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Methods and compositions for treatment of lysosomal storage disorders

JME Group Associates Inc.
2023
Online Patent

Titel:
Methods and compositions for treatment of lysosomal storage disorders
Autor/in / Beteiligte Person: JME Group Associates Inc.
Link:
Veröffentlichung: 2023
Medientyp: Patent
Sonstiges:
  • Nachgewiesen in: USPTO Patent Grants
  • Sprachen: English
  • Patent Number: 11839,641
  • Publication Date: December 12, 2023
  • Appl. No: 17/404680
  • Application Filed: August 17, 2021
  • Assignees: JME GROUP ASSOCIATES INC. (Roseland, NJ, US)
  • Claim: 1. A method of treating a lysosomal storage disease resulting from a deficiency of acid maltase and/or acid α-glucosidase, said method comprising: selecting a subject having a lysosomal storage disease resulting from a deficiency of acid maltase and/or acid α-glucosidase, and administering ground germinated barley (GGB) to the selected subject to treat the lysosomal storage disease; wherein the GBB possesses barley acid α-glucosidase (bGAA) enzymatic activity; and wherein the lysosomal storage disease is selected from the group consisting of a glycogen storage disease type II, acid maltase deficiency, Pompe's disease, and combinations thereof.
  • Claim: 2. The method of claim 1 , wherein the lysosomal storage disease is glycogen storage disease type II.
  • Claim: 3. The method of claim 2 , wherein the lysosomal storage disease is infantile glycogen storage disease type II.
  • Claim: 4. The method of claim 2 , wherein the lysosomal storage disease is juvenile glycogen storage disease type II.
  • Claim: 5. The method of claim 2 , wherein the lysosomal storage disease is adult-onset glycogen storage disease type II.
  • Claim: 6. The method of claim 1 , wherein said method is carried out in conjunction with enzyme replacement therapy.
  • Claim: 7. The method of claim 1 , wherein said method is carried out in conjunction with alglucosidase alfa treatment.
  • Claim: 8. The method of claim 7 , wherein the alglucosidase alfa treatment is carried out intravenously.
  • Claim: 9. The method of claim 1 , wherein said administering is carried out orally.
  • Claim: 10. The method of claim 1 , wherein said administering is carried out daily in a single dose or multiple doses of GGB.
  • Claim: 11. The method of claim 1 , wherein said administering is carried in daily doses of 1 to 3 g/kg of the selected subject.
  • Other References: Chien et al (Pediatrics and Neonatology 54:219-227, 2013) (Year: 2013). cited by examiner ; Hubner et al (Eur Food Res Technol 231:27-35, 2010) (Year: 2010). cited by examiner ; Rico et al (Foods 9:19 pages, 2020) (Year: 2020). cited by examiner ; Zhou et al (Food Sci Biotechnol 22:1753-1761, 2013) (Year: 2013). cited by examiner ; Deng et al (Int J Molecular Sciences 21:20 pages, 2020) (Year: 2020). cited by examiner ; Malunga et al (Frontiers in Nutrition, 8:9 pages, 2021) (Year: 2021). cited by examiner ; Frandsen et al., “Purification, Enzymatic Characterization, and Nucleotide Sequence of a High-Isoelectric-Point from Barley Malt,” Plant Physiology 123:275-286 (2000). cited by applicant ; Raben et al., “Enzyme Replacement Therapy in the Mouse Model of Pompe Disease,” Mol Genet Metab. 80:159-169 (2003). cited by applicant ; Martiniuk et al., “Further Studies of the Structure of Human Placental Acid Alpha-Glucosidase,” Arch Biochem Biophys 231:454-460 (1984). cited by applicant ; Andriotis et al., “The Maltase Involved in Starch Metabolism in Barley Endosperm is Encoded by a Single Gene,” PLoS ONE 11:e0151642 (2016). cited by applicant ; Van Gelder et al., “Enzyme Therapy and Immune Response in Relation to CRIM Status: The Dutch Experience in Classic Infantile Pompe Disease,” J Inherit Metab Dis.38:305-314 (2015). cited by applicant ; Martiniuk et al., “Correction of Glycogen Storage Disease Type II by Enzyme Replacement With a Recombinant Human Acid Maltase Produced by Over-Expression in a CHO-DHFR (Neg) Cell Line,” Biochem Biophys Res Commun. 276:917-923 (2000). cited by applicant ; Raben et al., “Targeted Disruption of the Acid Alpha-Glucosidase Gene in Mice Causes an Illness with Critical Features of Both Infantile and Adult Human Glycogen Storage Disease Type II,” J Biol Chem. 273:19086-19092 (1998). cited by applicant ; Jung et al., “Production and Characterization of Recombinant Human Acid Alpha-Glucosidase in Transgenic Rice Cell Suspension Culture”, J. Biotechnology 226:44-53 (2016). cited by applicant ; Jung et al., “Production of Recombinant Human Acid α-Glucosidase With High-Mannose Glycans in gnt1 Rice for the Treatment of Pompe Disease”, J. Biotechnology 249:42-50 (2017). cited by applicant ; Martiniuk et al., “Production of a Functional Human Acid Maltase in Tobacco Seeds: Biochemical Analysis, Uptake by Human GSDII Cells, and in vivo Studies in GAA Knockout Mice,” Appl Biochem Biotechnol. 171:916-926 (2013). cited by applicant
  • Primary Examiner: Ricci, Craig D
  • Attorney, Agent or Firm: Troutman Pepper Hamilton Sanders LLP (Rochester)

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