Source:http://linkedlifedata.com/resource/pubmed/id/16180101
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-2
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pubmed:dateCreated |
2005-9-23
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pubmed:abstractText |
Recently, it has become apparent that asparagine-linked (N-linked) oligosaccharide at an early stage of processing can play an important role in quality control of the secretory pathway. Here, we have developed a system for better understanding of the N-glycosylation machinery and its involvement in quality control in the endoplasmic reticulum (ER). Rough microsomes (RM) treated with 0.18% Tx-100 (TxRM) preserved translocation activities to a similar extent detected in RM. TxRM were depleted of many soluble proteins including glucosidase II, BiP and Erp72, but maintained approximately 80% of calnexin, a membrane protein. More importantly, TxRM revealed insufficient glycosylation of T cell receptor-alpha (TCR-alpha), suggesting that a factor or factors extracted with 0.18% Tx-100 is responsible for facilitating the transfer of oligosaccharides to the protein. In addition, the top band of TCR-alpha translated in TxRM migrated slower than that in RM, but faster than that in RM treated with castanospermine (CST), an inhibitor of glucosidase I/II. This suggests that the trimming of the inner two glucose sugars is impaired by the loss of glucosidase II. Furthermore, we demonstrated that TCR-alpha coprecipitated with calnexin migrated between unglucosylated and diglucosylated forms on SDS-PAGE. Thus, the treatment of RM with low concentration of detergent is a very powerful method for elucidating not only N-glycosylation processes but also other biological functions such as quality control in the ER.
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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/4-nitrophenyl-alpha-glucosidase,
http://linkedlifedata.com/resource/pubmed/chemical/Calnexin,
http://linkedlifedata.com/resource/pubmed/chemical/HSP47 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Octoxynol,
http://linkedlifedata.com/resource/pubmed/chemical/Oligosaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-Glucosidases
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0300-8177
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
278
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
157-63
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:16180101-Animals,
pubmed-meshheading:16180101-Calnexin,
pubmed-meshheading:16180101-Dogs,
pubmed-meshheading:16180101-Genes, T-Cell Receptor alpha,
pubmed-meshheading:16180101-Glycosylation,
pubmed-meshheading:16180101-HSP47 Heat-Shock Proteins,
pubmed-meshheading:16180101-Microsomes,
pubmed-meshheading:16180101-Octoxynol,
pubmed-meshheading:16180101-Oligosaccharides,
pubmed-meshheading:16180101-Pancreas,
pubmed-meshheading:16180101-alpha-Glucosidases
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pubmed:year |
2005
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pubmed:articleTitle |
A novel approach for N-glycosylation studies using detergent extracted microsomes.
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pubmed:affiliation |
Department of Anatomy, Biology and Medicine, Faculty of Medicine, Oita University, 1-1 Idaigaoka, Hasama-machi, Oita, Japan.
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pubmed:publicationType |
Journal Article,
In Vitro,
Evaluation Studies
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