Recombinant expression and characterization of a novel fibronectin isoform expressed in cartilaginous tissues |
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Authors: | Kozaki Tomohiro Matsui Yoshito Gu Jianguo Nishiuchi Ryoko Sugiura Nobuo Kimata Koji Ozono Keiichi Yoshikawa Hideki Sekiguchi Kiyotoshi |
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Affiliation: | Division of Protein Chemistry, Institute for Protein Research, Graduate School of Medicine, Osaka University, Suita, Japan. |
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Abstract: | 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 alpha5beta1, 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. |
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