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

Abstract:

: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 proalpha1(I) chain to generate transgenic tobacco plants expressing collagen I. The recombinant proalpha1(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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Ruggiero F,Exposito JY,Bournat P,Gruber V,Perret S,Comte J,Olagnier B,Garrone R,Theisen M

doi

10.1016/s0014-5793(00)01259-x

keywords:

subject

Has Abstract

pub_date

2000-03-03 00:00:00

pages

132-6

issue

1

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(00)01259-X

journal_volume

469

pub_type

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