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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1981-6-13
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pubmed:abstractText |
A cultured cell line of the mosquito, Aedes aegypti, is sensitive to tunicamycin as expected from the ability of crude membrane preparations to catalyse the formation of N-acetylglucosamine-linked dolichyl pyrophosphate. Formation of dolichylphosphomannose was also detected and this reaction was totally insensitive to tunicamycin. Incorporation of radioactive mannose into total acid-precipitable glycoproteins was inhibited greater than 90% in whole cells by tunicamycin, while the incorporation of leucine and glucosamine was less affected. Separation of the radioactive hexosamines from acid hydrolysates of cells incubated with [14C]glucosamine and tunicamycin showed predominant labelling of galactosamine, whereas in control cells not treated with the drug both glucosamine and galactosamine were labelled equally. Evidently, mosquito cells synthesise N-glycosidically linked carbohydrate chains assembled through tunicamycin-sensitive steps involving dolichyl pyrophospho-oligosaccharides, and O-glycosidically linked chains rich in N-acetylgalactosamine, the assembly of which is unaffected by tunicamycin. These results support structural evidence (Butters, T.D. and Hughes, R.C. (1981) Biochim. Biophys. Acta 640, 655-671) for the presence of high mannose N-glycans and N-acetylgalactosamine-rich O-glycans in mosquito cell glycoproteins. The absence of complex N-glycans was confirmed by the demonstration of negligible activities of N-acetylglucosaminyl-, galactosyl- and sialyltransferases responsible for assembly of the terminal sequences of N-glycans of mature mammalian glycoproteins.
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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/Glucosamine,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Octoxynol,
http://linkedlifedata.com/resource/pubmed/chemical/Polyethylene Glycols,
http://linkedlifedata.com/resource/pubmed/chemical/Tunicamycin
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
640
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
672-86
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pubmed:dateRevised |
2005-11-17
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pubmed:meshHeading |
pubmed-meshheading:7213699-Aedes,
pubmed-meshheading:7213699-Animals,
pubmed-meshheading:7213699-Carbohydrate Metabolism,
pubmed-meshheading:7213699-Cell Line,
pubmed-meshheading:7213699-Cell Membrane,
pubmed-meshheading:7213699-Glucosamine,
pubmed-meshheading:7213699-Glycoproteins,
pubmed-meshheading:7213699-Kinetics,
pubmed-meshheading:7213699-Lectins,
pubmed-meshheading:7213699-Membrane Proteins,
pubmed-meshheading:7213699-Octoxynol,
pubmed-meshheading:7213699-Polyethylene Glycols,
pubmed-meshheading:7213699-Tunicamycin
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pubmed:year |
1981
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pubmed:articleTitle |
Steps in the biosynthesis of mosquito cell membrane glycoproteins and the effects of tunicamycin.
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pubmed:publicationType |
Journal Article
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