Triple helix assembly and processing of human collagen produced in transgenic tobacco plants

被引：134

作者：

Ruggiero, F

Exposito, JY

Bournat, P

Gruber, V

Perret, S

Comte, J

Olagnier, B

Garrone, R

Theisen, M

机构：

[1] Univ Lyon 1, CNRS, UPR 412, Inst Biol & Chim Prot, F-69367 Lyon 07, France

[2] Meristem Therapeut, F-63100 Clermont Ferrand, France

来源：

FEBS LETTERS | 2000年 / 469卷 / 01期

关键词：

recombinant collagen; transgenic plant; triple helix assembly;

D O I：

10.1016/S0014-5793(00)01259-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The use of tobacco plants as a novel expression system for the production of human homotrimeric collagen I is presented in this report. Constructs were engineered from cDNA encoding the human pro alpha 1(I) chain to generate transgenic tobacco plants expressing collagen I. The recombinant pro alpha 1(I) chains were expressed as disulfide-bonded trimers and were shown to fold into a stable homotrimeric triple helix. Moreover. the recombinant procollagen was subsequently processed to collagen as it occurs in animals. Large amounts of recombinant collagen were purified from field grown plant material. The data suggest that plants are a valuable alternative for the recombinant production of collagen for various medical and scientific purposes. (C) 2000 Federation of European Biochemical Societies.

引用

页码：132 / 136

页数：5

共 27 条

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