| Autor: |
P D, Toman, F, Pieper, N, Sakai, C, Karatzas, E, Platenburg, I, de Wit, C, Samuel, A, Dekker, G A, Daniels, R A, Berg, G J, Platenburg |
| Rok vydání: |
2000 |
| Předmět: |
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| Zdroj: |
Transgenic research. 8(6) |
| ISSN: |
0962-8819 |
| Popis: |
The large scale production of recombinant collagen for use in biomaterials requires an efficient expression system capable of processing a large (400 Kd) multisubunit protein requiring post-translational modifications. To investigate whether the mammary gland of transgenic animals fulfills these requirements, transgenic mice were generated containing the alpha S1-casein mammary gland-specific promoter operatively linked to 37 Kb of the human alpha 1(I) procollagen structural gene and 3' flanking region. The frequency of transgenic lines established was 12%. High levels of soluble triple helical homotrimeric [(alpha 1)3] type I procollagen were detected (up to 8 mg/ml) exclusively in the milk of six out of 9 lines of lactating transgenic mice. The transgene-derived human procollagen chains underwent efficient assembly into a triple helical structure. Although proline or lysine hydroxylation has never been described for any milk protein, procollagen was detected with these post-translational modifications. The procollagen was stable in milk; minimal degradation was observed. These results show that the mammary gland is capable of expressing a large procollagen gene construct, efficiently assembling the individual polypeptide chains into a stable triple helix, and secreting the intact molecule into the milk. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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