The Action of Recombinant Human Lysosomal α-Glucosidase (rhGAA) on Human Liver Glycogen: Pathway to Complete Degradation

Glycogen is present in all tissues, but it primarily stored the liver and muscle. As a branched chain carbohydrate, broken down by phosphorylase debrancher enzymes, which are cytoplasmic. It also degraded lysosomal α-glucosidase (GAA) known as acid α-glucosidase. The deficiency of GAA patients Pompe disease, phenotypes infantile, juvenile later onset forms. disease treated enzyme replacement therapy (ERT) with recombinant form rhGAA. Following ERT mice human there residual carbohydrate material cytoplasm cells. goal this work to improve attempt identify treat cytoplasmic carbohydrate. Initial experiments were determine if rhGAA can completely degrade glycogen. cannot There glycosylated protein well soluble protein, terminal degradation product glycogen such serves biomarker for degradation. has very unusual composition protein: m-inositol, s-inositol sorbitol major carbohydrates, mannitol, mannose, glucose galactose. This describes likely contains same protein. serum control on ERT, not ERT. have another their may be disease. multiple glycosylation sites, each different components. These proteins complexity structure discussed, future directions try outcome being able monitor efficacy short term possibly adjust timing dose infusions.