The α2,8-sialyltransferase 6 (St8sia6) localizes in the ER and enhances the anchorage-independent cell growth in cancer.

Cell Growth Processes Endoplasmic Reticulum / enzymology Gangliosides / metabolism Golgi Apparatus / metabolism Humans Neoplasms / metabolism Sialyltransferases / metabolism
Cancer Colony formation ER localization Sialyltransferase

Journal

Biochemical and biophysical research communications
ISSN: 1090-2104
Titre abrégé: Biochem Biophys Res Commun
Pays: United States
ID NLM: 0372516

Informations de publication

Date de publication:
11 06 2022
Historique:
received: 21 03 2022
accepted: 27 03 2022
pubmed: 8 4 2022
medline: 29 4 2022
entrez: 7 4 2022
Statut: ppublish

Résumé

Sialylation, the final stage of post-translational modification of proteins, is achieved in the Golgi apparatus and is related to the malignant phenotype of cancer. Disialylation of ganglioside (GD3) by St8sia1 and polysialylation by St8sia2 and 4 have been shown to be related to malignant phenotypes; however, di/oligosialylation by St8sia6 is still unknown. In this study, we analyzed the malignant phenotype of St8sia6 and found that upregulation of St8sia6 in melanoma B16 cells increased anchorage-independent cell growth, which was not due to sialic acid cleavage by a sialidase. Moreover, unlike other sialyltransferases, St8sia6 localized to the endoplasmic reticulum (ER). We found that the localization to the Golgi apparatus could be regulated by swapping experiments using St8sia2; however, the malignant phenotype did not change. These data demonstrate that the enhancement of anchorage-independent cell growth by St8sia6 is not due to its localization of ER, but is due to the expression of the protein itself.

Identifiants

DOI: 10.1016/j.bbrc.2022.03.146 PMID: 35390672
pubmed: 35390672
pii: S0006-291X(22)00491-0
doi: 10.1016/j.bbrc.2022.03.146
pii:
doi:

Substances chimiques

Gangliosides 0
Sialyltransferases EC 2.4.99.-
ST8SIA6 protein, human EC 3.4.99.-

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

52-58

Informations de copyright

Copyright © 2022 Elsevier Inc. All rights reserved.

Auteurs

Rina Hatanaka (R)

Bioscience and Biotechnology Center, Nagoya University, Chikusa, Nagoya, 464-8601, Japan; Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa, Nagoya, 464-8601, Japan.

Erino Araki (E)

Bioscience and Biotechnology Center, Nagoya University, Chikusa, Nagoya, 464-8601, Japan; Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa, Nagoya, 464-8601, Japan; Integrated Glyco-Biomedical Research Center (iGMED), Institute for Glyco-core Research (iGCORE), Nagoya University, Chikusa, Nagoya, 464-8601, Japan.

Masaya Hane (M)

Bioscience and Biotechnology Center, Nagoya University, Chikusa, Nagoya, 464-8601, Japan; Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa, Nagoya, 464-8601, Japan; Integrated Glyco-Biomedical Research Center (iGMED), Institute for Glyco-core Research (iGCORE), Nagoya University, Chikusa, Nagoya, 464-8601, Japan.

Shiori Go (S)

Bioscience and Biotechnology Center, Nagoya University, Chikusa, Nagoya, 464-8601, Japan; Integrated Glyco-Biomedical Research Center (iGMED), Institute for Glyco-core Research (iGCORE), Nagoya University, Chikusa, Nagoya, 464-8601, Japan.

Di Wu (D)

Bioscience and Biotechnology Center, Nagoya University, Chikusa, Nagoya, 464-8601, Japan; Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa, Nagoya, 464-8601, Japan; Integrated Glyco-Biomedical Research Center (iGMED), Institute for Glyco-core Research (iGCORE), Nagoya University, Chikusa, Nagoya, 464-8601, Japan.

Ken Kitajima (K)

Bioscience and Biotechnology Center, Nagoya University, Chikusa, Nagoya, 464-8601, Japan; Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa, Nagoya, 464-8601, Japan; Integrated Glyco-Biomedical Research Center (iGMED), Institute for Glyco-core Research (iGCORE), Nagoya University, Chikusa, Nagoya, 464-8601, Japan.

Chihiro Sato (C)

Bioscience and Biotechnology Center, Nagoya University, Chikusa, Nagoya, 464-8601, Japan; Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa, Nagoya, 464-8601, Japan; Integrated Glyco-Biomedical Research Center (iGMED), Institute for Glyco-core Research (iGCORE), Nagoya University, Chikusa, Nagoya, 464-8601, Japan. Electronic address: chi@agr.nagoya-u.ac.jp.

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Classifications MeSH

questionsmedicales.fr › Phénomènes physiologiques › Croissance et développement › Croissance › Processus de croissance cellulaire › The α2,8-sialyltransferase 6 (St8sia6)...
questionsmedicales.fr › Cellules › Structures cellulaires › Espace intracellulaire › Cytoplasme › Structures cytoplasmiques › Organites › Réticulum endoplasmique › The α2,8-sialyltransferase 6 (St8sia6)...
questionsmedicales.fr › Lipides › Lipides membranaires › Sphingolipides › Glycosphingolipides › Glycosphingolipides acides › Gangliosides › The α2,8-sialyltransferase 6 (St8sia6)...
questionsmedicales.fr › Cellules › Structures cellulaires › Espace intracellulaire › Cytoplasme › Structures cytoplasmiques › Organites › Appareil de Golgi › The α2,8-sialyltransferase 6 (St8sia6)...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › The α2,8-sialyltransferase 6 (St8sia6)...
questionsmedicales.fr › Tumeurs › The α2,8-sialyltransferase 6 (St8sia6)...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Transferases › Glycosyltransferase › Sialyltransferases › The α2,8-sialyltransferase 6 (St8sia6)...