| pubmed-article:7512304 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7512304 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:7512304 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:7512304 | lifeskim:mentions | umls-concept:C0222677 | lld:lifeskim |
| pubmed-article:7512304 | lifeskim:mentions | umls-concept:C0007613 | lld:lifeskim |
| pubmed-article:7512304 | lifeskim:mentions | umls-concept:C0074825 | lld:lifeskim |
| pubmed-article:7512304 | lifeskim:mentions | umls-concept:C0205307 | lld:lifeskim |
| pubmed-article:7512304 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
| pubmed-article:7512304 | lifeskim:mentions | umls-concept:C0212523 | lld:lifeskim |
| pubmed-article:7512304 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:7512304 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:7512304 | pubmed:dateCreated | 1994-5-11 | lld:pubmed |
| pubmed-article:7512304 | pubmed:abstractText | Insulin-like growth factor binding protein 4 (IGFBP-4) is secreted by normal human osteoblast-like cells (hOB) and is a potent inhibitor of insulin-like growth factor (IGF) action in vitro. In previous studies, IGF treatment of hOB in culture led to markedly reduced medium levels of IGFBP-4 as detected by western ligand blotting. In the present study, incubation of hOB-conditioned medium (hOB-CM) with IGF under cell-free conditions resulted in a similar loss of IGFBP-4. Both IGF-I and IGF-II were capable of inducing a decrease in IGFBP-4; however, IGF-II was more effective. When the six characterized IGFBP were added to hOB-CM, only IGFBP-4 disappeared in response to IGF-II addition. This IGF-regulated loss of IGFBP-4 was inhibited by metalloproteinase inhibitors and appeared to be due to a proteinase that cleaved IGFBP-4 in 18 and 14 kD fragments identified by western immunoblotting. Conditioned media from eight of eight different donor hOB lines tested exhibited IGFBP-4 proteinase activity. To assess the biologic consequences of IGF-II-induced IGFBP-4 proteolysis, we treated hOB with IGF-II for 5 h, which decreased medium IGF-BP-4 by 70%, and then measured IGF-I and insulin stimulation of [3H]thymidine incorporation. IGF-II itself was not mitogenic and had no effect on insulin-stimulated [3H]thymidine incorporation. However, pretreatment of cultured hOB with IGF-II enhanced IGF-I-stimulated [3H]thymidine incorporation threefold.(ABSTRACT TRUNCATED AT 250 WORDS) | lld:pubmed |
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| pubmed-article:7512304 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7512304 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7512304 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7512304 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7512304 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:7512304 | pubmed:issn | 0884-0431 | lld:pubmed |
| pubmed-article:7512304 | pubmed:author | pubmed-author:RiggsB LBL | lld:pubmed |
| pubmed-article:7512304 | pubmed:author | pubmed-author:ConoverC ACA | lld:pubmed |
| pubmed-article:7512304 | pubmed:author | pubmed-author:KieferM CMC | lld:pubmed |
| pubmed-article:7512304 | pubmed:author | pubmed-author:DurhamS KSK | lld:pubmed |
| pubmed-article:7512304 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7512304 | pubmed:volume | 9 | lld:pubmed |
| pubmed-article:7512304 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7512304 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7512304 | pubmed:pagination | 111-7 | lld:pubmed |
| pubmed-article:7512304 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:7512304 | pubmed:meshHeading | pubmed-meshheading:7512304-... | lld:pubmed |
| pubmed-article:7512304 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:7512304 | pubmed:articleTitle | Regulation of insulin-like growth factor binding protein 4 by a specific insulin-like growth factor binding protein 4 proteinase in normal human osteoblast-like cells: implications in bone cell physiology. | lld:pubmed |
| pubmed-article:7512304 | pubmed:affiliation | Endocrine Research Unit, Mayo Clinic, Rochester, Minnesota. | lld:pubmed |
| pubmed-article:7512304 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7512304 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7512304 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:5069 | entrezgene:pubmed | pubmed-article:7512304 | lld:entrezgene |
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