Analysis of biochemical features of ST8 α-N-acetyl-neuraminide α2,8-sialyltransferase (St8sia) 5 isoforms.
Ganglioside, isoform
Melanoma
Sialic acid
Sialyltransferase
Journal
Glycoconjugate journal
ISSN: 1573-4986
Titre abrégé: Glycoconj J
Pays: United States
ID NLM: 8603310
Informations de publication
Date de publication:
04 2022
04 2022
Historique:
received:
15
10
2021
accepted:
08
12
2021
revised:
24
11
2021
pubmed:
5
1
2022
medline:
12
4
2022
entrez:
4
1
2022
Statut:
ppublish
Résumé
Gangliosides are important components of the membrane and are involved in many biological activities. St8sia5 is an α2,8-sialyltransferase involved in ganglioside synthesis, and has three isoforms. In this study, we analyzed the features of three isoforms, St8sia5-S, -M, and -L that had not been analyzed, and found that only St8sia5-L was localized in the Golgi, while the majority of St8sia5-M and -S were localized in the ER. The localization of Golgi of St8sia5 depended on the stem region. In addition, the incorporation of exogenous GD3 was upregulated only in St8sia5-L expressing cells. Taken together, the localization of St8sia5 is important for the activity of the enzyme.
Identifiants
pubmed: 34982351
doi: 10.1007/s10719-021-10034-8
pii: 10.1007/s10719-021-10034-8
doi:
Substances chimiques
Gangliosides
0
Protein Isoforms
0
Sialyltransferases
EC 2.4.99.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
291-302Informations de copyright
© 2021. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.
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