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Uptake and stability of human and bovine acid alpha-glucosidase in cultured fibroblasts and skeletal muscle cells from glycogenosis type II patients.
Exp Cell Res. 1984 Nov; 155(1):178-89.EC

Abstract

Acid alpha-glucosidase (EC 3.2.1.20) was purified from human placenta and bovine testis by affinity chromatography using concanavalin A (conA) and Sephadex G 200. When added to the culture medium of human fibroblasts, the enzyme purified from bovine testis is taken up with a 200-fold higher efficiency than the enzyme from human placenta. Uptake of acid alpha-glucosidase from bovine testis is mediated by the mannose-6-phosphate receptor, whereas only a minor fraction of placental enzyme appears to be equipped with the mannose-6-phosphate recognition marker. Once internalized, both human and bovine acid alpha-glucosidase demonstrate a half-life of about 10 days in fibroblasts from control individuals and patients with different clinical forms of glycogenosis type II (Pompe's disease, acid alpha-glucosidase deficiency). Evidence is presented that the mannose-6-phosphate receptor is also present on the plasma membrane of the clonal myogenic skeletal muscle cell lines G8-1 and L6J1 (respectively from mouse and rat origin) and on cultured human skeletal muscle cells derived from a muscle biopsy. Addition of bovine testis acid alpha-glucosidase to skeletal muscle cell cultures from an adult patient with glycogenosis type II leads to complete correction of the enzyme deficiency.

Authors

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Pub Type(s)

Journal Article

Language

eng

PubMed ID

6237928

Citation

Reuser, A J., et al. "Uptake and Stability of Human and Bovine Acid Alpha-glucosidase in Cultured Fibroblasts and Skeletal Muscle Cells From Glycogenosis Type II Patients." Experimental Cell Research, vol. 155, no. 1, 1984, pp. 178-89.
Reuser AJ, Kroos MA, Ponne NJ, et al. Uptake and stability of human and bovine acid alpha-glucosidase in cultured fibroblasts and skeletal muscle cells from glycogenosis type II patients. Exp Cell Res. 1984;155(1):178-89.
Reuser, A. J., Kroos, M. A., Ponne, N. J., Wolterman, R. A., Loonen, M. C., Busch, H. F., Visser, W. J., & Bolhuis, P. A. (1984). Uptake and stability of human and bovine acid alpha-glucosidase in cultured fibroblasts and skeletal muscle cells from glycogenosis type II patients. Experimental Cell Research, 155(1), 178-89.
Reuser AJ, et al. Uptake and Stability of Human and Bovine Acid Alpha-glucosidase in Cultured Fibroblasts and Skeletal Muscle Cells From Glycogenosis Type II Patients. Exp Cell Res. 1984;155(1):178-89. PubMed PMID: 6237928.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Uptake and stability of human and bovine acid alpha-glucosidase in cultured fibroblasts and skeletal muscle cells from glycogenosis type II patients. AU - Reuser,A J, AU - Kroos,M A, AU - Ponne,N J, AU - Wolterman,R A, AU - Loonen,M C, AU - Busch,H F, AU - Visser,W J, AU - Bolhuis,P A, PY - 1984/11/1/pubmed PY - 1984/11/1/medline PY - 1984/11/1/entrez SP - 178 EP - 89 JF - Experimental cell research JO - Exp. Cell Res. VL - 155 IS - 1 N2 - Acid alpha-glucosidase (EC 3.2.1.20) was purified from human placenta and bovine testis by affinity chromatography using concanavalin A (conA) and Sephadex G 200. When added to the culture medium of human fibroblasts, the enzyme purified from bovine testis is taken up with a 200-fold higher efficiency than the enzyme from human placenta. Uptake of acid alpha-glucosidase from bovine testis is mediated by the mannose-6-phosphate receptor, whereas only a minor fraction of placental enzyme appears to be equipped with the mannose-6-phosphate recognition marker. Once internalized, both human and bovine acid alpha-glucosidase demonstrate a half-life of about 10 days in fibroblasts from control individuals and patients with different clinical forms of glycogenosis type II (Pompe's disease, acid alpha-glucosidase deficiency). Evidence is presented that the mannose-6-phosphate receptor is also present on the plasma membrane of the clonal myogenic skeletal muscle cell lines G8-1 and L6J1 (respectively from mouse and rat origin) and on cultured human skeletal muscle cells derived from a muscle biopsy. Addition of bovine testis acid alpha-glucosidase to skeletal muscle cell cultures from an adult patient with glycogenosis type II leads to complete correction of the enzyme deficiency. SN - 0014-4827 UR - https://www.unboundmedicine.com/medline/citation/6237928/Uptake_and_stability_of_human_and_bovine_acid_alpha_glucosidase_in_cultured_fibroblasts_and_skeletal_muscle_cells_from_glycogenosis_type_II_patients_ L2 - https://linkinghub.elsevier.com/retrieve/pii/0014-4827(84)90779-1 DB - PRIME DP - Unbound Medicine ER -