Source:http://linkedlifedata.com/resource/pubmed/id/12735930
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2-3
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pubmed:dateCreated |
2003-5-8
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pubmed:abstractText |
Insulin-like growth factor (IGF) binding protein-3 (IGFBP-3) possesses both growth-inhibitory and -potentiating effects on cells, which are independent of IGF action and mediated through specific IGFBP-3 binding proteins/receptors located at the cell membrane, cytosol, or nuclear compartments as well as in the extracellular matrix. We here characterized type Ialpha collagen as one of these IGFBP-3 binding proteins. Human serum was fractionated over an IGFBP-3 affinity column, and bands at 70-100 kDa were eluted as IGFBP-3 ligands. The 100-kDa band was extracted, subjected to N-terminal amino acid sequencing, and identified through database searching as the N-terminal chain of type Ialpha collagen protein. In a separate screening approach, using a yeast two-hybrid system, we cloned the type Ialpha collagen cDNA from a human liver cDNA library as an IGFBP-3 protein partner. Anti-IGFBP-3 antibodies co-immunoprecipitated type Ialpha collagen and IGFBP-3 from the conditioned media of human fibroblasts and vice versa. We demonstrated through ligand dot blot analysis that type Ialpha collagen binds IGFBP-3. IGFBP-3 mutants, with altered sequence at the nuclear localization sequence, bound type Ialpha collagen poorly. Western immunoblot showed that type Ialpha collagen binds only IGFBP-3 but not IGF-I, suggesting an IGF-I-independent mechanism of this interaction. Physiological effects of IGFBP-3-collagen interactions may include modulation of cell adhesion and migration.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Collagen Type I,
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/Nuclear Localization Signals
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pubmed:status |
MEDLINE
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pubmed:issn |
1096-6374
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
13
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
89-97
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:12735930-Binding Sites,
pubmed-meshheading:12735930-Cell Movement,
pubmed-meshheading:12735930-Cells, Cultured,
pubmed-meshheading:12735930-Collagen Type I,
pubmed-meshheading:12735930-Fibroblasts,
pubmed-meshheading:12735930-Humans,
pubmed-meshheading:12735930-Insulin-Like Growth Factor Binding Protein 3,
pubmed-meshheading:12735930-Insulin-Like Growth Factor I,
pubmed-meshheading:12735930-Mutation,
pubmed-meshheading:12735930-Nuclear Localization Signals,
pubmed-meshheading:12735930-Precipitin Tests,
pubmed-meshheading:12735930-Protein Binding,
pubmed-meshheading:12735930-Two-Hybrid System Techniques,
pubmed-meshheading:12735930-Yeasts
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pubmed:articleTitle |
Type Ialpha collagen is an IGFBP-3 binding protein.
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pubmed:affiliation |
David Geffen School of Medicine at UCLA, Los Angeles, CA, USA
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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