A Neutrophil Proteomic Signature in Surgical Trauma Wounds

dc.bibliographicCitation.firstPage761
dc.bibliographicCitation.issue3
dc.bibliographicCitation.journalTitleInternational journal of molecular scienceseng
dc.bibliographicCitation.volume19
dc.contributor.authorBekeschus, Sander
dc.contributor.authorLackmann, Jan-Wilm
dc.contributor.authorGümbel, Denis
dc.contributor.authorNapp, Matthias
dc.contributor.authorSchmidt, Anke
dc.contributor.authorWende, Kristian
dc.date.accessioned2023-01-10T10:44:19Z
dc.date.available2023-01-10T10:44:19Z
dc.date.issued2018-3-7
dc.description.abstractNon-healing wounds continue to be a clinical challenge for patients and medical staff. These wounds have a heterogeneous etiology, including diabetes and surgical trauma wounds. It is therefore important to decipher molecular signatures that reflect the macroscopic process of wound healing. To this end, we collected wound sponge dressings routinely used in vacuum assisted therapy after surgical trauma to generate wound-derived protein profiles via global mass spectrometry. We confidently identified 311 proteins in exudates. Among them were expected targets belonging to the immunoglobulin superfamily, complement, and skin-derived proteins, such as keratins. Next to several S100 proteins, chaperones, heat shock proteins, and immune modulators, the exudates presented a number of redox proteins as well as a discrete neutrophil proteomic signature, including for example cathepsin G, elastase, myeloperoxidase, CD66c, and lipocalin 2. We mapped over 200 post-translational modifications (PTMs; cysteine/methionine oxidation, tyrosine nitration, cysteine trioxidation) to the proteomic profile, for example, in peroxiredoxin 1. Investigating manually collected exudates, we confirmed presence of neutrophils and their products, such as microparticles and fragments containing myeloperoxidase and DNA. These data confirmed known and identified less known wound proteins and their PTMs, which may serve as resource for future studies on human wound healing.eng
dc.description.versionpublishedVersioneng
dc.identifier.urihttps://oa.tib.eu/renate/handle/123456789/10818
dc.identifier.urihttp://dx.doi.org/10.34657/9844
dc.language.isoeng
dc.publisherBasel : Molecular Diversity Preservation International
dc.relation.doihttps://doi.org/10.3390/ijms19030761
dc.relation.essn1422-0067
dc.rights.licenseCC BY 4.0 Unported
dc.rights.urihttps://creativecommons.org/licenses/by/4.0
dc.subject.ddc570
dc.subject.ddc540
dc.subject.otherChaperoneseng
dc.subject.otherDamage-associated molecular patternseng
dc.subject.otherHeat-shock proteinseng
dc.subject.otherMass spectrometryeng
dc.subject.otherMatrix metalloproteinaseeng
dc.subject.otherPeptidaseseng
dc.subject.otherPost-translational modificationseng
dc.subject.otherRedox regulationeng
dc.titleA Neutrophil Proteomic Signature in Surgical Trauma Woundseng
dc.typeArticleeng
dc.typeTexteng
tib.accessRightsopenAccesseng
wgl.contributorINP
wgl.subjectBiowissenschaften/Biologieger
wgl.subjectChemieger
wgl.typeZeitschriftenartikelger
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