pubmed-article:9688635 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9688635 | lifeskim:mentions | umls-concept:C0018270 | lld:lifeskim |
pubmed-article:9688635 | lifeskim:mentions | umls-concept:C0032140 | lld:lifeskim |
pubmed-article:9688635 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:9688635 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
pubmed-article:9688635 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
pubmed-article:9688635 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
pubmed-article:9688635 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
pubmed-article:9688635 | pubmed:issue | 2 Pt 1 | lld:pubmed |
pubmed-article:9688635 | pubmed:dateCreated | 1998-9-16 | lld:pubmed |
pubmed-article:9688635 | pubmed:abstractText | Limited proteolysis lowers affinity of insulin-like growth factor (IGF)-binding protein (IGFBP)-3 for bound IGFs, resulting in greater IGF bioavailability. Plasmin is one of many proteases that cleave IGFBP-3, and the plasmin system may regulate IGFBP-3 proteolysis and IGF bioavailability in cultured cells in vitro. A role for the plasmin system in IGFBP-3 proteolysis in vivo is suggested by data presented here showing that IGFBP-3 binds plasminogen (Pg; Glu-Pg) with a dissociation constant (Kd) ranging from 1.43 to 3.12 nM. IGF-I and Glu-Pg do not compete for IGFBP-3 binding; instead, the binary IGFBP-3/Glu-Pg complex binds IGF-I with high affinity (Kd = 0. 47 nM) to form a ternary complex. Competitive binding studies suggest that the kringle 1, 4, and 5 domains of Glu-Pg and the heparin-binding domain of IGFBP-3 participate in forming the IGFBP-3/Glu-Pg complex, and other studies show that Glu-Pg in this complex is activated at a normal rate by tissue Pg activator. Importantly, IGFBP-3/Glu-Pg complexes were detected in both human citrate plasma and serum, indicating that these complexes exist in vivo. Binding of IGFBP-3 to Glu-Pg in vivo suggests how Glu-Pg activation can specifically lead to IGFBP-3 proteolysis with subsequent release of IGFs to local target tissues. | lld:pubmed |
pubmed-article:9688635 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9688635 | pubmed:language | eng | lld:pubmed |
pubmed-article:9688635 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9688635 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9688635 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9688635 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9688635 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9688635 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9688635 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9688635 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9688635 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9688635 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9688635 | pubmed:month | Aug | lld:pubmed |
pubmed-article:9688635 | pubmed:issn | 0002-9513 | lld:pubmed |
pubmed-article:9688635 | pubmed:author | pubmed-author:HayesJ DJD | lld:pubmed |
pubmed-article:9688635 | pubmed:author | pubmed-author:CampbellP GPG | lld:pubmed |
pubmed-article:9688635 | pubmed:author | pubmed-author:PowellD RDR | lld:pubmed |
pubmed-article:9688635 | pubmed:author | pubmed-author:DurhamS KSK | lld:pubmed |
pubmed-article:9688635 | pubmed:author | pubmed-author:SuwanichkulAA | lld:pubmed |
pubmed-article:9688635 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9688635 | pubmed:volume | 275 | lld:pubmed |
pubmed-article:9688635 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9688635 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9688635 | pubmed:pagination | E321-31 | lld:pubmed |
pubmed-article:9688635 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
pubmed-article:9688635 | pubmed:meshHeading | pubmed-meshheading:9688635-... | lld:pubmed |
pubmed-article:9688635 | pubmed:meshHeading | pubmed-meshheading:9688635-... | lld:pubmed |
pubmed-article:9688635 | pubmed:meshHeading | pubmed-meshheading:9688635-... | lld:pubmed |
pubmed-article:9688635 | pubmed:meshHeading | pubmed-meshheading:9688635-... | lld:pubmed |
pubmed-article:9688635 | pubmed:meshHeading | pubmed-meshheading:9688635-... | lld:pubmed |
pubmed-article:9688635 | pubmed:meshHeading | pubmed-meshheading:9688635-... | lld:pubmed |
pubmed-article:9688635 | pubmed:meshHeading | pubmed-meshheading:9688635-... | lld:pubmed |
pubmed-article:9688635 | pubmed:meshHeading | pubmed-meshheading:9688635-... | lld:pubmed |
pubmed-article:9688635 | pubmed:meshHeading | pubmed-meshheading:9688635-... | lld:pubmed |
pubmed-article:9688635 | pubmed:meshHeading | pubmed-meshheading:9688635-... | lld:pubmed |
pubmed-article:9688635 | pubmed:meshHeading | pubmed-meshheading:9688635-... | lld:pubmed |
pubmed-article:9688635 | pubmed:meshHeading | pubmed-meshheading:9688635-... | lld:pubmed |
pubmed-article:9688635 | pubmed:meshHeading | pubmed-meshheading:9688635-... | lld:pubmed |
pubmed-article:9688635 | pubmed:meshHeading | pubmed-meshheading:9688635-... | lld:pubmed |
pubmed-article:9688635 | pubmed:meshHeading | pubmed-meshheading:9688635-... | lld:pubmed |
pubmed-article:9688635 | pubmed:meshHeading | pubmed-meshheading:9688635-... | lld:pubmed |
pubmed-article:9688635 | pubmed:meshHeading | pubmed-meshheading:9688635-... | lld:pubmed |
pubmed-article:9688635 | pubmed:meshHeading | pubmed-meshheading:9688635-... | lld:pubmed |
pubmed-article:9688635 | pubmed:meshHeading | pubmed-meshheading:9688635-... | lld:pubmed |
pubmed-article:9688635 | pubmed:meshHeading | pubmed-meshheading:9688635-... | lld:pubmed |
pubmed-article:9688635 | pubmed:year | 1998 | lld:pubmed |
pubmed-article:9688635 | pubmed:articleTitle | Plasminogen binds the heparin-binding domain of insulin-like growth factor-binding protein-3. | lld:pubmed |
pubmed-article:9688635 | pubmed:affiliation | Orthopaedic Research Laboratory, Allegheny University of Health Sciences, Pittsburgh, Pennsylvania 15212, USA. | lld:pubmed |
pubmed-article:9688635 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9688635 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
entrez-gene:3486 | entrezgene:pubmed | pubmed-article:9688635 | lld:entrezgene |
entrez-gene:5340 | entrezgene:pubmed | pubmed-article:9688635 | lld:entrezgene |
http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:9688635 | lld:entrezgene |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9688635 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9688635 | lld:pubmed |