Analysis of hepatic glycogen-associated proteins

作者：Stapleton David; Nelson Chad; Parsawar Krishna; McClain Donald; Gilbert Wilson Ryan; Barker Elizabeth; Rudd Brant; Brown Kevin; Hendrix Wayne; O'Donnell Paul; Parker Glendon^*

来源：Proteomics, 2010, 10(12): 2320-2329.

DOI：10.1002/pmic.200900628

• Carbohydrate binding domains
• Cell biology
• Glucose metabolism
• Glycogen particle
• Starch binding domain protein 1
• Sub-cellular localization

Glycogen particles are associated with a population of proteins that mediate its biological functions, including: management of glucose flux into and out of the glycogen particle, maintenance of glycogen structure and regulation of particle size, number, and cellular location. A survey of the glycogen-associated proteome would be predicted to identify the relative representation of known members of this population, and associations with unexpected proteins that have the potential to mediate other functions of the glycogen particle. We therefore purified glycogen particles from both mouse and rat liver, using different techniques, and analyzed the resulting tryptic peptides by MS. We also specifically eluted glycogen-binding proteins from the pellet using malto-oligosaccharides. Comparison of the rat and mouse populations, and analysis of specifically eluted proteins allow some conclusions to be made about the hepatic glycogen sub-proteome. With the exception of glycogen branching enzyme all glycogen metabolic proteins were detected. Novel associations were identified, including ferritin and starch-binding domain protein 1, a protein that contains both a transmembrane endoplasmic reticulum signal peptide and a carbohydrate-binding module. This study therefore provides insight into the organization of the glycogen proteome, identifies other associated proteins and provides a starting point to explore the dynamic nature and cellular distribution of this metabolically important protein population.

• 出版日期2010-6