Production of functional climeric collagens

胶原蛋白具有良好的生物相容性、对细胞和组织的亲和性和生物降解性，已被用作天然生物材料。本研究开发了一种重组技术，赋予III型胶原蛋白的促有丝分裂活性，通过融合它的表皮生长因子（EGF）在胶原蛋白的N-末端。在昆虫细胞中合成了EGF-Ⅲ型胶原融合蛋白。合成的嵌合蛋白具有胶原蛋白的三螺旋构象和EGF的促有丝分裂活性。还证明了嵌合蛋白可以作为纤维形式固定在组织培养皿上和胶原凝胶中，而不会消除其EGF的原始促有丝分裂活性。该融合蛋白可作为生物相容性、生物可降解性和粘附性纤维丝裂原用于组织工程领域的多种目的。

Collagen has been utilized as a natural biomaterial because of its high biocompatibility, adhesiveness to cells and tissues, and biodegradability. The present study developed a recombinant technology to confer a mitogenic activity on type III collagen by fusing it to epidermal growth factor (EGF) at the collagen's N-terminus. The fusion protein of EGF-type III collagen was synthesized in insect cells which had been transfected with baculoviruses bearing its cDNA. The synthesized chimeric protein was shown to hold the triple helical conformation of collagen and the mitogenic activity of EGF. It was also demonstrated that the chimeric protein can be immobilized on tissue culture dishes as a fibrous form and in collagen gels without abolishing its original mitogenic activity of EGF. This fusion protein can be utilized as a biocompatible, biodegradable, and adhesive fibrous mitogen for a variety of purposes in the area of tissue engineering.