Molecular structure and tissue distribution of matrilin-3, a filament-forming extracellular matrix protein expressed during skeletal development
| Autor: | Mats Paulsson, Raimund Wagener, Matthias Mörgelin, Andreas R. Klatt, D P Nitsche, Birgit Kobbe |
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| Rok vydání: | 2000 |
| Předmět: |
Protein Conformation
Connective tissue Matrix (biology) Biochemistry Mass Spectrometry Extracellular matrix Mice Chondrocytes medicine Cartilaginous Tissue Perichondrium Animals Matrilin Proteins Electrophoresis Gel Two-Dimensional RNA Messenger Molecular Biology Aggrecan In Situ Hybridization Extracellular Matrix Proteins Bone Development Cartilage Cell Biology Anatomy Costal cartilage Immunohistochemistry Recombinant Proteins Cell biology Rats Microscopy Electron medicine.anatomical_structure Animals Newborn Connective Tissue Cattle Collagen |
| Zdroj: | The Journal of biological chemistry. 275(6) |
| ISSN: | 0021-9258 |
| Popis: | Matrilin-3 is a recently identified member of the superfamily of proteins containing von Willebrand factor A-like domains and is able to form hetero-oligomers with matrilin-1 (cartilage matrix protein) via a C-terminal coiled-coil domain. Full-length matrilin-3 and a fragment lacking the assembly domain were expressed in 293-EBNA cells, purified, and subjected to biochemical characterization. Recombinantly expressed full-length matrilin-3 occurs as monomers, dimers, trimers, and tetramers, as detected by electron microscopy and SDS-polyacrylamide gel electrophoresis, whereas matrilin-3, purified from fetal calf cartilage, forms homotetramers as well as hetero-oligomers of variable stoichiometry with matrilin-1. In the matrix formed by cultured chondrosarcoma cells, matrilin-3 is found in a filamentous, collagen-dependent network connecting cells and in a collagen-independent pericellular network. Affinity-purified antibodies detect matrilin-3 expression in a variety of mouse cartilaginous tissues, such as sternum, articular, and epiphyseal cartilage, and in the cartilage anlage of developing bones. It is found both inside the lacunae and in the interterritorial matrix of the resting, proliferating, hypertrophic, and calcified cartilage zones, whereas the expression is lower in the superficial articular cartilage. In trachea and in costal cartilage of adult mice, an expression was seen in the perichondrium. Furthermore, matrilin-3 is found in bone, and its expression is, therefore, not restricted to chondroblasts and chondrocytes. |
| Databáze: | OpenAIRE |
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