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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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Detalles Bibliográficos
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
Descripción
Sumario:[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.