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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2 Pt 1
|
| pubmed:dateCreated |
1998-9-16
|
| 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.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Heparin,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin-Like Growth Factor Binding...,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin-Like Growth Factor I,
http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Plasminogen,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
0002-9513
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
275
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
E321-31
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:9688635-Amino Acid Sequence,
pubmed-meshheading:9688635-Animals,
pubmed-meshheading:9688635-Base Sequence,
pubmed-meshheading:9688635-Binding Sites,
pubmed-meshheading:9688635-CHO Cells,
pubmed-meshheading:9688635-Cricetinae,
pubmed-meshheading:9688635-DNA, Complementary,
pubmed-meshheading:9688635-Gene Library,
pubmed-meshheading:9688635-Heparin,
pubmed-meshheading:9688635-Humans,
pubmed-meshheading:9688635-Insulin-Like Growth Factor Binding Protein 3,
pubmed-meshheading:9688635-Insulin-Like Growth Factor I,
pubmed-meshheading:9688635-Kinetics,
pubmed-meshheading:9688635-Molecular Sequence Data,
pubmed-meshheading:9688635-Mutagenesis, Site-Directed,
pubmed-meshheading:9688635-Oligodeoxyribonucleotides,
pubmed-meshheading:9688635-Placenta,
pubmed-meshheading:9688635-Plasminogen,
pubmed-meshheading:9688635-Recombinant Proteins,
pubmed-meshheading:9688635-Transfection
|
| pubmed:year |
1998
|
| pubmed:articleTitle |
Plasminogen binds the heparin-binding domain of insulin-like growth factor-binding protein-3.
|
| pubmed:affiliation |
Orthopaedic Research Laboratory, Allegheny University of Health Sciences, Pittsburgh, Pennsylvania 15212, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|