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Hyaluronidase increases the biodistribution of acid alpha-1,4 glucosidase in the muscle of Pompe disease mice: an approach to enhance the efficacy of enzyme replacement therapy.
Biochem Biophys Res Commun 2006; 350(3):783-7BB

Abstract

Pompe disease (glycogen storage disease type II) is a glycogen storage disease caused by a deficiency of the lysosomal enzyme, acid maltase/acid alpha-1,4 glucosidase (GAA). Deficiency of the enzyme leads primarily to intra-lysosomal glycogen accumulation, primarily in cardiac and skeletal muscles, due to the inability of converting glycogen into glucose. Enzyme replacement therapy (ERT) has been applied to replace the deficient enzyme and to restore the lost function. However, enhancing the enzyme activity to the muscle following ERT is relatively insufficient. In order to enhance GAA activity into the muscle in Pompe disease, efficacy of hyaluronidase (hyase) was examined in the heart, quadriceps, diaphragm, kidney, and brain of mouse model of Pompe disease. Administration of hyase 3000 U/mouse (intravenous) i.v. or i.p. (intraperitoneal) and 10 min later recombinant human GAA (rhGAA) 20 mg/kg i.v. showed more GAA activity in hyase i.p. injected mice compared to those mice injected with hyase via i.v. Injection of low dose of hyase (3000 U/mouse) or high dose of hyase (10,000 U/mouse) i.p. and 20 min or 60 min later 20 mg/kg rhGAA i.v. increased GAA activity into the heart, diaphragm, kidney, and quadriceps compared to hyase untreated mice. These studies suggest that hyase enhances penetration of enzyme into the tissues including muscle during ERT and therefore hyase pretreatment may be important in treating Pompe disease.

Authors+Show Affiliations

Department of Pediatrics, The University of Texas Medical Branch, Galveston, TX 77555-0359, USA. rmatalon@utmb.eduNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

17027913

Citation

Matalon, Reuben, et al. "Hyaluronidase Increases the Biodistribution of Acid Alpha-1,4 Glucosidase in the Muscle of Pompe Disease Mice: an Approach to Enhance the Efficacy of Enzyme Replacement Therapy." Biochemical and Biophysical Research Communications, vol. 350, no. 3, 2006, pp. 783-7.
Matalon R, Surendran S, Campbell GA, et al. Hyaluronidase increases the biodistribution of acid alpha-1,4 glucosidase in the muscle of Pompe disease mice: an approach to enhance the efficacy of enzyme replacement therapy. Biochem Biophys Res Commun. 2006;350(3):783-7.
Matalon, R., Surendran, S., Campbell, G. A., Michals-Matalon, K., Tyring, S. K., Grady, J., ... Kaye, E. (2006). Hyaluronidase increases the biodistribution of acid alpha-1,4 glucosidase in the muscle of Pompe disease mice: an approach to enhance the efficacy of enzyme replacement therapy. Biochemical and Biophysical Research Communications, 350(3), pp. 783-7.
Matalon R, et al. Hyaluronidase Increases the Biodistribution of Acid Alpha-1,4 Glucosidase in the Muscle of Pompe Disease Mice: an Approach to Enhance the Efficacy of Enzyme Replacement Therapy. Biochem Biophys Res Commun. 2006 Nov 24;350(3):783-7. PubMed PMID: 17027913.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Hyaluronidase increases the biodistribution of acid alpha-1,4 glucosidase in the muscle of Pompe disease mice: an approach to enhance the efficacy of enzyme replacement therapy. AU - Matalon,Reuben, AU - Surendran,Sankar, AU - Campbell,Gerald A, AU - Michals-Matalon,Kimberlee, AU - Tyring,Stephen K, AU - Grady,James, AU - Cheng,Seng, AU - Kaye,Edward, Y1 - 2006/10/02/ PY - 2006/09/20/received PY - 2006/09/22/accepted PY - 2006/10/10/pubmed PY - 2006/12/9/medline PY - 2006/10/10/entrez SP - 783 EP - 7 JF - Biochemical and biophysical research communications JO - Biochem. Biophys. Res. Commun. VL - 350 IS - 3 N2 - Pompe disease (glycogen storage disease type II) is a glycogen storage disease caused by a deficiency of the lysosomal enzyme, acid maltase/acid alpha-1,4 glucosidase (GAA). Deficiency of the enzyme leads primarily to intra-lysosomal glycogen accumulation, primarily in cardiac and skeletal muscles, due to the inability of converting glycogen into glucose. Enzyme replacement therapy (ERT) has been applied to replace the deficient enzyme and to restore the lost function. However, enhancing the enzyme activity to the muscle following ERT is relatively insufficient. In order to enhance GAA activity into the muscle in Pompe disease, efficacy of hyaluronidase (hyase) was examined in the heart, quadriceps, diaphragm, kidney, and brain of mouse model of Pompe disease. Administration of hyase 3000 U/mouse (intravenous) i.v. or i.p. (intraperitoneal) and 10 min later recombinant human GAA (rhGAA) 20 mg/kg i.v. showed more GAA activity in hyase i.p. injected mice compared to those mice injected with hyase via i.v. Injection of low dose of hyase (3000 U/mouse) or high dose of hyase (10,000 U/mouse) i.p. and 20 min or 60 min later 20 mg/kg rhGAA i.v. increased GAA activity into the heart, diaphragm, kidney, and quadriceps compared to hyase untreated mice. These studies suggest that hyase enhances penetration of enzyme into the tissues including muscle during ERT and therefore hyase pretreatment may be important in treating Pompe disease. SN - 0006-291X UR - https://www.unboundmedicine.com/medline/citation/17027913/Hyaluronidase_increases_the_biodistribution_of_acid_alpha_14_glucosidase_in_the_muscle_of_Pompe_disease_mice:_an_approach_to_enhance_the_efficacy_of_enzyme_replacement_therapy_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-291X(06)02175-9 DB - PRIME DP - Unbound Medicine ER -