| pubmed-article:12735930 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12735930 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:12735930 | lifeskim:mentions | umls-concept:C0009325 | lld:lifeskim |
| pubmed-article:12735930 | lifeskim:mentions | umls-concept:C0123707 | lld:lifeskim |
| pubmed-article:12735930 | lifeskim:mentions | umls-concept:C0242210 | lld:lifeskim |
| pubmed-article:12735930 | pubmed:issue | 2-3 | lld:pubmed |
| pubmed-article:12735930 | pubmed:dateCreated | 2003-5-8 | lld:pubmed |
| pubmed-article:12735930 | 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. | lld:pubmed |
| pubmed-article:12735930 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12735930 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12735930 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12735930 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12735930 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12735930 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12735930 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12735930 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12735930 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12735930 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12735930 | pubmed:issn | 1096-6374 | lld:pubmed |
| pubmed-article:12735930 | pubmed:author | pubmed-author:CohenPinchasP | lld:pubmed |
| pubmed-article:12735930 | pubmed:author | pubmed-author:LiuBingrongB | lld:pubmed |
| pubmed-article:12735930 | pubmed:author | pubmed-author:WeinzimerStua... | lld:pubmed |
| pubmed-article:12735930 | pubmed:author | pubmed-author:GibsonTara... | lld:pubmed |
| pubmed-article:12735930 | pubmed:author | pubmed-author:MascarenhasDe... | lld:pubmed |
| pubmed-article:12735930 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12735930 | pubmed:volume | 13 | lld:pubmed |
| pubmed-article:12735930 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12735930 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12735930 | pubmed:pagination | 89-97 | lld:pubmed |
| pubmed-article:12735930 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:12735930 | pubmed:meshHeading | pubmed-meshheading:12735930... | lld:pubmed |
| pubmed-article:12735930 | pubmed:meshHeading | pubmed-meshheading:12735930... | lld:pubmed |
| pubmed-article:12735930 | pubmed:articleTitle | Type Ialpha collagen is an IGFBP-3 binding protein. | lld:pubmed |
| pubmed-article:12735930 | pubmed:affiliation | David Geffen School of Medicine at UCLA, Los Angeles, CA, USA | lld:pubmed |
| pubmed-article:12735930 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12735930 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:12735930 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12735930 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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