ArticleThe EMBO journal1997
Assembly of human prolyl 4-hydroxylase and type III collagen in the yeast pichia pastoris: formation of a stable enzyme tetramer requires coexpression with collagen and assembly of a stable collagen requires coexpression with prolyl 4-hydroxylase.
Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers, 1 of them a synthesis that pooled it.
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Who cites it
33 citing papers in PubMed, 1 synthesis or guideline pooled it, 176 citations in OpenAlex.
- Clinical effect of vitamin C supplementation on bone healing: A systematic review.Medicina oral, patologia oral y cirugia bucal · 2022Pooled it
- Enhanced biosynthesis of full-length triple-helical human type III collagen in engineered Komagataella phaffii.Applied microbiology and biotechnology · 2026Article
- Marine collagen for regenerative medicine: Structure-function advantages, limitations, and translational pathways.Bioactive materials · 2026Review
- Progress in the Expression, Purification, and Characterization of Recombinant Collagen.Bioengineering (Basel, Switzerland) · 2026Review
- Recombinant collagen in regenerative medicine: Expression strategies, structural design, and translational applications.Materials today. Bio · 2025Review
- Applications of recombinant type III collagen in tissue engineering.Biomedical engineering online · 2025Review
- Efficient secretory expression of type III recombinant human collagen with triple-helical structure in Komagataella phaffii.Applied microbiology and biotechnology · 2025Article
- Expression, characterization, and application potentiality evaluation of recombinant human-like collagen in Pichia pastoris.Bioresources and bioprocessing · 2022Article
- Synthetic methylotrophic yeasts for the sustainable fuel and chemical production.Biotechnology for biofuels and bioproducts · 2022Review
- Comparative genomic and biochemical analyses identify a collagen galactosylhydroxylysyl glucosyltransferase from Acanthamoeba polyphaga mimivirus.Scientific reports · 2022Article
- Collagen- and hyaluronic acid-based hydrogels and their biomedical applications.Materials science & engineering. R, Reports : a review journal · 2021Article
- Article
- Collagen analogs with phosphorylcholine are inflammation-suppressing scaffolds for corneal regeneration from alkali burns in mini-pigs.Communications biology · 2021Article
- Three Decades of Research on Recombinant Collagens: Reinventing the Wheel or Developing New Biomedical Products?Bioengineering (Basel, Switzerland) · 2020Review
- Role of prolyl hydroxylation in the molecular interactions of collagens.Essays in biochemistry · 2019Review
- Review
- Production of human type II collagen using an efficient baculovirus-silkworm multigene expression system.Molecular genetics and genomics : MGG · 2016Article
- Engineering of an elastic scaffolding polyprotein based on an SH3-binding intrinsically disordered titin PEVK module.Protein expression and purification · 2012Article
- Assaying proline hydroxylation in recombinant collagen variants by liquid chromatography-mass spectrometry.BMC biotechnology · 2012Article
- Natural and Genetically Engineered Proteins for Tissue Engineering.Progress in polymer science · 2012Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prolyl 4-hydroxylase, the key enzyme of collagen synthesis, is an alpha2beta2 tetramer, the beta subunit of which is protein disulfide isomerase (PDI). Coexpression of the human alpha subunit and PDI in Pichia produced trace amounts of an active tetramer. A much higher, although still low, assembly level was obtained using a Saccharomyces pre-pro sequence in PDI. Coexpression with human type III procollagen unexpectedly increased the assembly level 10-fold, with no increase in the total amounts of the subunits. The recombinant enzyme was active not only in Pichia extracts but also inside the yeast cell, indicating that Pichia must have a system for transporting all the cosubstrates needed by the enzyme into the lumen of the endoplasmic reticulum. The 4-hydroxyproline-containing procollagen polypeptide chains were of full length and formed molecules with stable triple helices even though Pichia probably has no Hsp47-like protein. The data indicate that collagen synthesis in Pichia, and probably also in other cells, involves a highly unusual control mechanism, in that production of a stable prolyl 4-hydroxylase requires collagen expression while assembly of a stable collagen requires enzyme expression. This Pichia system seems ideal for the high-level production of various recombinant collagens for numerous scientific and medical purposes.
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Registered trials
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