Ontology highlight
ABSTRACT: Background
During sepsis or sterile tissue injury, the nuclear protein high mobility group box 1 (HMGB1) can be released to the extracellular space and ultimately into systemic circulation, where it mediates systemic inflammation and remote organ failure. The proinflammatory effects of HMGB1 can be suppressed by recombinant thrombomodulin (rTM), in part through a mechanism involving thrombin-rTM-mediated degradation of HMGB1. Given that HMGB1 is proinflammatory but the HMGB1 degradation product (desHMGB1) is not, an analytical method that discriminates between these two molecules may provide a more in-depth understanding of HMGB1-induced pathogenicity as well as rTM-mediated therapeutic efficiency.Methods
A peptide that has a shared amino-terminal structure with desHMGB1 wa
SUBMITTER: Totoki T
PROVIDER: S-EPMC8190996 | biostudies-literature | 2021 Jun
REPOSITORIES: biostudies-literature