Evidence map›Paper›PMID 34435180›Full record

ArticleMatrix biology plus2021

Procollagen C-proteinase enhancer-1 (PCPE-1), a potential biomarker and therapeutic target for fibrosis.

Priscillia Lagoutte, Emmanuel Bettler, Sandrine Vadon-Le Goff, Catherine Moali

Open access · goldAbstract read
In one paragraph

Article in Matrix biology plus, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
6.8field-weighted citation impact, top 2% of its field
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

31 citing papers in PubMed, 41 citations in OpenAlex.

  1. Trial
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  7. PCPE1 and PCPE2: When Sequence Similarity Masks Functional Diversity.Arteriosclerosis, thrombosis, and vascular biology · 2026
    Review
  8. Article
  9. Article
  10. Collagen in Fibrotic Diseases.Sub-cellular biochemistry · 2026
    Review
  11. Review
  12. Evaluating serum biomarkers in keratoconus: the role of PCPE-1 and PCPE-2 in collagen metabolism and disease progression.Graefe's archive for clinical and experimental ophthalmology = Albrecht von Graefes Archiv fur klinische und experimentelle Ophthalmologie · 2025
    Article
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  16. Review
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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

4 authors at 1 institution in 1 country.

Priscillia LagoutteUniversity of Lyon, CNRS, Tissue Biology and Therapeutic Engineering Laboratory, LBTI, UMR5305, F-69367 Lyon, France.
Emmanuel BettlerUniversity of Lyon, CNRS, Tissue Biology and Therapeutic Engineering Laboratory, LBTI, UMR5305, F-69367 Lyon, France.
Sandrine Vadon-Le GoffUniversity of Lyon, CNRS, Tissue Biology and Therapeutic Engineering Laboratory, LBTI, UMR5305, F-69367 Lyon, France.
Catherine MoaliUniversity of Lyon, CNRS, Tissue Biology and Therapeutic Engineering Laboratory, LBTI, UMR5305, F-69367 Lyon, France.
Université Claude Bernard Lyon 1 · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The correct balance between collagen synthesis and degradation is essential for almost every aspect of life, from development to healthy aging, reproduction and wound healing. When this balance is compromised by external or internal stress signals, it very often leads to disease as is the case in fibrotic conditions. Fibrosis occurs in the context of defective tissue repair and is characterized by the excessive, aberrant and debilitating deposition of fibril-forming collagens. Therefore, the numerous proteins involved in the biosynthesis of fibrillar collagens represent a potential and still underexploited source of therapeutic targets to prevent fibrosis. One such target is procollagen C-proteinase enhancer-1 (PCPE-1) which has the unique ability to accelerate procollagen maturation by BMP-1/tolloid-like proteinases (BTPs) and contributes to trigger collagen fibrillogenesis, without interfering with other BTP functions or the activities of other extracellular metalloproteinases. This role is achieved through a fine-tuned mechanism of action that is close to being elucidated and offers promising perspectives for drug design. Finally, the

Indexed as

ADAMTS, a disintegrin and metalloproteinase with thrombospondin motifsAS, aortic valve stenosisBiomarkerBMP, bone morphogenetic proteinCKD, chronic kidney diseaseCollagenCP, C-propeptideCUB, complement, Uegf, BMP-1CVD, cardiovascular diseaseDMD, Duchenne muscular dystrophyECM, extracellular matrixEGF, epidermal growth factoreGFR, estimated glomerular filtration rateELISA, enzyme-linked immunosorbent assayFibrillogenesisFibrosisHDL, high-density lipoproteinHSC, hepatic stellate cellHTS, hypertrophic scarIPF, idiopathic pulmonary fibrosisLDL, low-density lipoproteinMI, myocardial infarctionMMP, matrix metalloproteinasemTLD, mammalian tolloidmTLL, mammalian tolloid-likeNASH, nonalcoholic steatohepatitisNTR, netrinOPMD, oculopharyngeal muscular dystrophyPABPN1, poly(A)-binding protein nuclear 1PCPE, procollagen C-proteinase enhancerPCP, procollagen C-proteinasePNP, procollagen N-proteinaseProteolysisSPC, subtilisin proprotein convertaseTGF-β, transforming growth-factor βTherapeutic targetTIMP, tissue inhibitor of metalloproteinasesTSPN, thrombospondin-like N-terminal

Identifiers

PMID34435180
PMCPMC8377038
OpenAlexW3152999945

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

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 Socratic graph.