Abstract
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.
Highlights
The integrity of extracellular matrix is maintained by supramolecular networks assembled by a large variety of matrix macromolecules
The isoforms differ in their histological and developmental distribution: the large forms XIIA-1 and XIIA-2 are preferably expressed during embryonic stages, whereas the expression of the small forms persists in adult tissues [7]
Collagen XII belongs to the subfamily of collagens designated as fibril-associated collagens with interrupted triple helices (FACITs)
Summary
The integrity of extracellular matrix is maintained by supramolecular networks assembled by a large variety of matrix macromolecules. Contains the Binding Site for Tenascin-X—Collagen XII interacts with collagen I-containing fibrils through its collagenous domain [8].
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