| pubmed-article:1695626 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1695626 | lifeskim:mentions | umls-concept:C0567416 | lld:lifeskim |
| pubmed-article:1695626 | lifeskim:mentions | umls-concept:C0074825 | lld:lifeskim |
| pubmed-article:1695626 | lifeskim:mentions | umls-concept:C1274040 | lld:lifeskim |
| pubmed-article:1695626 | lifeskim:mentions | umls-concept:C0021665 | lld:lifeskim |
| pubmed-article:1695626 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:1695626 | lifeskim:mentions | umls-concept:C1510827 | lld:lifeskim |
| pubmed-article:1695626 | lifeskim:mentions | umls-concept:C0443172 | lld:lifeskim |
| pubmed-article:1695626 | lifeskim:mentions | umls-concept:C2699782 | lld:lifeskim |
| pubmed-article:1695626 | lifeskim:mentions | umls-concept:C1515926 | lld:lifeskim |
| pubmed-article:1695626 | pubmed:issue | 21 | lld:pubmed |
| pubmed-article:1695626 | pubmed:dateCreated | 1990-8-30 | lld:pubmed |
| pubmed-article:1695626 | pubmed:abstractText | Insulin-like growth factor (IGF)-binding proteins (BPs) bind IGF-I and IGF-II with high affinity. They are present in extracellular fluids and modulate the interactions of their ligands with the type 1 IGF cell surface receptor. These studies utilized IGF-I analogs that have reduced binding affinity for either the type 1 IGF receptor or binding proteins to study the ligand specificity of IGF-BP-1 and the role of IGF-BP-1 in modulating the biological activity of IGF-I. The data indicate that the regions of IGF-I which are responsible for binding to IGF-BP-1 and to human serum-binding proteins are distinct but overlapping and are clearly distinct from the type I receptor binding sites. In the absence of exogenously added IGF-BP-1, the analogs with reduced affinity for IGF-BP-1 are more potent than IGF-I in stimulating DNA synthesis by porcine aortic smooth muscle cells. In contrast, when cells are concomitantly exposed to IGF-BP-1, two of the analogs with reduced affinity for binding protein give only 40-65% of the maximal IGF-I response. [Leu24, 1-62]IGF-I, which has a 100-fold reduced affinity for the type 1 IGF receptor, gave a value that was 62% of the maximal IGF-BP-1 potentiated response. A second biological response, that of stimulating binding protein secretion by IGF-I, was also examined. [Leu24, 1-62]IGF-I is more potent than IGF-I whereas the activity of the analogs with lower affinity for IGF-BP-1 is significantly reduced. Thus, the ability to activate DNA synthesis and binding protein secretion maximally in the presence of IGF-BP-1 is dependent on the affinity of IGFs for both type 1 receptors and binding proteins. | lld:pubmed |
| pubmed-article:1695626 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1695626 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1695626 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1695626 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1695626 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1695626 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1695626 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1695626 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1695626 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1695626 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1695626 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1695626 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1695626 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:1695626 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:1695626 | pubmed:author | pubmed-author:ClemmonsD RDR | lld:pubmed |
| pubmed-article:1695626 | pubmed:author | pubmed-author:CascieriM AMA | lld:pubmed |
| pubmed-article:1695626 | pubmed:author | pubmed-author:BayneM LML | lld:pubmed |
| pubmed-article:1695626 | pubmed:author | pubmed-author:McCuskerR HRH | lld:pubmed |
| pubmed-article:1695626 | pubmed:author | pubmed-author:Camacho-Hubne... | lld:pubmed |
| pubmed-article:1695626 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1695626 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:1695626 | pubmed:volume | 265 | lld:pubmed |
| pubmed-article:1695626 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1695626 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1695626 | pubmed:pagination | 12210-6 | lld:pubmed |
| pubmed-article:1695626 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:1695626 | pubmed:meshHeading | pubmed-meshheading:1695626-... | lld:pubmed |
| pubmed-article:1695626 | pubmed:meshHeading | pubmed-meshheading:1695626-... | lld:pubmed |
| pubmed-article:1695626 | pubmed:meshHeading | pubmed-meshheading:1695626-... | lld:pubmed |
| pubmed-article:1695626 | pubmed:meshHeading | pubmed-meshheading:1695626-... | lld:pubmed |
| pubmed-article:1695626 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:1695626 | pubmed:articleTitle | Discrete alterations of the insulin-like growth factor I molecule which alter its affinity for insulin-like growth factor-binding proteins result in changes in bioactivity. | lld:pubmed |
| pubmed-article:1695626 | pubmed:affiliation | Department of Medicine, University of North Carolina School of Medicine, Chapel Hill 27599. | lld:pubmed |
| pubmed-article:1695626 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1695626 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:1695626 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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