Veit, Guido; Hansen, Uwe; Keene, Douglas R; Bruckner, Peter; Chiquet-Ehrismann, Ruth; Chiquet, Matthias; Koch, Manuel (2006). Collagen XII interacts with avian tenascin-X through its NC3 domain. Journal of biological chemistry, 281(37), pp. 27461-70. Bethesda, Md.: American Society for Biochemistry and Molecular Biology 10.1074/jbc.M603147200
Full text not available from this repository. (Request a copy)Large oligomeric proteins often contain several binding sites for different molecules and can therefore induce formation of larger protein complexes. Collagen XII, a multidomain protein with a small collagenous region, interacts with fibrillar collagens through its C-terminal region. However, no interactions to other extracellular proteins have been identified involving the non-collagenous N-terminal NC3 domain. To further elucidate the components of protein complexes present close to collagen fibrils, different extracellular matrix proteins were tested for interaction in a solid phase assay. Binding to the NC3 domain of collagen XII was found for the avian homologue of tenascin-X that in humans is linked to Ehlers-Danlos disease. The binding was further characterized by surface plasmon resonance spectroscopy and supported by immunohistochemical co-localization in chick and mouse tissue. On the ultrastructural level, detection of collagen XII and tenascin-X by immunogold labeling confirmed this finding.
Item Type: |
Journal Article (Original Article) |
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Division/Institute: |
04 Faculty of Medicine > Pre-clinic Human Medicine > BioMedical Research (DBMR) > DBMR Forschung Mu35 > Center of Regenerative Medicine for Skeletal Tissues [discontinued] 04 Faculty of Medicine > Pre-clinic Human Medicine > BioMedical Research (DBMR) > DBMR Forschung Mu35 > Center of Regenerative Medicine for Skeletal Tissues [discontinued] |
UniBE Contributor: |
Chiquet, Matthias |
ISSN: |
0021-9258 |
ISBN: |
16861231 |
Publisher: |
American Society for Biochemistry and Molecular Biology |
Language: |
English |
Submitter: |
Factscience Import |
Date Deposited: |
04 Oct 2013 14:45 |
Last Modified: |
05 Dec 2022 14:14 |
Publisher DOI: |
10.1074/jbc.M603147200 |
PubMed ID: |
16861231 |
Web of Science ID: |
000240397700073 |
URI: |
https://boris.unibe.ch/id/eprint/18532 (FactScience: 720) |
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