Molecular and metabolic aspects of lysosomal glycogen.

Abstract

The high molecular weight glycogen associated with the lysosomal compartment in glycogen storage disease type VIII is more resistant to degradation by proteinase than normal glycogen. The assembly of large glycogen particles on disulphide-linked protein backbones has been confirmed and the disulphide-reducing nature of the lysosome appears to confer an advantage in the amylolytic degradation of glycogen. Experiments utilising acarbose, a lysosomal (1----4)-alpha-D-glucosidase inhibitor, show that some blood glucose could arise in normal mammals from extra-hepatic tissue, by degradation of the glycogen in the lysosomal compartment.

• Authors: R Geddes, P Jeyarathan, J A Taylor
• Journal: Carbohydrate research (Carbohydr Res) Vol. 227 Pg. 339-49 (Apr 06 1992) ISSN: 0008-6215 [Print] Netherlands
• PMID: 1499032 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Blood Glucose
• Glycoside Hydrolase Inhibitors
• Lactates
• Pyruvates
• Trisaccharides
• Glycogen
• Phosphorylase Kinase
• Serine Endopeptidases
• Endopeptidase K
• Acarbose

Topics

• Acarbose
• Animals
• Blood Glucose (analysis)
• Disease Models, Animal
• Endopeptidase K
• Glycogen (metabolism)
• Glycogen Storage Disease Type VII (metabolism)
• Glycoside Hydrolase Inhibitors
• Lactates (blood)
• Lysosomes (drug effects, metabolism)
• Phosphorylase Kinase (deficiency)
• Pyruvates (blood)
• Rats
• Serine Endopeptidases (metabolism)
• Trisaccharides (pharmacology)