Linked Life Data

11104702

Source:http://linkedlifedata.com/resource/pubmed/id/11104702

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pubmed-article:11104702pubmed:abstractTextWe have reported previously on the expression of recombinant human type X collagen (hrColX) in HEK 293 and HT 1080 cells by using the eukaryotic expression vector pCMVsis (in which CMV stands for cytomegalovirus). Several stably transfected clones secreted full-length triple-helical hrColX molecules in large amounts, but the secreted collagen was underhydroxylated, with a hydroxyproline-to-proline ratio of 0.25 and a melting temperature (T(m)) of 31 degrees C. By comparison, native chicken type X procollagen has a T(m) of 46 degrees C. To stabilize the triple helix of hrColX, an hrColX-expressing clone (A6/16) was co-transfected with both alpha and beta subunits of human prolyl 4-hydroxylase. Clones were selected that secreted proalpha1(X) collagen chains with an apparent molecular mass of 75 kDa and an increased hydroxyproline-to-proline ratio of close to 0.5. As a result of enhanced prolyl hydroxylation, the T(m) of the hrColX was increased to 41 degrees C as measured by CD analysis at various temperatures. The CD spectra indicated a minimum ellipticity at 198 nm and a peak at 225 nm at 20 degrees C, confirming the presence of a triple helix. The same T(m) of 41 degrees C was measured for the triple-helical core fragments of hrColX of 60-65 kDa that were retained after brief digestion with chymotrypsin/trypsin at increasing temperatures. This shows that the human cell line HEK-293 is suitable for the simultaneous expression of three genes and the stable production of substantial amounts of recombinant, fully hydroxylated type X collagen over several years.lld:pubmed
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pubmed-article:11104702pubmed:articleTitleCoexpression of alpha and beta subunits of prolyl 4-hydroxylase stabilizes the triple helix of recombinant human type X collagen.lld:pubmed
pubmed-article:11104702pubmed:affiliationDepartment of Experimental Medicine I, Nikolaus-Fiebiger Center für Molecular Medicine, University of Erlangen-Nuremberg, Glückstrasse 6, D-91054 Erlangen, Germany.lld:pubmed
pubmed-article:11104702pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:11104702pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed