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
Biomacromoleculesjournal_title
Biomacromoleculesauthors
Stein H,Wilensky M,Tsafrir Y,Rosenthal M,Amir R,Avraham T,Ofir K,Dgany O,Yayon A,Shoseyov Odoi
10.1021/bm900571bsubject
Has Abstractpub_date
2009-09-14 00:00:00pages
2640-5issue
9eissn
1525-7797issn
1526-4602journal_volume
10pub_type
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