| Literature DB >> 30843882 |
Su Xu1, Yi Lun1, Michelle Frascella1, Anadina Garcia1, Rebecca Soska1, Anju Nair1, Abdul S Ponery1, Adriane Schilling1, Jessie Feng1, Steven Tuske1, Maria Cecilia Della Valle1, José A Martina2, Evelyn Ralston3, Russell Gotschall1, Kenneth J Valenzano1, Rosa Puertollano2, Hung V Do1, Nina Raben2, Richie Khanna1.
Abstract
Pompe disease is a rare inherited disorder of lysosomal glycogen metabolism due to acid α-glucosidase (GAA) deficiency. Enzyme replacement therapy (ERT) using alglucosidase alfa, a recombinant human GAA (rhGAA), is the only approved treatment for Pompe disease. Although alglucosidase alfa has provided clinical benefits, its poor targeting to key disease-relevant skeletal muscles results in suboptimal efficacy. We are developing an rhGAA, ATB200 (Amicus proprietary rhGAA), with high levels of mannose-6-phosphate that are required for efficient cellular uptake and lysosomal trafficking. When administered in combination with the pharmacological chaperone AT2221 (miglustat), which stabilizes the enzyme and improves its pharmacokinetic properties, ATB200/AT2221 was substantially more potent than alglucosidase alfa in a mouse model of Pompe disease. The new investigational therapy is more effective at reversing the primary abnormality - intralysosomal glycogen accumulation - in multiple muscles. Furthermore, unlike the current standard of care, ATB200/AT2221 dramatically reduces autophagic buildup, a major secondary defect in the diseased muscles. The reversal of lysosomal and autophagic pathologies leads to improved muscle function. These data demonstrate the superiority of ATB200/AT2221 over the currently approved ERT in the murine model.Entities:
Keywords: Chaperones; Genetic diseases; Genetics; Lysosomes; Therapeutics
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Year: 2019 PMID: 30843882 PMCID: PMC6483515 DOI: 10.1172/jci.insight.125358
Source DB: PubMed Journal: JCI Insight ISSN: 2379-3708