Evidence map›Paper›PMID 29162919›Full record

ArticleScientific reports2017

Production of recombinant human procollagen type I C-terminal propeptide and establishment of a sandwich ELISA for quantification.

Woo-Young Seo, Jeong-Ho Kim, Du-San Baek, Su-Jung Kim, Sujin Kang, Won Suk Yang, Ji-Ae Song, Moo-Seung Lee, Sunghoon Kim, Yong-Sung Kim

Abstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

27 citing papers in PubMed.

  1. Review
  2. Review
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  5. Review
  6. Review
  7. Article
  8. Article
  9. Rosarugosides A and D fromPlants (Basel, Switzerland) · 2024
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  10. Human ProbioticCells · 2023
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  11. Article
  12. Exploration of the skeletal phenotype of theFrontiers in endocrinology · 2023
    Article
  13. Chemical Composition ofPharmaceuticals (Basel, Switzerland) · 2022
    Article
  14. Article
  15. Chemical Composition ofPlants (Basel, Switzerland) · 2022
    Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Collagen's enigmatic, highly conservedProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors.

Woo-Young SeoMedicinal Bioconvergence Research Center, Seoul National University, Suwon, 16229, Korea.
Jeong-Ho KimDepartment of Molecular Science and Technology, Ajou University, Suwon, 16499, Korea.
Du-San BaekDepartment of Molecular Science and Technology, Ajou University, Suwon, 16499, Korea.
Su-Jung KimDepartment of Molecular Science and Technology, Ajou University, Suwon, 16499, Korea.
Sujin KangMedicinal Bioconvergence Research Center, Seoul National University, Suwon, 16229, Korea.
Won Suk YangMedicinal Bioconvergence Research Center, Seoul National University, Suwon, 16229, Korea.
Ji-Ae SongMedicinal Bioconvergence Research Center, Seoul National University, Suwon, 16229, Korea.
Moo-Seung LeeInfectious Disease Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, 34141, Korea.
Sunghoon KimMedicinal Bioconvergence Research Center, Seoul National University, Suwon, 16229, Korea. sungkim@snu.ac.kr.
Yong-Sung KimDepartment of Molecular Science and Technology, Ajou University, Suwon, 16499, Korea. kimys@ajou.ac.kr.ORCID 0000-0003-2673-1509

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Procollagen type I carboxy-terminal propeptide (PICP), derived from type I procollagen, has been identified as an indicator of type I collagen synthesis in bone matrix formation and skin recovery. PICP is a heterotrimeric glycoprotein consisting of two α1 chains (PICPα1) and one α2 chain (PICPα2). Here, we report the recombinant expression of human PICP using a mammalian expression system. Co-expression of PICPα1 and PICPα2 in HEK293F cells resulted in the production of functional PICP in the correctly assembled heterotrimeric form. Using the recombinant PICP as an antigen, we isolated PICP-specific human monoclonal antibodies from phage-displayed antibody libraries and raised rabbit polyclonal antibodies. Using those antibodies, we then developed a sandwich ELISA for PICP with a limit of detection of 1 ng/mL and a measurable range of 1-640 ng/mL. Both intra- and inter-assay imprecision values were <10%. For measuring PICP levels in human fibroblast cellular extracts and culture supernatants and a human serum, the developed ELISA kit displayed comparable performance to that of a commercialized kit. Our results provide an efficient production strategy for recombinant PICP, facilitating the generation of PICP-specific antibodies and development of PICP sandwich ELISA, with potential use in clinical diagnosis of serum samples and testing of cosmeceutical ingredients in fibroblast cell cultures.

Indexed as

Amino Acid SequenceAntibodies, MonoclonalEnzyme-Linked Immunosorbent AssayHEK293 CellsHumansPeptide FragmentsProcollagenProtein BindingRecombinant ProteinsReproducibility of ResultsAntibodies, MonoclonalPeptide FragmentsProcollagenprocollagen type I carboxy terminal peptideRecombinant Proteins

Identifiers

PMID29162919
PMCPMC5698462

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Registered trials

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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.