Formation of Recombinant Human Procollagen I Heterotrimers in a Baculovirus Expression System
Identifieur interne : 003C69 ( Main/Exploration ); précédent : 003C68; suivant : 003C70Formation of Recombinant Human Procollagen I Heterotrimers in a Baculovirus Expression System
Auteurs : Masahiro Tomita ; Takashi Kitajima ; Katsutoshi YoshizatoSource :
- The Journal of Biochemistry [ 0021-924X ] ; 1997.
Abstract
The present study describes the production of human procollagen I in a baculovirus expression system. Recombinant baculovirus carrying proαl(I) or proα2(I) cDNA was constructed and infected to Sf9 cells. Full-length proαl(I) or proα2(I) chains were synthesized by the cells infected with either of the recombinant viruses. The proαl(I) chains formed pepsin-resistant homotrimers stabilized by interchain disulfide bonds, a small proportion of which was secreted into the culture medium. The proα2(I) chains were not linked into trimers by disulfide bonds and failed to form stable triple helices, although some chains were suggested to exist as dimers or unstable trimers in which only two chains were linked by disulfide bonds. In spite of their non-helicity, the proα2(I) chains were secreted at a higher rate than the proαl(I) chains. Sf9 cells simultaneously synthesized both proαl(I) and proα2(I) chains when the cells were co-infected with the two recombinant viruses. Pepsin-treatment of the product clearly demonstrated the production of procollagen I heterotrimers composed of two proαl(I) chains and one proα2(I) chain, homotrimers of the proαl(I) chains being negligible. This expression system appears to offer a unique means of studying the mechanism of chain association and secretion during procollagen biosynthesis.
Url:
DOI: 10.1093/oxfordjournals.jbchem.a021695
Affiliations:
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Recombinant baculovirus carrying proαl(I) or proα2(I) cDNA was constructed and infected to Sf9 cells. Full-length proαl(I) or proα2(I) chains were synthesized by the cells infected with either of the recombinant viruses. The proαl(I) chains formed pepsin-resistant homotrimers stabilized by interchain disulfide bonds, a small proportion of which was secreted into the culture medium. The proα2(I) chains were not linked into trimers by disulfide bonds and failed to form stable triple helices, although some chains were suggested to exist as dimers or unstable trimers in which only two chains were linked by disulfide bonds. In spite of their non-helicity, the proα2(I) chains were secreted at a higher rate than the proαl(I) chains. Sf9 cells simultaneously synthesized both proαl(I) and proα2(I) chains when the cells were co-infected with the two recombinant viruses. Pepsin-treatment of the product clearly demonstrated the production of procollagen I heterotrimers composed of two proαl(I) chains and one proα2(I) chain, homotrimers of the proαl(I) chains being negligible. This expression system appears to offer a unique means of studying the mechanism of chain association and secretion during procollagen biosynthesis.</div></front></TEI><affiliations><list></list><tree><noCountry><name sortKey="Kitajima, Takashi" sort="Kitajima, Takashi" uniqKey="Kitajima T" first="Takashi" last="Kitajima">Takashi Kitajima</name><name sortKey="Tomita, Masahiro" sort="Tomita, Masahiro" uniqKey="Tomita M" first="Masahiro" last="Tomita">Masahiro Tomita</name><name sortKey="Yoshizato, Katsutoshi" sort="Yoshizato, Katsutoshi" uniqKey="Yoshizato K" first="Katsutoshi" last="Yoshizato">Katsutoshi Yoshizato</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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