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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...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2018
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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. |
format | Online Article Text |
id | pubmed-6045358 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
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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