ArticleBMC biotechnology2015
Development and characterization of a eukaryotic expression system for human type II procollagen.
Article in BMC biotechnology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 31 citations in OpenAlex.
- Article
- Atomic Force Microscopy Investigations of Collagen: From Single Molecules to Fibrils.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Status and developmental trends in recombinant collagen preparation technology.Regenerative biomaterials · 2024Review
- Carrageenan-Based Crowding and Confinement Combination Approach to Increase Collagen Deposition for In Vitro Tissue Development.Gels (Basel, Switzerland) · 2023Article
- Synthesis, Characterization and Biological Properties of Type I Collagen-Chitosan Mixed Hydrogels: A Review.Gels (Basel, Switzerland) · 2023Review
- Pharmacological Functions, Synthesis, and Delivery Progress for Collagen as Biodrug and Biomaterial.Pharmaceutics · 2023Review
- Collagen- and hyaluronic acid-based hydrogels and their biomedical applications.Materials science & engineering. R, Reports : a review journal · 2021Article
- Engineered Collagen Matrices.Bioengineering (Basel, Switzerland) · 2020Review
- Optical Tweezers Approaches for Probing Multiscale Protein Mechanics and Assembly.Frontiers in molecular biosciences · 2020Review
- Tension in fibrils suppresses their enzymatic degradation - A molecular mechanism for 'use it or lose it'.Matrix biology : journal of the International Society for Matrix Biology · 2020Review
- Environmentally Controlled Curvature of Single Collagen Proteins.Biophysical journal · 2018Article
- Single-Molecule Assay for Proteolytic Susceptibility: Force-Induced Collagen Destabilization.Biophysical journal · 2018Article
- Intact Telopeptides Enhance Interactions between Collagens.Biophysical journal · 2016Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
backgroundTriple helical collagens are the most abundant structural protein in vertebrates and are widely used as biomaterials for a variety of applications including drug delivery and cellular and tissue engineering. In these applications, the mechanics of this hierarchically structured protein play a key role, as does its chemical composition. To facilitate investigation into how gene mutations of collagen lead to disease as well as the rational development of tunable mechanical and chemical properties of this full-length protein, production of recombinant expressed protein is required.
resultsHere, we present a human type II procollagen expression system that produces full-length procollagen utilizing a previously characterized human fibrosarcoma cell line for production. The system exploits a non-covalently linked fluorescence readout for gene expression to facilitate screening of cell lines. Biochemical and biophysical characterization of the secreted, purified protein are used to demonstrate the proper formation and function of the protein. Assays to demonstrate fidelity include proteolytic digestion, mass spectrometric sequence and posttranslational composition analysis, circular dichroism spectroscopy, single-molecule stretching with optical tweezers, atomic-force microscopy imaging of fibril assembly, and transmission electron microscopy imaging of self-assembled fibrils.
conclusionsUsing a mammalian expression system, we produced full-length recombinant human type II procollagen. The integrity of the collagen preparation was verified by various structural and degradation assays. This system provides a platform from which to explore new directions in collagen manipulation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.