Abstract |
Oridonin is a diterpenoid isolated from the Rabdosia rubescens and has multiple biological effects, such as anti- inflammation and anti- tumor activities. In present study, we revealed that the sensitizing effect of oridonin on tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced apoptosis in several cancer cells, but not in normal cells. Oridonin enhanced death-signaling inducing complexes (DISC) formation and DR5 glycosylation without affecting expression of downstream intracellular apoptosis-related proteins. Oridonin upregulated peptidyl O- glycosyltransferase GALNT14 in a dose- and time-dependent manner. Knockdown of GALNT14 by siRNA and Endo H treatment reduced oridonin-induced DR5 glycosylation. Furthermore, treatment with inhibitor of glycosylation (benzyl-α-GalNAc) blocked oridonin plus TRAIL-induced apoptosis. Collectively, our results suggest that oridonin-induced DR5 glycosylation contributes to TRAIL-induced apoptotic cell death in cancer cells.
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Authors | Mi-Yeon Jeon, Seung Un Seo, Seon Min Woo, Kyoung-Jin Min, Hee Sun Byun, Gang Min Hur, Sun Chul Kang, Taeg Kyu Kwon |
Journal | Biochimie
(Biochimie)
Vol. 165
Pg. 108-114
(Oct 2019)
ISSN: 1638-6183 [Electronic] France |
PMID | 31336136
(Publication Type: Journal Article)
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Copyright | Copyright © 2019 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM). All rights reserved. |
Chemical References |
- Apoptosis Regulatory Proteins
- Diterpenes, Kaurane
- Receptors, TNF-Related Apoptosis-Inducing Ligand
- TNF-Related Apoptosis-Inducing Ligand
- TNFRSF10B protein, human
- oridonin
- N-Acetylgalactosaminyltransferases
- UDP-N-acetyl-D-galactosamine polypeptide N-acetylgalactosaminyltransferase 14, human
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Topics |
- Apoptosis
(drug effects)
- Apoptosis Regulatory Proteins
(metabolism)
- Cell Line
- Diterpenes, Kaurane
(pharmacology)
- Glycosylation
- Humans
- N-Acetylgalactosaminyltransferases
(metabolism)
- Receptors, TNF-Related Apoptosis-Inducing Ligand
(metabolism)
- TNF-Related Apoptosis-Inducing Ligand
(pharmacology, physiology)
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