Peptidomic analysis of endogenous and bacterial protease activity in human plasma and wound fluids

Research output: Contribution to journal › Journal article › Research › peer-review

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Peptidomic analysis of endogenous and bacterial protease activity in human plasma and wound fluids. / Cai, Jun; Nielsen, Maike W; Kalogeropoulos, Konstantinos; Auf dem Keller, Ulrich; van der Plas, Mariena J A.

In: iScience, Vol. 27, No. 2, 109005, 2024.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Cai, J, Nielsen, MW, Kalogeropoulos, K, Auf dem Keller, U & van der Plas, MJA 2024, 'Peptidomic analysis of endogenous and bacterial protease activity in human plasma and wound fluids', iScience, vol. 27, no. 2, 109005. https://doi.org/10.1016/j.isci.2024.109005

APA

Cai, J., Nielsen, M. W., Kalogeropoulos, K., Auf dem Keller, U., & van der Plas, M. J. A. (2024). Peptidomic analysis of endogenous and bacterial protease activity in human plasma and wound fluids. iScience, 27(2), [109005]. https://doi.org/10.1016/j.isci.2024.109005

Vancouver

Cai J, Nielsen MW, Kalogeropoulos K, Auf dem Keller U, van der Plas MJA. Peptidomic analysis of endogenous and bacterial protease activity in human plasma and wound fluids. iScience. 2024;27(2). 109005. https://doi.org/10.1016/j.isci.2024.109005

Author

Cai, Jun ; Nielsen, Maike W ; Kalogeropoulos, Konstantinos ; Auf dem Keller, Ulrich ; van der Plas, Mariena J A. / Peptidomic analysis of endogenous and bacterial protease activity in human plasma and wound fluids. In: iScience. 2024 ; Vol. 27, No. 2.

Bibtex

@article{0743a9710bdf46469f3e246285847e45,

title = "Peptidomic analysis of endogenous and bacterial protease activity in human plasma and wound fluids",

abstract = "Endogenous and bacterial proteases play important roles in wound healing and infection. Analysis of alterations in the low-molecular-weight peptidome by individual enzymes could therefore provide insight into proteolytic events occurring in wounds and may aid in the discovery of biomarkers. Using liquid chromatography with tandem mass spectrometry, we characterized the peptidome of plasma and acute wound fluids digested ex vivo with human (neutrophil elastase and cathepsin G) and bacterial proteases ( Pseudomonas aeruginosa LasB and Staphyloccocus aureus V8). We identified over 100 protein targets for each enzyme and characterized enzyme specific peptides and cleavage patterns. Moreover, we found unique peptide regions in V8 digested samples that were also present in dressing extracts from S. aureus infected wounds. Finally, the work indicates that peptidomic analysis of qualitative differences of proteolytic activity of individual enzymes may aid in the discovery of potential diagnostic biomarkers for wound healing status. ",

author = "Jun Cai and Nielsen, {Maike W} and Konstantinos Kalogeropoulos and {Auf dem Keller}, Ulrich and {van der Plas}, {Mariena J A}",

note = "{\textcopyright} 2024 The Author(s).",

year = "2024",

doi = "10.1016/j.isci.2024.109005",

language = "English",

volume = "27",

journal = "iScience",

issn = "2589-0042",

publisher = "Elsevier",

number = "2",

}

RIS

TY - JOUR

T1 - Peptidomic analysis of endogenous and bacterial protease activity in human plasma and wound fluids

AU - Cai, Jun

AU - Nielsen, Maike W

AU - Kalogeropoulos, Konstantinos

AU - Auf dem Keller, Ulrich

AU - van der Plas, Mariena J A

PY - 2024

Y1 - 2024

N2 - Endogenous and bacterial proteases play important roles in wound healing and infection. Analysis of alterations in the low-molecular-weight peptidome by individual enzymes could therefore provide insight into proteolytic events occurring in wounds and may aid in the discovery of biomarkers. Using liquid chromatography with tandem mass spectrometry, we characterized the peptidome of plasma and acute wound fluids digested ex vivo with human (neutrophil elastase and cathepsin G) and bacterial proteases ( Pseudomonas aeruginosa LasB and Staphyloccocus aureus V8). We identified over 100 protein targets for each enzyme and characterized enzyme specific peptides and cleavage patterns. Moreover, we found unique peptide regions in V8 digested samples that were also present in dressing extracts from S. aureus infected wounds. Finally, the work indicates that peptidomic analysis of qualitative differences of proteolytic activity of individual enzymes may aid in the discovery of potential diagnostic biomarkers for wound healing status.

AB - Endogenous and bacterial proteases play important roles in wound healing and infection. Analysis of alterations in the low-molecular-weight peptidome by individual enzymes could therefore provide insight into proteolytic events occurring in wounds and may aid in the discovery of biomarkers. Using liquid chromatography with tandem mass spectrometry, we characterized the peptidome of plasma and acute wound fluids digested ex vivo with human (neutrophil elastase and cathepsin G) and bacterial proteases ( Pseudomonas aeruginosa LasB and Staphyloccocus aureus V8). We identified over 100 protein targets for each enzyme and characterized enzyme specific peptides and cleavage patterns. Moreover, we found unique peptide regions in V8 digested samples that were also present in dressing extracts from S. aureus infected wounds. Finally, the work indicates that peptidomic analysis of qualitative differences of proteolytic activity of individual enzymes may aid in the discovery of potential diagnostic biomarkers for wound healing status.

U2 - 10.1016/j.isci.2024.109005

DO - 10.1016/j.isci.2024.109005

M3 - Journal article

C2 - 38333691

VL - 27

JO - iScience

JF - iScience

SN - 2589-0042

IS - 2

M1 - 109005

ER -

ID: 382379152

Faculty of Law