Budde, B and Blumbach, K and Ylostalo, J and Zaucke, F and Ehlen, HWA and Wagener, R and Ala-Kokko, L and Paulsson, M and Bruckner, P and Graessel, Susanne (2005) Altered integration of matrilin-3 into cartilage extracellular matrix in the absence of collagen IX. MOLECULAR AND CELLULAR BIOLOGY, 25 (23). pp. 10465-10478. ISSN 0270-7306, 1098-5549
Full text not available from this repository. (Request a copy)Abstract
The matrilins are a family of four noncollagenous oligomeric extracellular matrix proteins with a modular structure. Matrilins can act as adapters which bridge different macromolecular networks. We therefore investigated the effect of collagen IX deficiency on matrilin-3 integration into cartilage tissues. Mice harboring a deleted Col9a.1 gene lack synthesis of a functional protein and produce cartilage fibrils completely devoid of collagen IX. Newborn collagen IX knockout mice exhibited significantly decreased matrilin-3 and cartilage oligomeric matrix protein (COMP) signals, particularly in the cartilage primordium of vertebral bodies and ribs. In the absence of collagen IX, a substantial amount of matrilin-3 is released into the medium of cultured chondrocytes instead of being integrated into the cell layer as in wild-type and COMP-deficient cells. Gene expression of matrilin-3 is not affected in the absence of collagen IX, but protein extraction from cartilage is greatly facilitated. Matrilin-3 interacts with collagen IX-containing cartilage fibrils, while fibrils from collagen IX knockout mice lack matrilin-3, and COMP-deficient fibrils exhibit an intermediate integration. In summary, the integration of matrilin-3 into cartilage fibrils occurs both by a direct interaction with collagen IX and indirectly with COMP serving as an adapter. Matrilin-3 can be considered as an interface component, capable of interconnecting macromolecular networks and mediating interactions between cartilage fibrils and the extrafibrillar matrix.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | MULTIPLE EPIPHYSEAL DYSPLASIA; COVALENT CROSS-LINKING; SKELETAL DEVELOPMENT; MOLECULAR-STRUCTURE; TISSUE DISTRIBUTION; A-DOMAIN; PROTEIN; FIBRILS; MUTATIONS; DECORIN; |
| Subjects: | 600 Technology > 610 Medical sciences Medicine |
| Divisions: | Medicine > Lehrstuhl für Orthopädie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 20 Apr 2021 11:23 |
| Last Modified: | 20 Apr 2021 11:23 |
| URI: | https://pred.uni-regensburg.de/id/eprint/35380 |
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