Recent progress with recombinant collagens produced in Escherichia coli. (June 2019)

• Record Type: Journal Article
• Authors: Ramshaw, John A.M.; Werkmeister, Jerome A.; Glattauer, Veronica
• Is Part Of: Current opinion in biomedical engineering. Volume 10(2019)
• Page Start: 149
• Page End: 155
• Publication Date: 2019-06
• Subjects: Collagen -- Recombinant -- Expression -- Bacterial collagens -- Hydroxyproline; P4H prolyl 4-hydroxylase -- Hyp hydroxyproline (3-letter code) -- O hydroxyproline (single-letter code) -- SOD superoxide dismutase -- DAAO d-amino acid oxidase -- V domain globular domain of bacterial collagens -- CL triple helical collagen domain of bacterial collagens -- DDR discoidin domain receptor -- EOCs endothelial progenitor cells -- HUVECs human umbilical vein endothelial cells -- RGD/RGDS Arg-Gly-Asp/Arg-Gly-Asp-Ser -- CD circular dichroism spectrometry -- PEG polyethylene glycol -- MSC mesenchymal stem cell -- MMP-1 matrix metalloproteinase-1 -- ECM extracellular matrix; Biomedical engineering -- Periodicals; 610.28
• DOI: 10.1016/j.cobme.2019.06.001
• Languages: English
• ISSNs: 2468-4511

Abstract

Abstract: Bacterial systems, especially using Escherichia coli, provide a useful system for recombinant production of collagen and collagen-like proteins. These systems provide high yields of products but have lacked the ability to introduce hydroxyproline when it is needed for stability and function. Recent progress, in the last 30 months, of animal-based recombinant proteins has focussed on further development of collagen peptide materials and their applications. The proposal of new approaches for incorporation of hydroxyproline may enhance the utility of these products and enable production of new materials. Bacterial, collagen-like constructs have also continued to be developed for use in understanding collagen structure and functions, while progress has also been made on their application as new biomedical materials.