Recombinant Expression and Characterization of a Novel Fibronectin Isoform Expressed in Cartilaginous Tissues
| Autor: | Hideki Yoshikawa, Tomohiro Kozaki, Ryoko Nishiuchi, Kiyotoshi Sekiguchi, Keiichi Ozono, Jianguo Gu, Nobuo Sugiura, Yoshito Matsui, Koji Kimata |
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| Jazyk: | angličtina |
| Rok vydání: | 2003 |
| Předmět: |
Gene isoform
DNA Complementary RNA Splicing Immunoblotting CHO Cells Matrix (biology) Transfection Biochemistry Cell Line Mice chemistry.chemical_compound Cricetinae Cell Adhesion Cartilaginous Tissue medicine Animals Protein Isoforms Chondroitin Disulfides Chondroitin sulfate Fluorescent Antibody Technique Indirect Cell adhesion Molecular Biology Cells Cultured Glycosaminoglycans Dose-Response Relationship Drug Models Genetic biology Heparin Chemistry Cartilage Chondroitin Sulfates Antibodies Monoclonal Cell Biology Molecular biology Recombinant Proteins Fibronectins Fibronectin medicine.anatomical_structure biology.protein RNA Electrophoresis Polyacrylamide Gel Proteoglycans Peptides Integrin alpha5beta1 Protein Binding |
| Zdroj: | Journal of Biological Chemistry. 278(50):50546-50553 |
| ISSN: | 1083-351X |
| Popis: | This research was originally published in the Journal of Biological Chemistry. Tomohiro Kozaki, Yoshito Matsui, Jianguo Gu, Ryoko Nishiuchi, Nobuo Sugiura, Koji Kimata, Keiichi Ozono, Hideki Yoshikawa and Kiyotoshi Sekiguchi. Recombinant Expression and Characterization of a Novel Fibronectin Isoform Expressed in Cartilaginous Tissues. J. Biol. Chem. 2003; 278: 50546-50553 © the American Society for Biochemistry and Molecular Biology A novel fibronectin (FN) isoform lacking the segment from IIICS (type III connecting segment) through the I-10 module is expressed predominantly in normal cartilaginous tissues. We expressed and purified recombinant cartilage-type FN using a mammalian expression system and characterized its molecular and biological properties. Although FNs have been shown to be secreted as disulfide-bonded dimers, cartilage-type FN was secreted mainly as a monomer. It was less potent than plasma-type FN in promoting cell adhesion and binding to integrin α5β1, although it was more active than plasma-type FN in binding to chondroitin sulfate E. When added exogenously, cartilage-type FN was poorly assembled into the fibrillar FN matrix, mostly because of its monomeric structure. Given that cartilage is characterized by its non-fibrillar matrix with abundant chondroitin sulfate-containing proteoglycans, it is likely that cartilage-type FN has evolved to adapt itself to the non-fibrillar structure of the cartilage matrix through acquisition of a novel mechanism of alternative pre-mRNA splicing. |
| Databáze: | OpenAIRE |
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