Production of bioactive, post-translationally modified, heterotrimeric, human recombinant type-I collagen in transgenic tobacco.

Abstract:

:Collagen's biocompatibility, biodegradability and low immunogenicity render it advantageous for extensive application in pharmaceutical or biotechnological disciplines. However, typical collagen extraction from animal or cadaver sources harbors risks including allergenicity and potential sample contamination with pathogens. In this work, two human genes encoding recombinant heterotrimeric collagen type I (rhCOL1) were successfully coexpressed in tobacco plants with the human prolyl-4-hydroxylase (P4H) and lysyl hydroxylase 3 (LH3) enzymes, responsible for key posttranslational modifications of collagen. Plants coexpressing all five vacuole-targeted proteins generated intact procollagen yields of approximately 2% of the extracted total soluble proteins. Plant-extracted rhCOL1 formed thermally stable triple helical structures and demonstrated biofunctionality similar to human tissue-derived collagen supporting binding and proliferation of adult peripheral blood-derived endothelial progenitor-like cells. Through a simple, safe and scalable method of rhCOL1 production and purification from tobacco plants, this work broadens the potential applications of human recombinant collagen in regenerative medicine.

journal_name

Biomacromolecules

journal_title

Biomacromolecules

authors

Stein H,Wilensky M,Tsafrir Y,Rosenthal M,Amir R,Avraham T,Ofir K,Dgany O,Yayon A,Shoseyov O

doi

10.1021/bm900571b

subject

Has Abstract

pub_date

2009-09-14 00:00:00

pages

2640-5

issue

9

eissn

1525-7797

issn

1526-4602

journal_volume

10

pub_type

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