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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
15
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pubmed:dateCreated |
1989-8-28
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pubmed:abstractText |
The effect of the alpha-glucosidase inhibitor N-hydroxyethyl-1-deoxynojirimycin (Bay m 1099) on the glycosylation and secretion of alpha 1-antitrypsin (three complex type oligosaccharide chains) and of alpha 1-acid glycoprotein (six complex type oligosaccharide chains) was studied in rat hepatocyte primary cultures. In the presence of 4 mM Bay m 1099 the processing of high-mannose to complex type oligosaccharides was partially inhibited leading to the secretion of alpha 1-antitrypsin and alpha 1-acid glycoprotein carrying a mixture of both high-mannose and complex type oligosaccharides. The major part of alpha 1-antitrypsin secreted by Bay m 1099 treated cells still carried two complex type oligosaccharide chains, the majority of alpha 1-acid glycoprotein carried three to five. Despite its effects on protein glycosylation Bay m 1099 did not lead to pronounced changes in the synthesis or secretion of alpha 1-antitrypsin, alpha 1-acid glycoprotein or albumin. At concentrations of Bay m 1099 lower than 0.5 mM no inhibitory effect on oligosaccharide trimming could be observed. After removal of Bay m 1099 from hepatocytes its inhibitory effect on protein glycosylation was immediately reversible.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/1-Deoxynojirimycin,
http://linkedlifedata.com/resource/pubmed/chemical/Acetylglucosaminidase,
http://linkedlifedata.com/resource/pubmed/chemical/Glucosamine,
http://linkedlifedata.com/resource/pubmed/chemical/Imino Pyranoses,
http://linkedlifedata.com/resource/pubmed/chemical/Mannosyl-Glycoprotein...,
http://linkedlifedata.com/resource/pubmed/chemical/Orosomucoid,
http://linkedlifedata.com/resource/pubmed/chemical/alpha 1-Antitrypsin,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-Glucosidases,
http://linkedlifedata.com/resource/pubmed/chemical/miglitol
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0006-2952
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
38
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2479-86
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:2502984-1-Deoxynojirimycin,
pubmed-meshheading:2502984-Acetylglucosaminidase,
pubmed-meshheading:2502984-Animals,
pubmed-meshheading:2502984-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:2502984-Female,
pubmed-meshheading:2502984-Glucosamine,
pubmed-meshheading:2502984-Imino Pyranoses,
pubmed-meshheading:2502984-Liver,
pubmed-meshheading:2502984-Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase,
pubmed-meshheading:2502984-Orosomucoid,
pubmed-meshheading:2502984-Precipitin Tests,
pubmed-meshheading:2502984-Rats,
pubmed-meshheading:2502984-Rats, Inbred Strains,
pubmed-meshheading:2502984-alpha 1-Antitrypsin,
pubmed-meshheading:2502984-alpha-Glucosidases
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pubmed:year |
1989
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pubmed:articleTitle |
Effect of the alpha-glucosidase inhibitor N-hydroxyethyl-1-deoxynojirimycin (Bay m 1099) on the biosynthesis of liver secretory glycoproteins.
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pubmed:affiliation |
Medizinische Klinik, Albert-Ludwigs-Universität, Freiburg, West Germany.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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