pubmed-article:3359262 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:3359262 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
pubmed-article:3359262 | lifeskim:mentions | umls-concept:C0034818 | lld:lifeskim |
pubmed-article:3359262 | lifeskim:mentions | umls-concept:C0028959 | lld:lifeskim |
pubmed-article:3359262 | lifeskim:mentions | umls-concept:C0486616 | lld:lifeskim |
pubmed-article:3359262 | lifeskim:mentions | umls-concept:C0205349 | lld:lifeskim |
pubmed-article:3359262 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:3359262 | pubmed:issue | 1-2 | lld:pubmed |
pubmed-article:3359262 | pubmed:dateCreated | 1988-5-31 | lld:pubmed |
pubmed-article:3359262 | pubmed:abstractText | Typical insulin receptors are present on neuroblastoma cell lines. High affinity binding for insulin was present in membrane preparations from NG108 (a hybrid mouse neuroblastoma-rat glioma) as well as in membranes from SK-N-MC and SK-N-SH, two human neuroblastoma cell lines. Specific [125I]insulin binding was 24.4% for NG108, 16.9% for SK-N-MC and 5.2% for SK-N-SH at membrane protein concentrations of 0.4 mg/ml. IC50 for [125I]insulin binding was 3.4 nM in NG108 membrane preparations and 0.9 nM for SK-N-SH and 1.8 nM in SK-N-MC membranes. Apparent mol. wt. for the alpha subunits (identified by specific immunoprecipitation using the anti-insulin receptor antiserum B10) on SDS PAGE was 134 kDa for NG108; 124 kDa for SK-N-MC and 120 kDa for SK-N-SH. Neuraminidase digestion increased the mobility of the alpha subunit from both NG108 and SK-N-MC receptors to 120 kDa, whereas that from SK-N-SH were unaffected. Endoglycosidase H and endoglycosidase F digestions increased the mobility of the alpha subunits of all 3 cell lines to varying degrees, suggesting the presence of N-linked glycosylation. Insulin induced autophosphorylation of the insulin receptor beta subunit in WGA-purified membranes from all 3 cell lines. In addition, phosphorylation of a protein with an apparent mol. wt. 105 kDa was stimulated by insulin in WGA purified membranes from NG108. Tyrosine-specific kinase activity was present in the membranes from each cell line and was stimulated by insulin in a dose-dependent manner from 10(-9) to 10(-6) M. Proinsulin was about 100 times less potent in stimulating phosphorylation of the artificial substrate poly (Glu, Tyr)4:1 when compared to insulin in accordance with its lower binding affinity to the insulin receptor. Hexose transport was stimulated by insulin in all 3 cell lines. These results indicate that neuroblastoma cells contain specific insulin receptors and that they may be useful as models for studying the role of insulin in nervous tissue. | lld:pubmed |
pubmed-article:3359262 | pubmed:language | eng | lld:pubmed |
pubmed-article:3359262 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3359262 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:3359262 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3359262 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3359262 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3359262 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3359262 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3359262 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:3359262 | pubmed:month | Mar | lld:pubmed |
pubmed-article:3359262 | pubmed:issn | 0006-8993 | lld:pubmed |
pubmed-article:3359262 | pubmed:author | pubmed-author:LeRoithDD | lld:pubmed |
pubmed-article:3359262 | pubmed:author | pubmed-author:PrussR MRM | lld:pubmed |
pubmed-article:3359262 | pubmed:author | pubmed-author:PUTRR | lld:pubmed |
pubmed-article:3359262 | pubmed:author | pubmed-author:ShemerJJ | lld:pubmed |
pubmed-article:3359262 | pubmed:author | pubmed-author:LoweW LWLJr | lld:pubmed |
pubmed-article:3359262 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:3359262 | pubmed:day | 8 | lld:pubmed |
pubmed-article:3359262 | pubmed:volume | 443 | lld:pubmed |
pubmed-article:3359262 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:3359262 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:3359262 | pubmed:pagination | 1-11 | lld:pubmed |
pubmed-article:3359262 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:3359262 | pubmed:year | 1988 | lld:pubmed |
pubmed-article:3359262 | pubmed:articleTitle | Characterization of the altered oligosaccharide composition of the insulin receptor on neural-derived cells. | lld:pubmed |
pubmed-article:3359262 | pubmed:affiliation | Section of Molecular and Cellular Physiology, NIDDK, Bethesda, MD 20892. | lld:pubmed |
pubmed-article:3359262 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:3359262 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3359262 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3359262 | lld:pubmed |