ArticleTransgenic research1999
Production of recombinant human type I procollagen homotrimer in the mammary gland of transgenic mice.
Article in Transgenic research, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
13 citing papers in PubMed, 68 citations in OpenAlex.
- 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
- Recombinant fibrous protein biomaterials meet skin tissue engineering.Frontiers in bioengineering and biotechnology · 2024Review
- Pharmacological Functions, Synthesis, and Delivery Progress for Collagen as Biodrug and Biomaterial.Pharmaceutics · 2023Review
- Review
- Sources of Collagen for Biomaterials in Skin Wound Healing.Bioengineering (Basel, Switzerland) · 2019Review
- Bioactive polymer scaffold for fabrication of vascularized engineering tissue.Journal of artificial organs : the official journal of the Japanese Society for Artificial Organs · 2012Review
- The creation of transgenic pigs expressing human proteins using BAC-derived, full-length genes and intracytoplasmic sperm injection-mediated gene transfer.Transgenic research · 2012Article
- Natural and Genetically Engineered Proteins for Tissue Engineering.Progress in polymer science · 2012Article
- Design and construction of two yeast shuttle vectors containing human procollagen genes expression cassette for expression in yeast.Avicenna journal of medical biotechnology · 2011Article
- A Streptococcus pyogenes derived collagen-like protein as a non-cytotoxic and non-immunogenic cross-linkable biomaterial.Biomaterials · 2010Article
- Collagens as biomaterials.Journal of materials science. Materials in medicine · 2009Review
- Prospects and limitations of the rational engineering of fibrillar collagens.Protein science : a publication of the Protein Society · 2003Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The large scale production of recombinant collagen for use in biomaterials requires an efficient expression system capable of processing a large (> 400 Kd) multisubunit protein requiring post-translational modifications. To investigate whether the mammary gland of transgenic animals fulfills these requirements, transgenic mice were generated containing the alpha S1-casein mammary gland-specific promoter operatively linked to 37 Kb of the human alpha 1(I) procollagen structural gene and 3' flanking region. The frequency of transgenic lines established was 12%. High levels of soluble triple helical homotrimeric [(alpha 1)3] type I procollagen were detected (up to 8 mg/ml) exclusively in the milk of six out of 9 lines of lactating transgenic mice. The transgene-derived human procollagen chains underwent efficient assembly into a triple helical structure. Although proline or lysine hydroxylation has never been described for any milk protein, procollagen was detected with these post-translational modifications. The procollagen was stable in milk; minimal degradation was observed. These results show that the mammary gland is capable of expressing a large procollagen gene construct, efficiently assembling the individual polypeptide chains into a stable triple helix, and secreting the intact molecule into the milk.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.