Proteomic Investigation of the Binding Agent between Liver Glycogen β Particles

Xinle Tan; Mitchell A Sullivan; Sharif S. Nada; Bin Deng; Benjamin L Schulz; Robert G. Gilbert

doi:10.1021/acsomega.8b00119

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Proteomic Investigation of the Binding Agent between Liver Glycogen β Particles

Journal article

Open access

Peer reviewed

Proteomic Investigation of the Binding Agent between Liver Glycogen β Particles

Xinle Tan, Mitchell A Sullivan, Sharif S. Nada, Bin Deng, Benjamin L Schulz and Robert G. Gilbert

ACS Omega, Vol.3(4), pp.3640-3645

2018

DOI: https://doi.org/10.1021/acsomega.8b00119

PMID: 30023874

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Abstract

Glycogen is a highly branched glucose polymer which plays an important role in glucose storage and the maintenance of blood sugar homeostasis. The dimeric protein glycogenin can self-glucosylate to act as a primer for glycogen synthesis, eventually resulting in small (similar to 20 nm diameter) glycogen beta particles with a dimer of glycogenin at their core. In the liver, glycogen is also found in the form of a particles: large bound composites of many beta particles. Here, we provide evidence using qualitative and quantitative proteomics and size-exclusion chromatography from healthy rat, mouse, and human liver glycogen that glycogenin is the binding agent linking beta particles together into alpha particles.

Details

Title: Proteomic Investigation of the Binding Agent between Liver Glycogen β Particles
Authors: Xinle Tan - Yangzhou University
Mitchell A Sullivan - Translational Research Institute
Sharif S. Nada - The University of Queensland
Bin Deng - Huazhong University of Science and Technology
Benjamin L Schulz (Corresponding Author) - The University of Queensland
Robert G. Gilbert (Corresponding Author) - Yangzhou University
Publication details: ACS Omega, Vol.3(4), pp.3640-3645
Publisher: American Chemical Society
Date published: 2018
DOI: 10.1021/acsomega.8b00119
ISSN: 2470-1343
PMID: 30023874
Copyright note: This is an open access article published under an ACS AuthorChoice License, which permitscopying and redistribution of the article or any adaptations for non-commercial purposes.
Organisation Unit: School of Health - Biomedicine
Language: English
Record Identifier: 991035096502621
Output Type: Journal article

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Collaboration types: Domestic collaboration; International collaboration
Web Of Science research areas: Chemistry, Multidisciplinary

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