Evidence map›Paper›PMID 29030565›Full record

ArticleScientific reports2017

Proteolytic signatures define unique thrombin-derived peptides present in human wound fluid in vivo.

Rathi Saravanan, Sunil S Adav, Yeu Khai Choong, Mariena J A van der Plas, Jitka Petrlova, Sven Kjellström, Siu Kwan Sze, Artur Schmidtchen

Open access · goldAbstract 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 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

14 citing papers in PubMed, 27 citations in OpenAlex.

  1. Trial
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  6. Wound fluid sampling methods for proteomic studies: A scoping review.Wound repair and regeneration : official publication of the Wound Healing Society [and] the European Tissue Repair Society · 2022
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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

8 authors at 2 institutions in 3 countries.

Rathi SaravananLee Kong Chian School of Medicine, Nanyang Technological University, 59 Nanyang Drive, Singapore, 636921, Singapore. rathi@ntu.edu.sg.
Sunil S AdavLee Kong Chian School of Medicine, Nanyang Technological University, 59 Nanyang Drive, Singapore, 636921, Singapore.ORCID 0000-0002-8559-4885
Yeu Khai ChoongLee Kong Chian School of Medicine, Nanyang Technological University, 59 Nanyang Drive, Singapore, 636921, Singapore.
Mariena J A van der PlasDivision of Dermatology, Department of Clinical Sciences, Lund University, Lund, Sweden.
Jitka PetrlovaDivision of Dermatology, Department of Clinical Sciences, Lund University, Lund, Sweden.
Sven KjellströmCentre of Excellence in Biological and Medical Mass Spectrometry "CEBMMS", Biomedical Centre D13, Lund University, Lund, Sweden.
Siu Kwan SzeSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore, 637551, Singapore.ORCID 0000-0002-5652-1687
Artur SchmidtchenLee Kong Chian School of Medicine, Nanyang Technological University, 59 Nanyang Drive, Singapore, 636921, Singapore.
Nanyang Technological University · SGLund University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The disease burden of failing skin repair and non-healing ulcers is extensive. There is an unmet need for new diagnostic approaches to better predict healing activity and wound infection. Uncontrolled and excessive protease activity, of endogenous or bacterial origin, has been described as a major contributor to wound healing impairments. Proteolytic peptide patterns could therefore correlate and "report" healing activity and infection. This work describes a proof of principle delineating a strategy by which peptides from a selected protein, human thrombin, are detected and attributed to proteolytic actions. With a particular focus on thrombin-derived C-terminal peptides (TCP), we show that distinct peptide patterns are generated in vitro by the human S1 peptidases human neutrophil elastase and cathepsin G, and the bacterial M4 peptidases Pseudomonas aeruginosa elastase and Staphylococcus aureus aureolysin, respectively. Corresponding peptide sequences were identified in wound fluids from acute and non-healing ulcers, and notably, one peptide, FYT21 (FYTHVFRLKKWIQKVIDQFGE), was only present in wound fluid from non-healing ulcers colonized by P. aeruginosa and S. aureus. Our result is a proof of principle pointing at the possibility of defining peptide biomarkers reporting distinct proteolytic activities, of potential implication for improved diagnosis of wound healing and infection.

Indexed as

Bacterial ProteinsCathepsin GHumansPancreatic ElastasePeptide HydrolasesPeptidesPseudomonas aeruginosaStaphylococcus aureusThrombinWound HealingBacterial ProteinsCathepsin GPancreatic ElastasePeptide HydrolasesPeptidesThrombin

Identifiers

PMID29030565
PMCPMC5640616
OpenAlexW2761944502

What OpenQuestion holds

Textmetadata
LicenceCC BY
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 OpenQuestion graph.