REVIEW: Spatial Structure of Glycogen Molecules in Cells

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N. N. Bezborodkina^1,a*, A. Yu. Chestnova¹, M. L. Vorobev¹, and B. N. Kudryavtsev¹

¹Institute of Cytology, Russian Academy of Sciences, 194064 St. Petersburg, Russia

^* To whom correspondence should be addressed.

Received October 16, 2017; Revision received November 9, 2017

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Glycogen is a strongly branched polymer of α-D-glucose, with glucose residues in the linear chains linked by 1→4-bonds (~93% of the total number of bonds) and with branching after every 4-8 residues formed by 1→6-glycosidic bonds (~7% of the total number of bonds). It is thought currently that a fully formed glycogen molecule (β-particle) with the self-glycosylating protein glycogenin in the center has a spherical shape with diameter of ~42 nm and contains ~ 55,000 glucose residues. The glycogen molecule also includes numerous proteins involved in its synthesis and degradation, as well as proteins performing a carcass function. However, the type and force of bonds connecting these proteins to the polysaccharide moiety of glycogen are significantly different. This review presents the available data on the spatial structure of the glycogen molecule and its changes under various physiological and pathological conditions.

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KEY WORDS: glycogen molecule, α-particles, β-particles, polysaccharide–protein complex, glycogen fractions, liver, skeletal muscles

DOI: 10.1134/S0006297918050012

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