Journal article
The fragility of liver glycogen from humans with type 2 diabetes: A pilot study
International Journal of Biological Macromolecules, Vol.221, pp.83-90
2022
PMID: 36075306
Abstract
Liver glycogen is a highly branched glucose polymer found as β particles (~20 nm in diameter), which can bind together into larger composite α particles. Hepatic α particles have been shown to be structurally fragile (breaking up into smaller particles in certain solvents) in mouse models of diabetes; if occurring in vivo, the resulting small glycogen particles could exacerbate the poor blood-sugar homeostasis characteristic of the disease. Here we tested if this α-particle fragility also occurred in liver glycogen obtained from humans with diabetes. It was found that liver glycogen from diabetic humans was indeed more fragile than from non-diabetic humans, which was also seen in the mouse experiments we ran in parallel. Proteomic analysis revealed three candidate proteins from differentially expressed glycogen proteins (Diabetes/ Non-diabetes) in both human and mouse groups. Identifying these proteins may give clues to the binding mechanism that holds together α particles together, which, being different in diabetic glycogen, is relevant to diabetes prevention and management.
Details
- Title
- The fragility of liver glycogen from humans with type 2 diabetes: A pilot study
- Authors
- Ziyi Wang - University of QueenslandXiaobo Min - Huazhong University of Science and TechnologyZhenxia Hu - Wuhan UniversityMitchell A Sullivan - University of QueenslandYong Tang - Huazhong University of Science and TechnologyLiang Wang - Xuzhou Medical CollegeRobert G Gilbert - University of QueenslandChen Shi (Corresponding Author) - Huazhong University of Science and TechnologyBin Deng (Corresponding Author) - Huazhong University of Science and Technology
- Publication details
- International Journal of Biological Macromolecules, Vol.221, pp.83-90
- Publisher
- Elsevier BV
- Date published
- 2022
- DOI
- 10.1016/j.ijbiomac.2022.08.212
- ISSN
- 1879-0003
- PMID
- 36075306
- Organisation Unit
- School of Health - Biomedicine
- Language
- English
- Record Identifier
- 991035093302621
- Output Type
- Journal article
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- Domestic collaboration
- International collaboration
- Web Of Science research areas
- Biochemistry & Molecular Biology
- Chemistry, Applied
- Polymer Science
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