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|Title:||Proteolytic signatures define unique thrombin-derived peptides present in human wound fluid in vivo||Authors:||Saravanan, Rathi
Adav, Sunil Shankar
Choong, Yeu Khai
van der Plas, Mariena J. A.
Sze, Siu Kwan
|Issue Date:||2017||Source:||Saravanan, R., Adav, S. S., Choong, Y. K., van der Plas, M. J. A., Petrlova, J., Kjellström, S., et al. (2017). Proteolytic signatures define unique thrombin-derived peptides present in human wound fluid in vivo. Scientific Reports, 7, 13136-.||Series/Report no.:||Scientific Reports||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.||URI:||https://hdl.handle.net/10356/86498
|DOI:||http://dx.doi.org/10.1038/s41598-017-13197-3||Rights:||© 2017 The Author(s) Open Access. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder.||metadata.item.grantfulltext:||open||metadata.item.fulltext:||With Fulltext|
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