| pubmed-article:8265625 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8265625 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:8265625 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:8265625 | lifeskim:mentions | umls-concept:C0034785 | lld:lifeskim |
| pubmed-article:8265625 | lifeskim:mentions | umls-concept:C0024742 | lld:lifeskim |
| pubmed-article:8265625 | lifeskim:mentions | umls-concept:C0086376 | lld:lifeskim |
| pubmed-article:8265625 | lifeskim:mentions | umls-concept:C0021666 | lld:lifeskim |
| pubmed-article:8265625 | lifeskim:mentions | umls-concept:C0037791 | lld:lifeskim |
| pubmed-article:8265625 | lifeskim:mentions | umls-concept:C0439836 | lld:lifeskim |
| pubmed-article:8265625 | pubmed:issue | 24 | lld:pubmed |
| pubmed-article:8265625 | pubmed:dateCreated | 1994-1-21 | lld:pubmed |
| pubmed-article:8265625 | pubmed:abstractText | The 14-residue peptide (peptide 14) corresponding to Arg2410-Lys2423 of the insulin-like growth factor II receptor (IGF-IIR) can activate the adenylate cyclase-inhibitor guanine nucleotide-binding protein Gi, and the 15-residue beta III-2 peptide Arg259-Lys273 of the beta 2-adrenergic receptor (beta 2AR) can activate the stimulatory protein Gs. In phospholipid vesicles, IGF-IIR and beta 2AR activate Gi and Gs in response to IGF-II and isoproterenol, respectively. We constructed a chimeric IGF-II receptor (beta III-2/IGF-IIR) by converting its native peptide 14 sequence to the beta III-2 sequence. In cells expressing beta III-2/IGF-IIR, membrane adenylate cyclase activity markedly increased without IGF-II and was further promoted by IGF-II. This was verified by measuring chloramphenicol acetyltransferase (CAT) activity in beta III-2/IGF-IIR cells with cotransfection of a cAMP response element-CAT construct. This study shows not only the conversion of G-protein specificity of a receptor from Gi to Gs but also the simulation of G protein-coupled receptor signals by using a short receptor region and intact cells. These findings indicate that the G protein-activation signals are interchangeable, self-determined structural motifs that function in the setting of either a single-spanning or multiple-spanning receptor. | lld:pubmed |
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| pubmed-article:8265625 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8265625 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8265625 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8265625 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8265625 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8265625 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:8265625 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:8265625 | pubmed:author | pubmed-author:TakahashiSS | lld:pubmed |
| pubmed-article:8265625 | pubmed:author | pubmed-author:TakahashiKK | lld:pubmed |
| pubmed-article:8265625 | pubmed:author | pubmed-author:OgataEE | lld:pubmed |
| pubmed-article:8265625 | pubmed:author | pubmed-author:OkamotoTT | lld:pubmed |
| pubmed-article:8265625 | pubmed:author | pubmed-author:YokotaTT | lld:pubmed |
| pubmed-article:8265625 | pubmed:author | pubmed-author:MurayamaYY | lld:pubmed |
| pubmed-article:8265625 | pubmed:author | pubmed-author:NishimotoII | lld:pubmed |
| pubmed-article:8265625 | pubmed:author | pubmed-author:IkezuTT | lld:pubmed |
| pubmed-article:8265625 | pubmed:author | pubmed-author:GiambarellaUU | lld:pubmed |
| pubmed-article:8265625 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8265625 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8265625 | pubmed:volume | 90 | lld:pubmed |
| pubmed-article:8265625 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8265625 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8265625 | pubmed:pagination | 11772-6 | lld:pubmed |
| pubmed-article:8265625 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:8265625 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8265625 | pubmed:articleTitle | Conversion of G-protein specificity of insulin-like growth factor II/mannose 6-phosphate receptor by exchanging of a short region with beta-adrenergic receptor. | lld:pubmed |
| pubmed-article:8265625 | pubmed:affiliation | Department of Medicine, Harvard Medical School, Massachusetts General Hospital-East, Charlestown 02129. | lld:pubmed |
| pubmed-article:8265625 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8265625 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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