pubmed-article:9437240 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9437240 | lifeskim:mentions | umls-concept:C0025936 | lld:lifeskim |
pubmed-article:9437240 | lifeskim:mentions | umls-concept:C0037663 | lld:lifeskim |
pubmed-article:9437240 | lifeskim:mentions | umls-concept:C0037657 | lld:lifeskim |
pubmed-article:9437240 | lifeskim:mentions | umls-concept:C0074825 | lld:lifeskim |
pubmed-article:9437240 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:9437240 | lifeskim:mentions | umls-concept:C0441889 | lld:lifeskim |
pubmed-article:9437240 | lifeskim:mentions | umls-concept:C0021665 | lld:lifeskim |
pubmed-article:9437240 | lifeskim:mentions | umls-concept:C0175630 | lld:lifeskim |
pubmed-article:9437240 | lifeskim:mentions | umls-concept:C1515655 | lld:lifeskim |
pubmed-article:9437240 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:9437240 | pubmed:dateCreated | 1998-2-5 | lld:pubmed |
pubmed-article:9437240 | pubmed:abstractText | To study interactions between insulin-like growth factor-II (IGF-II) and growth hormone (GH) in vivo, we crossed hemizygous transgenic mice carrying phosphoenolpyruvate carboxykinase (PEPCK)-IGF-II fusion genes with hemizygous PEPCK-bovine GH (bGH) transgenic mice. Offspring harbouring both transgenes (IB), the IGF-II transgene (I) or the bGH transgene (B), and non-transgenic littermates (C) were obtained. Blood samples were taken before (end of week 12) and after (end of week 14) the mice had received a diet high in protein and low in carbohydrates to stimulate PEPCK promoter-controlled transgene expression. Mean serum GH concentrations of both B and IB mice corresponded to 900 ng/ml and increased more than twofold (P < 0.001) after 1 week of the high-protein diet. GH concentrations in controls and I mice were less than 20 ng/ml. Serum IGF-II concentrations in I and IB mice were three-to fourfold higher than those in C and B mice. Whereas IGF-II concentrations were not changed by the high-protein diet in the last two groups, serum IGF-II increased significantly in I (P < 0.001) and IB mice (P < 0.05). This increase was significantly (P < 0.05) less pronounced in IB than in C and I mice. Circulating IGF-I concentrations were about twofold (P < 0.001) higher in B and IB than in C and I mice, and showed a tendency to be lower in I than in C and in IB than in B mice when animals were maintained on the standard diet. The high-protein diet did not change circulating IGF-I concentrations in controls and B mice, but resulted in a significant reduction of serum IGF-I concentrations in I (P < 0.05) and IB mice (P < 0.001). Consequently, after PEPCK-IGF-II transgene expression was stimulated, serum IGF-I concentrations were significantly (P < 0.05) lower in I than in C and in IB than in B mice. Serum IGF-binding protein (IGFBP)-2 concentrations were significantly (P < 0.05) higher in I mice than in all other groups when mice were maintained on the standard diet, with a tendency to reduced IGFBP-2 concentrations in B mice. After the high-protein diet, serum IGFBP-2 concentrations did not change in C and I mice, but increased by two- to threefold in B and IB mice (P < 0.001). Serum IGFBP-3 concentrations tended to be greater in B and IB than in C and I mice, but these differences were mostly not significant. IGFBP-4 concentrations were significantly (P < 0.001) increased by GH overproduction in B and IB mice. Our data suggest that the reduction in circulating IGF-I concentrations by increased IGF-II is most probably due to the limited serum IGF binding capacity and the short half-life of free IGFs, rather than to a reduction in GH-dependent IGF-I production. Effects of GH overproduction on serum IGFBP-2 concentrations depend on dietary factors and may be both inhibitory and stimulatory. | lld:pubmed |
pubmed-article:9437240 | pubmed:language | eng | lld:pubmed |
pubmed-article:9437240 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9437240 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9437240 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9437240 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9437240 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9437240 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9437240 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9437240 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9437240 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9437240 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9437240 | pubmed:month | Dec | lld:pubmed |
pubmed-article:9437240 | pubmed:issn | 0804-4643 | lld:pubmed |
pubmed-article:9437240 | pubmed:author | pubmed-author:WolfEE | lld:pubmed |
pubmed-article:9437240 | pubmed:author | pubmed-author:BlumW FWF | lld:pubmed |
pubmed-article:9437240 | pubmed:author | pubmed-author:BresAA | lld:pubmed |
pubmed-article:9437240 | pubmed:author | pubmed-author:StrasburgerC... | lld:pubmed |
pubmed-article:9437240 | pubmed:author | pubmed-author:Dressendörfer... | lld:pubmed |
pubmed-article:9437240 | pubmed:author | pubmed-author:BlackburnAA | lld:pubmed |
pubmed-article:9437240 | pubmed:author | pubmed-author:ErhardMM | lld:pubmed |
pubmed-article:9437240 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9437240 | pubmed:volume | 137 | lld:pubmed |
pubmed-article:9437240 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9437240 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9437240 | pubmed:pagination | 701-8 | lld:pubmed |
pubmed-article:9437240 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
pubmed-article:9437240 | pubmed:meshHeading | pubmed-meshheading:9437240-... | lld:pubmed |
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pubmed-article:9437240 | pubmed:meshHeading | pubmed-meshheading:9437240-... | lld:pubmed |
pubmed-article:9437240 | pubmed:year | 1997 | lld:pubmed |
pubmed-article:9437240 | pubmed:articleTitle | Interactions of insulin-like growth factor (IGF)-II and growth hormone in vivo: circulating levels of IGF-I and IGF-binding proteins in transgenic mice. | lld:pubmed |
pubmed-article:9437240 | pubmed:affiliation | Lehrstuhl für Molekulare Tierzucht und Haustiergenetik/Genzentrum, Ludwig-Maximilians-Universität, München, Germany. | lld:pubmed |
pubmed-article:9437240 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9437240 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9437240 | lld:pubmed |