Collagen XII interacts with avian tenascin-X through its NC3 domain.
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.
Veit
Guido
G
Center for Biochemistry, Department of Dermatology, Medical Faculty, University of Cologne, D-50931 Cologne, Germany, and Shriners Hospital for Children Research Center, Portland, Oregon 97239, USA.
Hansen
Uwe
U
Keene
Douglas R
DR
Bruckner
Peter
P
Chiquet-Ehrismann
Ruth
R
Chiquet
Matthias
M
Koch
Manuel
M
D000818:Animals; D002645:Chickens; D003094:Collagen / Q000737:chemistry; D024082:Collagen Type XII / Q000737:chemistry*; D004535:Ehlers-Danlos Syndrome / Q000378:metabolism; D006493:Heparin / Q000737:chemistry; D006801:Humans; D007150:Immunohistochemistry; D051379:Mice; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D020349:Surface Plasmon Resonance; D019063:Tenascin / Q000737:chemistry*
D024082:Collagen Type XII; D019063:Tenascin; C081865:tenascin X; D006493:Heparin; D003094:Collagen