Subcutaneous administration of recombinant human acid α-glucosidase co-formulated with the pharmacological chaperone AT2220 leads to lysosomal uptake of rhGAA and glycogen reduction in disease-relevant tissues of mice with Pompe disease

2014 ◽  
Vol 111 (2) ◽  
pp. S73
Author(s):  
Yi Lun ◽  
Lee Pellegrino ◽  
Su Xu ◽  
Jessie Feng ◽  
Rebecca Soska ◽  
...  
Keyword(s):  
Pompe Disease ◽  
Subcutaneous Administration ◽  
Pharmacological Chaperone ◽  
Human Acid

scholarly journals The Pharmacological Chaperone AT2220 Increases Recombinant Human Acid α-Glucosidase Uptake and Glycogen Reduction in a Mouse Model of Pompe Disease

PLoS ONE ◽  
2012 ◽  
Vol 7 (7) ◽  
pp. e40776 ◽  
Author(s):  
Richie Khanna ◽  
John J. Flanagan ◽  
Jessie Feng ◽  
Rebecca Soska ◽  
Michelle Frascella ◽  
...  
Keyword(s):  
Mouse Model ◽  
Pompe Disease ◽  
Pharmacological Chaperone ◽  
Human Acid

scholarly journals The molecular basis for Pompe disease revealed by the structure of human acid α-glucosidase

2017 ◽  
Author(s):  
Derrick Deming ◽  
Karen Lee ◽  
Tracey McSherry ◽  
Ronnie R. Wei ◽  
Tim Edmunds ◽  
...  
Keyword(s):  
Pompe Disease ◽  
Molecular Basis ◽  
Glycogen Storage ◽  
Type Ii ◽  
Pharmacological Chaperone ◽  
Enzyme Replacement ◽  
Human Acid ◽  
Glycogen Storage Disorder ◽  
Cellular Dysfunction ◽  
Disorder Type

AbstractPompe disease results from a defect in human acid α-glucosidase (GAA), a lysosomal enzyme that cleaves terminal α1-4 and α1-6 glucose from glycogen. In Pompe disease (also known as Glycogen Storage Disorder type II), the accumulation of undegraded glycogen in lysosomes leads to cellular dysfunction, primarily in muscle and heart tissues. Pompe disease is an active candidate of clinical research, with pharmacological chaperone therapy tested and enzyme replacement therapy approved. Despite production of large amounts of recombinant GAA annually, the structure of GAA has not been reported until now. Here, we describe the first structure of GAA, at 1.7Å resolution. Three structures of GAA complexes reveal the molecular basis for the hundreds of mutations that lead to Pompe disease and for pharmacological chaperoning in the protein. The GAA structure reveals a surprising second sugar-binding site 34Å from the active site, suggesting a possible mechanism for processing of large glycogen substrates. Overall, the structure will assist in the design of next-generation treatments for Pompe disease.

Pregnancy in a Case of Pompe Disease Treated with Recombinant Human Acid Alpha Glucosidase (Myozyme)

2011 ◽  
Vol 33 (6) ◽  
pp. S22
Author(s):  
F. Zagnoli ◽  
A. Leblanc ◽  
C. Blanchard ◽  
A. Philippe ◽  
M. Lastennet
Keyword(s):  
Pompe Disease ◽  
Human Acid ◽  
Alpha Glucosidase

Benefit of Recombinant Human Acid Alpha Glucosidase Treatment (Myozyme) in Late Onset Pompe Disease: About Five Cases Treated for 3 Years

2011 ◽  
Vol 33 (6) ◽  
pp. S23
Author(s):  
F. Zagnoli ◽  
A. Leblanc ◽  
C. Blanchard ◽  
A. Philippe ◽  
M. Lastennet
Keyword(s):  
Pompe Disease ◽  
Late Onset ◽  
Human Acid ◽  
Alpha Glucosidase
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