | |||||||
| 関連識別子 | 10.1016/j.bcp.2009.11.020 | |||||||
| 出版者 | ||||||||
| 出版者 | Elsevier | |||||||
| 抄録 | ||||||||
| 内容記述タイプ | Abstract | |||||||
| 内容記述 | UDP-glucuronosyltransferases (UGTs) catalyze the glucuronidation of a variety of xeno/endobiotics. UGTs are type I membrane proteins of the endoplasmic reticulum (ER) with a glycosylated luminal domain. In the present study, we investigated the role of N-glycosylation in the function of human UGT1A9. Mutation analysis at the potential N-glycosylation sites at residues 71, 292, and 344 (from asparagine to glutamine) revealed that all of them were glycosylated, but the extent of glycosylation and/or size of the glycan differed. In comparison with the wild-type, these mutants showed decreased enzyme activities in parallel with the extent of the band shift in Western blot analysis. To evaluate the role of glycosylation in the enzyme activity, we produced unglycosylated UGT1A9 by treating HEK293 cells transiently transfected with expression plasmid with tunicamycin. The unglycosylated UGT1A9 was almost inactive, which was not an indirect effect of ER stress. To the contrary, the deglycosylated UGT1A9, which was produced by the treatment with Endo H under the non-denaturing condition, showed the same enzyme kinetics as the control. These results suggest that the glycosylation that occurs during translation is important for the folding of UGT1A9. The thermal stability analysis of the mutated and deglycosylated UGT1A9 proteins supported the findings. In conclusion, we found that the N-glycosylation has an important role in the folding of UGT1A9. © 2009 Elsevier Inc. | |||||||
| 著者版フラグ | ||||||||
| 出版タイプ | AM | |||||||
| 出版タイプResource | http://purl.org/coar/version/c_ab4af688f83e57aa | |||||||
| 関連URI | ||||||||
| 識別子タイプ | URI | |||||||
| 関連識別子 | http://www.elsevier.com/locate/issn/00062952 | |||||||
