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  • Influence
DAMPs, PAMPs and alarmins: all we need to know about danger
  • M. Bianchi
  • Biology, Medicine
    Journal of leukocyte biology
  • 1 January 2007
TLDR
The term “alarmin” is proposed to categorize such endogenous molecules that signal tissue and cell damage, and can be considered subgroups of a larger set, the damage‐associated molecular patterns (DAMPs).
Release of chromatin protein HMGB1 by necrotic cells triggers inflammation
TLDR
It is reported that Hmgb1-/- necrotic cells have a greatly reduced ability to promote inflammation, which proves that the release of HMGB1 can signal the demise of a cell to its neighbours, and cells undergoing apoptosis are programmed to withhold the signal that is broadcast by cells that have been damaged or killed by trauma.
Release of chromatin protein HMGB1 by necrotic cells triggers inflammation
TLDR
This corrects the article to show that the method used to derive the H2O2 “spatially aggregating force” is based on a two-step process, not a single step, like in the previous version of this paper.
Monocytic cells hyperacetylate chromatin protein HMGB1 to redirect it towards secretion
TLDR
It is shown here that in all cells HMGB1 shuttles actively between the nucleus and cytoplasm, and secreted when monocytic cells receive an appropriate second signal.
Toll-like receptor 4 and high-mobility group box-1 are involved in ictogenesis and can be targeted to reduce seizures
TLDR
HMGB1-TLR4 signaling may contribute to generating and perpetuating seizures in humans and might be targeted to attain anticonvulsant effects in epilepsies that are currently resistant to drugs.
The nuclear protein HMGB1 is secreted by monocytes via a non‐classical, vesicle‐mediated secretory pathway
TLDR
It is shown that activation of monocytes results in the redistribution of HMGB1 from the nucleus to cytoplasmic organelles, which display ultrastructural features of endolysosomes, which means that in monocytes, non‐classical secretion can occur through vescicle compartments that are at least partially distinct.
HMGB1 promotes recruitment of inflammatory cells to damaged tissues by forming a complex with CXCL12 and signaling via CXCR4
TLDR
CXCL12 forms a complex with HMGB1 that binds to the chemokine receptor CXCR4 and increases inflammatory cell migration and increasesinflammatory cell migration.
HMGB proteins function as universal sentinels for nucleic-acid-mediated innate immune responses
TLDR
It is shown that high-mobility group box (HMGB) proteins 1, 2 and 3 function as universal sentinels for nucleic acids and indicate a hierarchy in the nucleic-acid-mediated activation of immune responses, wherein the selective activation of nucleic -acid-sensing receptors is contingent on the more promiscuous sensing ofucleic acids by HMGBs.
A novel role for HMGB1 in TLR9-mediated inflammatory responses to CpG-DNA.
TLDR
The DNA-binding protein HMGB1 shuttles in and out of immune cells and regulates inflammatory responses to CpG-DNA.
Endogenous HMGB1 regulates autophagy
HMGB1 displaces Bcl-2 from Beclin1 to induce and sustain autophagy in response to cell stress.
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