| pubmed-article:12719415 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12719415 | lifeskim:mentions | umls-concept:C0330390 | lld:lifeskim |
| pubmed-article:12719415 | lifeskim:mentions | umls-concept:C0040300 | lld:lifeskim |
| pubmed-article:12719415 | lifeskim:mentions | umls-concept:C0009325 | lld:lifeskim |
| pubmed-article:12719415 | lifeskim:mentions | umls-concept:C0752265 | lld:lifeskim |
| pubmed-article:12719415 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:12719415 | lifeskim:mentions | umls-concept:C0231441 | lld:lifeskim |
| pubmed-article:12719415 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:12719415 | lifeskim:mentions | umls-concept:C1511539 | lld:lifeskim |
| pubmed-article:12719415 | pubmed:issue | 27 | lld:pubmed |
| pubmed-article:12719415 | pubmed:dateCreated | 2003-6-30 | lld:pubmed |
| pubmed-article:12719415 | pubmed:abstractText | Transforming growth factor-beta induced gene-h3 (betaig-h3) was found to co-purify with collagen VI microfibrils, extracted from developing fetal ligament, after equilibrium density gradient centrifugation under both nondenaturing and denaturing conditions. Analysis of the collagen VI fraction from the non-denaturing gradient by gel electrophoresis under non-reducing conditions revealed the present of a single high molecular weight band that immunostained for both collagen VI and betaig-h3. When the fraction was analyzed under reducing conditions, collagen VI alpha chains and betaig-h3 were the only species evident. The results indicated that betaig-h3 is associated with collagen VI in tissues by reducible covalent bonding, presumably disulfide bridges. Rotary shadowing and immunogold staining of the collagen VI microfibrils and isolated tetramers indicated that betaig-h3 was specifically and periodically associated with the double-beaded region of many of the microfibrils and that this covalent binding site was located in or near the amino-terminal globular domain of the collagen VI molecule. Using solid phase and co-immunoprecipitation assays, recombinant betaig-h3 was found to bind both native and pepsin-treated collagen VI but not individual pepsin-collagen VI alpha chains. Blocking experiments indicated that the major in vitro betaig-h3 binding site was located in the pepsin-resistant region of collagen VI. In contrast to the tissue situation, the in vitro interaction had the characteristics of a reversible non-covalent interaction, and the Kd was measured as 1.63 x 10(-8) m. Rotary shadowing of immunogold-labeled complexes of recombinant betaig-h3 and pepsin-collagen VI indicated that the in vitro betaig-h3 binding site was located close to the amino-terminal end of the collagen VI triple helix. The evidence indicates that collagen VI may contain distinct covalent and non-covalent binding sites for betaig-h3, although the possibility that both interactions use the same binding region is discussed. Overall the study supports the concept that betaig-h3 is extensively associated with collagen VI in some tissues and that it plays an important modulating role in collagen VI microfibril function. | lld:pubmed |
| pubmed-article:12719415 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12719415 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12719415 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12719415 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12719415 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12719415 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12719415 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:12719415 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:12719415 | pubmed:author | pubmed-author:ReinbothBetty... | lld:pubmed |
| pubmed-article:12719415 | pubmed:author | pubmed-author:HanssenEricE | lld:pubmed |
| pubmed-article:12719415 | pubmed:author | pubmed-author:GibsonMark... | lld:pubmed |
| pubmed-article:12719415 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12719415 | pubmed:day | 4 | lld:pubmed |
| pubmed-article:12719415 | pubmed:volume | 278 | lld:pubmed |
| pubmed-article:12719415 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12719415 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12719415 | pubmed:pagination | 24334-41 | lld:pubmed |
| pubmed-article:12719415 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:12719415 | pubmed:meshHeading | pubmed-meshheading:12719415... | lld:pubmed |
| pubmed-article:12719415 | pubmed:meshHeading | pubmed-meshheading:12719415... | lld:pubmed |
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| pubmed-article:12719415 | pubmed:meshHeading | pubmed-meshheading:12719415... | lld:pubmed |
| pubmed-article:12719415 | pubmed:meshHeading | pubmed-meshheading:12719415... | lld:pubmed |
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| pubmed-article:12719415 | pubmed:meshHeading | pubmed-meshheading:12719415... | lld:pubmed |
| pubmed-article:12719415 | pubmed:meshHeading | pubmed-meshheading:12719415... | lld:pubmed |
| pubmed-article:12719415 | pubmed:meshHeading | pubmed-meshheading:12719415... | lld:pubmed |
| pubmed-article:12719415 | pubmed:meshHeading | pubmed-meshheading:12719415... | lld:pubmed |
| pubmed-article:12719415 | pubmed:meshHeading | pubmed-meshheading:12719415... | lld:pubmed |
| pubmed-article:12719415 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12719415 | pubmed:articleTitle | Covalent and non-covalent interactions of betaig-h3 with collagen VI. Beta ig-h3 is covalently attached to the amino-terminal region of collagen VI in tissue microfibrils. | lld:pubmed |
| pubmed-article:12719415 | pubmed:affiliation | Department of Pathology, University of Adelaide, South Australia, 5005, Australia. | lld:pubmed |
| pubmed-article:12719415 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12719415 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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