pubmed-article:8265816 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8265816 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:8265816 | lifeskim:mentions | umls-concept:C0026336 | lld:lifeskim |
pubmed-article:8265816 | lifeskim:mentions | umls-concept:C0229613 | lld:lifeskim |
pubmed-article:8265816 | lifeskim:mentions | umls-concept:C1522496 | lld:lifeskim |
pubmed-article:8265816 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
pubmed-article:8265816 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:8265816 | lifeskim:mentions | umls-concept:C0018270 | lld:lifeskim |
pubmed-article:8265816 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
pubmed-article:8265816 | lifeskim:mentions | umls-concept:C0018284 | lld:lifeskim |
pubmed-article:8265816 | lifeskim:mentions | umls-concept:C0242210 | lld:lifeskim |
pubmed-article:8265816 | lifeskim:mentions | umls-concept:C0023688 | lld:lifeskim |
pubmed-article:8265816 | pubmed:issue | 1-2 | lld:pubmed |
pubmed-article:8265816 | pubmed:dateCreated | 1994-1-27 | lld:pubmed |
pubmed-article:8265816 | pubmed:abstractText | Human IM-9 lymphoblasts bind growth hormone (hGH) and insulin-like growth factors (IGFs). We have systematically examined the IM-9 cells as a valuable model of the interaction of hGH and the IGFs at the cellular level. Cells were cultured in medium with 10% serum and for a subset of experiments cultured in serum-free medium. Binding of [125I]hGH and [125I]IGF-I and -II to intact IM-9 cells was measured: unlabeled hGH inhibited binding of [125I]hGH (half max. 20 ng/ml). Binding of [125I]IGF-I was inhibited by IGF-I (half max. 7.5 ng/ml), IGF-II (half max. 60 ng/ml), and insulin and anti IGF-I receptor antibody (alpha IR3). [125I]IGF-II was inhibited by IGF-II (half max. 15 ng/ml), IGF-I (half max. 500 ng/ml), insulin (half max. 250 ng/ml) but not by alpha IR3. Crosslinking experiments with [125I]IGF-II and DSS as the crosslinking agent and analysis of radioligand-receptor complexes by SDS-PAGE under reducing conditions revealed that [125I]IGF-II bound to a 250 kDa and a 135 kDa receptor species. The latter possibly represents an insulin-type receptor whereas the 250 kDa species had the characteristics of the IGF-II/M6P receptor. When IM-9 cell conditioned medium was analyzed in ligand blotting experiments with either [125I]IGF-I or -II a 30 kDa IGFBP species was detected on the autoradiographs. Also, IGF-II immunoreactivity (approx. 1 ng/ml medium) was measured in the cell conditioned medium using an IGF-BP blocked RIA employing [125I]IGF-II. In a subset of experiments IM-9 cells were homogenized in 4 M guanidinium-thiocyanate and RNA extracted in 5.7 M CsCl. Denatured RNA was electrophoresed on 0.8% agarose gels and transferred to a nylon membrane, fixed and the blots hybridized with cDNA probes. Probes were labeled with [32P]dCTP using a random prime labeling procedure: a Pst I 700 bp fragment of the human IGF-I cDNA, a 554 bp Pst I-Sal I fragment of the IGF-II cDNA, a 614 bp Pst I fragment of the IGF-I receptor cDNA and a 663 bp Pst I fragment of the IGF-II/M6P receptor. Autoradiographs of Northern blots showed specific hybridization with the IGF-I probe at 3.7 kb and with the IGF-II probe at 5.3 kb. No signal was detected with the IGF-I receptor cDNA probe. Hybridization with the IGF-II/M6P receptor probe yielded a 9 kb RNA species.(ABSTRACT TRUNCATED AT 400 WORDS) | lld:pubmed |
pubmed-article:8265816 | pubmed:language | eng | lld:pubmed |
pubmed-article:8265816 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8265816 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8265816 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8265816 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8265816 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8265816 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8265816 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8265816 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8265816 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8265816 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8265816 | pubmed:month | Oct | lld:pubmed |
pubmed-article:8265816 | pubmed:issn | 0167-0115 | lld:pubmed |
pubmed-article:8265816 | pubmed:author | pubmed-author:YangYY | lld:pubmed |
pubmed-article:8265816 | pubmed:author | pubmed-author:SchwarzH PHP | lld:pubmed |
pubmed-article:8265816 | pubmed:author | pubmed-author:BlumWW | lld:pubmed |
pubmed-article:8265816 | pubmed:author | pubmed-author:KiessWW | lld:pubmed |
pubmed-article:8265816 | pubmed:author | pubmed-author:KesslerUU | lld:pubmed |
pubmed-article:8265816 | pubmed:author | pubmed-author:BarentonBB | lld:pubmed |
pubmed-article:8265816 | pubmed:author | pubmed-author:HoeflichAA | lld:pubmed |
pubmed-article:8265816 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8265816 | pubmed:day | 20 | lld:pubmed |
pubmed-article:8265816 | pubmed:volume | 48 | lld:pubmed |
pubmed-article:8265816 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8265816 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8265816 | pubmed:pagination | 41-53 | lld:pubmed |
pubmed-article:8265816 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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pubmed-article:8265816 | pubmed:year | 1993 | lld:pubmed |
pubmed-article:8265816 | pubmed:articleTitle | Human IM-9 lymphoblasts as a model of the growth hormone-insulin-like growth factor axis: gene expression, and interactions of ligands with receptors and binding proteins. | lld:pubmed |
pubmed-article:8265816 | pubmed:affiliation | Children's Hospital, Department of Paediatric Endocrinology, University of Munich, Germany. | lld:pubmed |
pubmed-article:8265816 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8265816 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |