The shed ectodomain of type XIII collagen associates with the fibrillar fibronectin matrix and may interfere with its assembly in vitro
| Autor: | Raija Sormunen, Timo Väisänen, Taina Pihlajaniemi, Hongmin Tu, Päivi Pirilä, Marja-Riitta Väisänen |
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| Rok vydání: | 2005 |
| Předmět: |
Matrix (biology)
Collagen Type XIII Biochemistry law.invention Extracellular matrix law Cricetinae Animals Humans Molecular Biology Cells Cultured biology Chemistry Cell Biology Transmembrane protein In vitro Extracellular Matrix Fibronectins Protein Structure Tertiary Up-Regulation Cell biology Fibronectin Collagen type I alpha 1 Ectodomain Recombinant DNA biology.protein Cattle Gene Deletion Procollagen Research Article Protein Binding |
| Zdroj: | Biochemical Journal. 393:43-50 |
| ISSN: | 1470-8728 0264-6021 |
| Popis: | Type XIII collagen is a transmembrane collagen, which is known to exist also as a soluble variant due to ectodomain shedding. Earlier studies with the recombinant ectodomain have shown it to interact in vitro with a number of extracellular matrix proteins, e.g. Fn (fibronectin). In view of its strong binding to Fn, we examined in the present study whether the released soluble ectodomain can bind to the fibrillar Fn matrix under cell-culture conditions and, if so, influence its assembly. In this study, we demonstrate that the type XIII collagen ectodomain of mammalian cells can associate with Fn fibres and may eventually hamper incorporation of the fibrillar Fn meshwork. The association between type XIII collagen and Fn was implicated to be mediated by the C-terminal end of type XIII collagen and the N-terminal end of Fn. The results presented here imply that the shedding of the type XIII collagen ectodomain results in a biologically active molecule capable of remodelling the structure of the pericellular matrix. |
| Databáze: | OpenAIRE |
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