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Review
. 2018 Jun;44(3):301-316.
doi: 10.1007/s00068-018-0962-3. Epub 2018 May 4.

Danger signals in trauma

Affiliations
Review

Danger signals in trauma

Borna Relja et al. Eur J Trauma Emerg Surg. 2018 Jun.

Abstract

This review summarizes a short list of currently discussed trauma-induced danger-associated molecular patterns (DAMP). Due to the bivalent character and often pleiotropic effects of a DAMP, it is difficult to describe its "friend or foe" role in post-traumatic inflammation and regeneration, both systemically as well locally in tissues. DAMP can be used as biomarkers to indicate or monitor disease or injury severity, but also may serve as clinically applicable parameters for better indication and timing of surgery. Due to the inflammatory processes at the local tissue level or the systemic level, the precise role of DAMP is not always clear to define. While in vitro and experimental studies allow for the detection of these biomarkers at the different levels of an organism-cellular, tissue, circulation-this is not always easily transferable to the human setting. Increased knowledge exploring the dual role of DAMP after trauma, and concentrating on their nuclear functions, transcriptional targets, release mechanisms, cellular sources, multiple functions, their interactions and potential therapeutic targeting is warranted.

Keywords: Biomarker; DAMP; Inflammation; Injury; Trauma.

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Conflict of interest statement

Conflict of interest

Borna Relja, Katharina Mörs and Ingo Marzi declare no conflicts of interest.

Human and animal rights

This study does not include any human participants and/or animals.

Informed consent

No informed consent is necessary.

Figures

Fig. 1
Fig. 1
Brief concept of selected danger-associated molecular pattern (DAMP) and pattern recognition receptor (PRR) localization and their release/activation upon trauma. Trauma with tissue injury leads correspondingly to tissue- or cell-specific death, and subsequent DAMP release. CLR C-type lectin receptors, CNS central nervous system, CypA cyclophilin A, HMGB1 high-mobility group box, HSP heat-shock protein, IL interleukin, Mincle macrophage-inducible C-type lectin, P2X7 P2X purinoceptor 7, RAGE receptor for advanced glycation end products, SAP130 spliceosome-associated protein 130, ST2 orphan receptor ST2

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