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Journal of Zhejiang University SCIENCE B 1998 Vol.-1 No.-1 P.

http://doi.org/10.1631/jzus.B2300917


Sialyltransferase ST3GAL6 silencing reduces α2,3-sialylated glycans to regulate autophagy by decreasing HSPB8-BAG3 in the brain with hepatic encephalopathy


Author(s):  Xiaocheng LI, Yaqing XIAO, Pengfei LI, Yayun ZHU, Yonghong GUO, Huijie BIAN, Zheng LI

Affiliation(s):  Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi’ more

Corresponding email(s):   zhengli@nwu.edu.cn, hjbian@fmmu.edu.cn, 276817684@qq.com

Key Words:  Hepatic encephalopathy, Hyperammonemia, Autophagy, ST3GAL6, HSPB8


Xiaocheng LI, Yaqing XIAO, Pengfei LI, Yayun ZHU, Yonghong GUO, Huijie BIAN, Zheng LI. Sialyltransferase ST3GAL6 silencing reduces α2,3-sialylated glycans to regulate autophagy by decreasing HSPB8-BAG3 in the brain with hepatic encephalopathy[J]. Journal of Zhejiang University Science B, 1998, -1(-1): .

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%T Sialyltransferase ST3GAL6 silencing reduces α2,3-sialylated glycans to regulate autophagy by decreasing HSPB8-BAG3 in the brain with hepatic encephalopathy
%A Xiaocheng LI
%A Yaqing XIAO
%A Pengfei LI
%A Yayun ZHU
%A Yonghong GUO
%A Huijie BIAN
%A Zheng LI
%J Journal of Zhejiang University SCIENCE B
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A1 - Pengfei LI
A1 - Yayun ZHU
A1 - Yonghong GUO
A1 - Huijie BIAN
A1 - Zheng LI
J0 - Journal of Zhejiang University Science B
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DOI - 10.1631/jzus.B2300917


Abstract: 
End-stage liver diseases, such as cirrhosis and liver cancer caused by hepatitis B, are often combined with hepatic encephalopathy (HE); ammonia poisoning is posited as one of its main pathogenesis mechanisms. Ammonia is closely related to autophagy, but the molecular mechanism of ammonia's regulatory effect on autophagy in HE remains unclear. Sialylation is an essential form of glycosylation. In the nervous system, abnormal sialylation affects various physiological processes, such as neural development and synapse formation. St3 beta-galactoside alpha-2,3-sialyltransferase 6 (ST3GAL6) is one of the significant glycosyltransferases responsible for adding α2,3-linked sialic acid to substrates and generating glycan structures. We found that the expression of ST3GAL6 was upregulated in the brains of mice with HE and in astrocytes after ammonia induction, and the expression of α2,3-sialylated glycans and autophagy-related proteins microtubule-associated protein light chain 3 (LC3) and Beclin-1 were upregulated in ammonia-induced astrocytes. These findings suggest that ST3GAL6 is related to autophagy in HE. Therefore, we aimed to determine the regulatory relationship between ST3GAL6 and autophagy. We found that silencing ST3GAL6 and blocking or degrading α2,3-sialylated glycans by way of Maackia Amurensis lectin-II (MAL-II) and neuraminidase can inhibit autophagy. In addition, silencing the expression of ST3GAL6 can downregulate the expression of heat shock protein beta 8 (HSPB8) and bcl2-associated athanogene 3 (BAG3). Notably, the overexpression of HSPB8 partially restored the reduced autophagy levels caused by silencing ST3GAL6 expression. Our results indicate that STGAL6 regulates autophagy through the HSPB8-BAG3 complex.

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