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Last update 08 May 2025

GYS2

Last update 08 May 2025

Basic Info

Synonyms

Glycogen [starch] synthase, liver, glycogen synthase 2, GYS2

Introduction

Glycogen synthase participates in the glycogen biosynthetic process along with glycogenin and glycogen branching enzyme. Extends the primer composed of a few glucose units formed by glycogenin by adding new glucose units to it. In this context, glycogen synthase transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan.

Drugs associated with GYS2

GYS2 siRNA(Dicerna Pharmaceuticals)

Target

GYS2

Mechanism

GYS2 inhibitors

Active Org.

University of Bonn

Originator Org.

Dicerna Pharmaceuticals, Inc.

Active Indication

acute leukemia

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

US11572562

Patent Mining

Target

GYS2

Mechanism-

Active Org.

Novo Nordisk A/S

Originator Org.

Novo Nordisk A/S

Active Indication

Congenital Disorders

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with GYS2

100 Translational Medicine associated with GYS2

0 Patents (Medical) associated with GYS2

184

Literatures (Medical) associated with GYS2

01 Apr 2025·Journal of Chromatography B

LC-HRMS profiling of Dendrobium huoshanense aqueous extract and its therapeutic effects on nonalcoholic fatty liver disease in mice through the TLR2-NF-κB and AMPK-SREBP1-SIRT1 signaling pathways

Article

Author: Ge, Xiyu ; Chen, Cunwu ; Yang, Li ; Huang, Ke ; Han, Bangxing ; Liu, Dong ; Lin, Qiyan ; Ma, Menghua ; Wang, Wei

Dendrobium huoshanense (DH) belongs to the Dendrobium genus of the Orchidaceae family and is a herbaceous plant that protects the liver and nourishes the Yin according to traditional Chinese Medicine (TCM) theory. This research aimed to determine the therapeutic effect and mechanisms of DH on a nonalcoholic fatty liver disease (NAFLD) mouse model and its chemical composition. For pharmacological research, the pathological damage and lipid accumulation in liver tissues were evaluated using HE and oil red staining, respectively. The differential proteins between the model and DHH groups were screened using 4D label-free quantitative proteomics, and the proteomic results were verified using Western blot. The potential mechanism was validated by metabolomic analysis. The main active ingredients in a DH aqueous extract were identified using UHPLC-Q Exactive HF HRMS. Pathological staining results showed that DH can reverse liver pathological damage and lipid accumulation in the NAFLD model. Quantitative proteomics revealed that the differential proteins were mainly associated with liver lipid deposition (LAL, AMPK, TM7SF2, SBCAD, and SIRT1), insulin resistance (GYS1, GYS2, PYGL, FoxO1, and PPAR-γ), and inflammation (TLR2 and MAPKAPK). Western blot verified the above-mentioned results. Metabolomic analysis also indicated that the DH aqueous extract ameliorated NAFLD in mice by affecting cholesterol metabolism and AMPK signaling pathway, proving its significant therapeutic effects on the NAFLD model. Sixty-five compounds were identified from DH aqueous extract by analyzing the precise molecular weight and MS/MS fragmentation pathway. The pharmacological mechanism of DH in treating NAFLD mainly involved the TLR2-NF-κB and AMPK-SREBP1-SIRT1 signaling pathways.

01 Apr 2025·Clinical and Translational Medicine

Skeletal muscle effects of antisense oligonucleotides targeting glycogen synthase 1 in a mouse model of Pompe disease

Article

Author: Yin, Hong ; Grossman, Tamar R ; Lee, Jonathan ; Paguio, Marvin ; Kimonis, Virginia ; Fazeli, Yasamin ; Chang, Mindy ; Pal, Pallabi ; Raben, Nina ; Yu, Howard ; Ta, Lac ; Shmara, Alyaa ; Carrer, Michele ; Weiss, John ; Jafar‐Nejad, Paymaan ; Martin, Angela ; Cheng, Cheng ; Weiss, Lan ; Boock, Victoria

AbstractPompe disease (PD) is a progressive myopathy caused by the aberrant accumulation of glycogen in skeletal and cardiac muscle resulting from the deficiency of the enzyme acid alpha‐glucosidase (GAA). Administration of recombinant human GAA as enzyme replacement therapy (ERT) works well in alleviating the cardiac manifestations of PD but loses sustained benefit in ameliorating the skeletal muscle pathology. The limited efficacy of ERT in skeletal muscle is partially attributable to its inability to curb the accumulation of new glycogen produced by the muscle enzyme glycogen synthase 1 (GYS1). Substrate reduction therapies aimed at knocking down GYS1 expression represent a promising avenue to improve Pompe myopathy. However, finding specific inhibitors for GYS1 is challenging given the presence of the highly homologous GYS2 in the liver. Antisense oligonucleotides (ASOs) are chemically modified oligomers that hybridise to their complementary target RNA to induce their degradation with exquisite specificity. In the present study, we show that ASO‐mediated Gys1 knockdown in the Gaa−/− mouse model of PD led to a robust reduction in glycogen accumulation in skeletal muscle. In addition, combining Gys1 ASO with ERT slightly further reduced glycogen content in muscle, eliminated autophagic buildup and lysosomal dysfunction, and improved motor function in Gaa−/− mice. Our results provide a strong foundation for validation of the use of Gys1 ASO, alone or in combination with ERT, as a therapy for PD. We propose that early administration of Gys1 ASO in combination with ERT may be the key to preventative treatment options in PD.Key points

Antisense oligonucleotide (ASO) treatment in a mouse model of Pompe disease achieves robust knockdown of glycogen synthase (GYS1).

ASO treatment reduces glycogen content in skeletal muscle.

Combination of ASO and enzyme replacement therapy (ERT) further improves motor performance compared to ASO alone in a mouse model of Pompe disease.

16 Dec 2024·Animal Biotechnology

Single nucleotide polymorphisms of GYS2 gene and its association with milk production traits of dairy cows

Article

Author: Han, Bo ; Chen, Ao ; Sun, Dongxiao ; Xu, Lingna ; Ye, Wen

Glycogen synthase 2 (GYS2) encodes liver glycogen synthase, a rate limiting enzyme in glycogen metabolism. Our preliminary work suggested that GYS2 was a candidate gene affecting milk production traits by analyzing the liver proteome of dairy cows. Herein, this research identified single nucleotide polymorphisms (SNPs) of GYS2, analyzed their genetic effects on traits of dairy cattle, and speculated the pathogenic mechanism through functional prediction of key mutation sites. Seven SNPs were found by resequencing and the association analysis showed that these SNPs were significantly associated with 305-day milk yield, fat yield, protein yield or fat percentage (p-value ≤ 0.0488). Six SNPs among them formed two haplotype blocks and they were associated with 305-day milk yield, fat yield, protein yield or fat percentage (p-value ≤ 0.0349). Furthermore, 5:g.88602007G > A and 5:g.88602026G > A were predicted to change the transcription factor binding sites (TFBSs), which might regulate the expression of GYS2. The missense mutation site, 5:g.88602535G > T, changed the secondary structure of mRNA and the secondary and tertiary structure of protein. In summary, the GYS2 was proved to have genetic effect on milk production traits, and its valuable seven SNPs, could provide more useful genetic information for molecular breeding of dairy cows.

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GYS2

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