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Proteomic Investigation of the Binding Agent between Liver Glycogen β Particles

[Image: see text] 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 (∼20 nm diamet...

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Autores principales: Tan, Xinle, Sullivan, Mitchell A., Nada, Sharif S., Deng, Bin, Schulz, Benjamin L., Gilbert, Robert G.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2018
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6045358/
https://www.ncbi.nlm.nih.gov/pubmed/30023874
http://dx.doi.org/10.1021/acsomega.8b00119
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author Tan, Xinle
Sullivan, Mitchell A.
Nada, Sharif S.
Deng, Bin
Schulz, Benjamin L.
Gilbert, Robert G.
author_facet Tan, Xinle
Sullivan, Mitchell A.
Nada, Sharif S.
Deng, Bin
Schulz, Benjamin L.
Gilbert, Robert G.
author_sort Tan, Xinle
collection PubMed
description [Image: see text] 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 (∼20 nm diameter) glycogen β particles with a dimer of glycogenin at their core. In the liver, glycogen is also found in the form of α particles: large bound composites of many β 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 β particles together into α particles.
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spelling pubmed-60453582018-07-16 Proteomic Investigation of the Binding Agent between Liver Glycogen β Particles Tan, Xinle Sullivan, Mitchell A. Nada, Sharif S. Deng, Bin Schulz, Benjamin L. Gilbert, Robert G. ACS Omega [Image: see text] 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 (∼20 nm diameter) glycogen β particles with a dimer of glycogenin at their core. In the liver, glycogen is also found in the form of α particles: large bound composites of many β 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 β particles together into α particles. American Chemical Society 2018-04-02 /pmc/articles/PMC6045358/ /pubmed/30023874 http://dx.doi.org/10.1021/acsomega.8b00119 Text en Copyright © 2018 American Chemical Society This is an open access article published under an ACS AuthorChoice License (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) , which permits copying and redistribution of the article or any adaptations for non-commercial purposes.
spellingShingle Tan, Xinle
Sullivan, Mitchell A.
Nada, Sharif S.
Deng, Bin
Schulz, Benjamin L.
Gilbert, Robert G.
Proteomic Investigation of the Binding Agent between Liver Glycogen β Particles
title Proteomic Investigation of the Binding Agent between Liver Glycogen β Particles
title_full Proteomic Investigation of the Binding Agent between Liver Glycogen β Particles
title_fullStr Proteomic Investigation of the Binding Agent between Liver Glycogen β Particles
title_full_unstemmed Proteomic Investigation of the Binding Agent between Liver Glycogen β Particles
title_short Proteomic Investigation of the Binding Agent between Liver Glycogen β Particles
title_sort proteomic investigation of the binding agent between liver glycogen β particles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6045358/
https://www.ncbi.nlm.nih.gov/pubmed/30023874
http://dx.doi.org/10.1021/acsomega.8b00119
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