Apr 3, 2020 · Here, we report the novel function of caspase-11 and gasdermin D (GsdmD) in LPS-induced active HMGB1 released from hepatocytes. HMGB1 release during endotoxemia was caspase-11/GsdmD dependent via an active way in vivo and in vitro.

Nov 6, 2021 · High mobility group box protein 1 (HMGB1) is a typical damage-associated molecular pattern (DAMP) molecule, which is cytotoxic and leads to cell death and tissue injury. Whether EVs are...

Feb 25, 2022 · Carbon monoxide-releasing molecule 2 (CORM-2) specifically inhibits NOS2 expression and NO production, which blocks LPS-induced HMGB1 release in macrophages through the IFNB-JAK2-STAT1...

Oct 16, 2018 · Hepatocyte-released HMGB1 directly binds to LPS, and the HMGB1-LPS complex is internalized via RAGE-mediated endocytosis. Subsequently, HMGB1 facilitates LPS translocation from endolysosomes to the cytosol by inducing lysosomal rupture.

Aug 4, 2022 · The high mobility group box 1 (HMGB1), a well-known danger-associated molecule pattern (DAMP) molecule, is a non-histone chromosomal protein localized in the nucleus under normal physiological conditions. HMGB1 exhibits diverse functions depending on …

Jan 19, 2023 · In this study, we investigated the role of HMGB1 in lipopolysaccharide (LPS)-induced autophagy and pyroptosis of macrophages. The results indicate that HMGB1 plays different roles in mediating LPS-induced autophagy and triggering pyroptosis, according to subcellular localization.

Here, we report the novel function of caspase-11 and gasdermin D (GsdmD) in LPS-induced active HMGB1 released from hepatocytes. HMGB1 release during endotoxemia was caspase-11/GsdmD dependent via an active way in vivo and in vitro.

Jun 1, 2012 · Background: High mobility group protein B1 (HMGB1) is an important late inflammatory mediator in sepsis. Understanding the mechanisms that regulate HMGB1 release from cells and their downstream signal transduction pathways may lead to the ability to develop anti-HMGB1 therapies to treat inflammation.

HMGB1 has two LPS-binding sites and thus forms an extracellular HMGB1–LPS complex that gets endocytosed via RAGE to finally reach the cytosol culminating in activation of the intracellular LPS sensor caspase-11 (caspases-4 and −5 in humans) …

Here we show that HMGB1 enables extracellular LPS to activate cytosolic caspase-11 in macrophages and endothelial cells via receptor for advanced glycation end-products (RAGE)-dependent internalization of HMGB1-LPS complexes into lysosomes, where HMGB1 permeabilizes the phospholipid bilayer under acidic conditions.