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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1984-12-7
|
| pubmed:abstractText |
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.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
0014-4827
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
155
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
178-89
|
| pubmed:dateRevised |
2004-11-17
|
| pubmed:meshHeading |
pubmed-meshheading:6237928-Animals,
pubmed-meshheading:6237928-Carrier Proteins,
pubmed-meshheading:6237928-Cattle,
pubmed-meshheading:6237928-Cells, Cultured,
pubmed-meshheading:6237928-Endocytosis,
pubmed-meshheading:6237928-Female,
pubmed-meshheading:6237928-Fibroblasts,
pubmed-meshheading:6237928-Glucosidases,
pubmed-meshheading:6237928-Glycogen Storage Disease,
pubmed-meshheading:6237928-Glycogen Storage Disease Type II,
pubmed-meshheading:6237928-Humans,
pubmed-meshheading:6237928-Male,
pubmed-meshheading:6237928-Metabolic Clearance Rate,
pubmed-meshheading:6237928-Muscles,
pubmed-meshheading:6237928-Placenta,
pubmed-meshheading:6237928-Receptor, IGF Type 2,
pubmed-meshheading:6237928-Testis,
pubmed-meshheading:6237928-alpha-Glucosidases
|
| pubmed:year |
1984
|
| pubmed:articleTitle |
Uptake and stability of human and bovine acid alpha-glucosidase in cultured fibroblasts and skeletal muscle cells from glycogenosis type II patients.
|
| pubmed:publicationType |
Journal Article
|