| pubmed-article:3827820 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3827820 | lifeskim:mentions | umls-concept:C0021641 | lld:lifeskim |
| pubmed-article:3827820 | lifeskim:mentions | umls-concept:C0034818 | lld:lifeskim |
| pubmed-article:3827820 | lifeskim:mentions | umls-concept:C0028959 | lld:lifeskim |
| pubmed-article:3827820 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:3827820 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:3827820 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:3827820 | pubmed:dateCreated | 1987-4-1 | lld:pubmed |
| pubmed-article:3827820 | pubmed:abstractText | The insulin receptor is synthesized as a 190,000-Mr single-chain precursor that contains exclusively asparagine-N-linked high-mannose-type carbohydrate chains. In this study we have characterized the structure of the pro-receptor oligosaccharides. IM-9 lymphocytes were pulse-chase-labelled with [3H]mannose, and the insulin pro-receptor was isolated by immunoprecipitation and SDS/polyacrylamide-gel electrophoresis. The pro-receptor oligosaccharides were removed from the protein backbone with endoglycosidase H and analysed by h.p.l.c. Immediately after a [3H]mannose pulse the largest oligosaccharide found in the pro-receptor was Glc1Man9GlcNAc2; this structure represented only a small fraction (3%) of the total. The predominant oligosaccharides present in the pro-receptor were Man9GlcNAc2 (25%) and Man8GlcNAc2 (48%). Smaller oligosaccharides were also detected: Man7GlcNAc2 (18%), Man6GlcNAc2 (3%) and Man5GlcNAc2 (3%). The relative distribution of the different oligosaccharides did not change at 1, 2 or 3 h after the pulse with the exception of the rapid disappearance of the Glc1Man9GlcNAc2 component. The mature alpha- and beta-subunits of the insulin receptor are known to contain both high-mannose-type and complex-type oligosaccharides. We have also examined here the structure of the high-mannose chains of these subunits. The predominant species in the alpha-subunit was Man8GlcNAc2 whereas in the beta-subunit it was Man7GlcNAc2. These results demonstrate that most (approx. 75%) oligosaccharides of the insulin pro-receptor are chains of the type Man8GlcNAc2 or Man9GlcNAc2. Thus, assuming that a Glc3Man9GlcNAc2 species is transferred co-translationally, carbohydrate processing of the pro-receptor appears to be very rapid and limited to the removal of the three glucose residues and one mannose residue. Further mannose removal does not occur until the pro-receptor has been proteolytically cleaved. In addition, the degree of mannose trimming appears to be different in the alpha- and beta-subunits. | lld:pubmed |
| pubmed-article:3827820 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:3827820 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3827820 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3827820 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3827820 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3827820 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3827820 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3827820 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3827820 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3827820 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3827820 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3827820 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3827820 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3827820 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3827820 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3827820 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3827820 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3827820 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3827820 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3827820 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3827820 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3827820 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3827820 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:3827820 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:3827820 | pubmed:author | pubmed-author:GordenPP | lld:pubmed |
| pubmed-article:3827820 | pubmed:author | pubmed-author:HedoJ AJA | lld:pubmed |
| pubmed-article:3827820 | pubmed:author | pubmed-author:McElduffAA | lld:pubmed |
| pubmed-article:3827820 | pubmed:author | pubmed-author:WatkinsonAA | lld:pubmed |
| pubmed-article:3827820 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3827820 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:3827820 | pubmed:volume | 239 | lld:pubmed |
| pubmed-article:3827820 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3827820 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3827820 | pubmed:pagination | 679-83 | lld:pubmed |
| pubmed-article:3827820 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:3827820 | pubmed:meshHeading | pubmed-meshheading:3827820-... | lld:pubmed |
| pubmed-article:3827820 | pubmed:meshHeading | pubmed-meshheading:3827820-... | lld:pubmed |
| pubmed-article:3827820 | pubmed:meshHeading | pubmed-meshheading:3827820-... | lld:pubmed |
| pubmed-article:3827820 | pubmed:meshHeading | pubmed-meshheading:3827820-... | lld:pubmed |
| pubmed-article:3827820 | pubmed:meshHeading | pubmed-meshheading:3827820-... | lld:pubmed |
| pubmed-article:3827820 | pubmed:meshHeading | pubmed-meshheading:3827820-... | lld:pubmed |
| pubmed-article:3827820 | pubmed:year | 1986 | lld:pubmed |
| pubmed-article:3827820 | pubmed:articleTitle | Characterization of the N-linked high-mannose oligosaccharides of the insulin pro-receptor and mature insulin receptor subunits. | lld:pubmed |
| pubmed-article:3827820 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3827820 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
