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

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Tytuł:: The α2,8-sialyltransferase 6 (St8sia6) localizes in the ER and enhances the anchorage-independent cell growth in cancer.
Autorzy:: 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.
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.
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.
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.
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.
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.
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: .
Źródło:: Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2022 Jun 11; Vol. 608, pp. 52-58. Date of Electronic Publication: 2022 Mar 28.
Typ publikacji:: Journal Article
Język:: English
Imprint Name(s):: Publication: <2002- >: San Diego, CA : Elsevier
Original Publication: New York, Academic Press.
MeSH Terms:: Endoplasmic Reticulum*/enzymology
Endoplasmic Reticulum*/metabolism
Neoplasms*/metabolism
Neoplasms*/pathology
Sialyltransferases*/metabolism
Cell Growth Processes ; Gangliosides/metabolism ; Golgi Apparatus/metabolism ; Humans
Contributed Indexing:: Keywords: Cancer; Colony formation; ER localization; Sialyltransferase
Substance Nomenclature:: 0 (Gangliosides)
EC 2.4.99.- (Sialyltransferases)
EC 3.4.99.- (ST8SIA6 protein, human)
Entry Date(s):: Date Created: 20220407 Date Completed: 20220428 Latest Revision: 20220531
Update Code:: 20240105
DOI:: 10.1016/j.bbrc.2022.03.146
PMID:: 35390672
: Czasopismo naukowe

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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.
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