Molecular insights into glycogen alpha-particle formation

Sullivan, Mitchell A., O'Connor, Mitchell J., Umana, Felipe, Roura, Eugeni, Jack, Kevin, Stapleton, David I. and Gilbert, Robert G. (2012) Molecular insights into glycogen alpha-particle formation. Biomacromolecules, 13 11: 3805-3813. doi:10.1021/bm3012727


Author Sullivan, Mitchell A.
O'Connor, Mitchell J.
Umana, Felipe
Roura, Eugeni
Jack, Kevin
Stapleton, David I.
Gilbert, Robert G.
Title Molecular insights into glycogen alpha-particle formation
Formatted title
Molecular insights into glycogen α-particle formation
Journal name Biomacromolecules   Check publisher's open access policy
ISSN 1525-7797
1526-4602
Publication date 2012-11-01
Year available 2012
Sub-type Article (original research)
DOI 10.1021/bm3012727
Open Access Status DOI
Volume 13
Issue 11
Start page 3805
End page 3813
Total pages 9
Place of publication Washington, DC, United States
Publisher American Chemical Society
Language eng
Abstract Glycogen, a hyperbranched complex glucose polymer, is an intracellular glucose store that provides energy for cellular functions, with liver glycogen involved in blood glucose regulation. Liver glycogen comprises complex alpha particles made up of smaller beta particles. The recent discovery that these alpha particles are and fewer. in diabetic, compared: with healthy, mice highlights the need to elucidate the nature of alpha-particle formation, this paper,tests various possibilities for binding within alpha particles. Acid hydrolysis effects, examined using dynamic light scattering and size exclusion.chromatography, showed that the binding is not simple alpha-(1 -> 4) or alpha-(1 -> 6) glycosidic linkages. There was no, significant :change in alpha particle size after the addition of various reagents, Which. disrupt disulfide, protein, and hydrogen bonds and hydrophobic interactions. The results are consistent with proteinaceous binding between beta particles in alpha particles, with the inability Of. protease to break apart particles being attributed to steric. hindrance.
Formatted abstract
Glycogen, a hyperbranched complex glucose polymer, is an intracellular glucose store that provides energy for cellular functions, with liver glycogen involved in blood glucose regulation. Liver glycogen comprises complex α particles made up of smaller β particles. The recent discovery that these α particles are smaller and fewer in diabetic, compared with healthy, mice highlights the need to elucidate the nature of α-particle formation; this paper tests various possibilities for binding within α particles. Acid  hydrolysis effects, examined using dynamic light scattering and size exclusion  chromatography, showed that the binding is not simple α-(1→4) or α-(1→6) glycosidic  linkages. There was no significant change in α particle size after the addition of  various reagents, which disrupt disulfide, protein, and hydrogen bonds and  hydrophobic interactions. The results are consistent with proteinaceous binding  between β particles in α particles, with the inability of protease to break apart particles  being attributed to steric hindrance.
Keyword Light-Scattering
Acid-Hydrolysis
H-1-Nmr Spectroscopy
Physical Constraints
Size Distributions
Muscle Glycogen
Beta-Particles
Liver-Glycogen
Starch
Macromolecules
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

 
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