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ID 117824
Title Alternative
Nonspecific phospholipase C3 of radish has phospholipase D activity toward glycosylinositol phosphoceramide
Author
Hasi, Rumana Yesmin Tokushima University
Ishikawa, Toshiki Saitama University
Sunagawa, Keigo Tokushima University
Takai, Yoshimichi Tokushima University
Ali, Hanif Tokushima University
Imai, Hiroyuki Konan University
Keywords
Glycosylinositol phosphoceramide
phospholipase D
phytoceramide 1-phosphate
nonspecific phospholipase C3
Raphanus sativus
Content Type
Journal Article
Description
Previously, we found an enzyme activity that produces phytoceramide 1-phosphate (PC1P) by hydrolysis of D position of glycosylinositol phosphoceramide (GIPC) in cabbage and called its activity as GIPC-phospholipase D (PLD). Here, we purified GIPC-PLD by sequential chromatography from radish roots. Peptide mass fingerprinting analysis revealed that the potential candidate for GIPC-PLD protein was nonspecific phospholipase C3 (NPC3), which has not been characterized as PLD. The recombinant NPC3 protein obtained by heterologous expression system with E. coli produced PC1P from GIPC, and showed essentially the same enzymatic properties as those we characterized as GIPC-PLD in cabbage, radish, and A. thaliana. From these results, we concluded that NPC3 is one of the enzymes that degrade GIPC, a major sphingolipid in plants.
Journal Title
FEBS Letters
ISSN
18733468
NCID
AA00642943
Publisher
Federation of European Biochemical Societies|Wiley
Volume
596
Issue
23
Start Page
3024
End Page
3036
Published Date
2022-10-20
Rights
This is the peer reviewed version of the following article: Hasi, R.Y., Ishikawa, T., Sunagawa, K., Takai, Y., Ali, H., Hayashi, J., Kawakami, R., Yuasa, K., Aihara, M., Kanemaru, K., Imai, H. and Tanaka, T. (2022), Nonspecific phospholipase C3 of radish has phospholipase D activity towards glycosylinositol phosphoceramide. FEBS Lett. 596: 3024-3036. which has been published in final form at https://doi.org/10.1002/1873-3468.14520. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions. This article may not be enhanced, enriched or otherwise transformed into a derivative work, without express permission from Wiley or by statutory rights under applicable legislation. Copyright notices must not be removed, obscured or modified. The article must be linked to Wiley’s version of record on Wiley Online Library and any embedding, framing or otherwise making available the article or pages thereof by third parties from platforms, services and websites other than Wiley Online Library must be prohibited.
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DOI (Published Version)
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language
eng
TextVersion
Author
departments
Bioscience and Bioindustry
Pharmaceutical Sciences