Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Editorial
. 2023 Jul 15;208(2):125-127.
doi: 10.1164/rccm.202305-0935ED.

CLUSTERINg Circulating Histones in Sepsis

Brijesh V Patel  1   2 , Teresa M L Lee  3 , Kieran O'Dea  3
Affiliations
Editorial

CLUSTERINg Circulating Histones in Sepsis

Brijesh V Patel et al. Am J Respir Crit Care Med. .
No abstract available

PubMed Disclaimer

Figures

Figure 1.
Figure 1.
Histones are basic proteins whose positive charges associate with DNA, enabling the negatively charged DNA to spool around them. They form memberships of chromatin beads called nucleosomes, with each nucleosome bead consisting of a histone octamer composed of two copies of each histone protein: H2A, H2B, H3, and H4. They are coiled within the cell, forming condensed chromatin material. Extracellular histones are released by cell death in response to infection and inflammation as chromatin material, nucleosome, or individual histones. CLU (Clusterin), an extracellular chaperone protein, forms bonds to misfolded or excess proteins, including histones, forming complexes. CLU–histone complexes neutralize histone activity. In addition, these complexes aid the clearance of extracellular histones by binding to cell surface receptor(s); they are internalized by receptor-mediated endocytosis and trafficked to autophagosomes for degradation. NET = neutrophil extracellular trap.
See this image and copyright information in PMC

Comment on

  • Clusterin Neutralizes the Inflammatory and Cytotoxic Properties of Extracellular Histones in Sepsis.
    Augusto JF, Beauvillain C, Poli C, Paolini L, Tournier I, Pignon P, Blanchard S, Preisser L, Soleti R, Delépine C, Monnier M, Douchet I, Asfar P, Beloncle F, Guisset O, Prével R, Mercat A, Vinatier E, Goret J, Subra JF, Couez D, Wilson MR, Blanco P, Jeannin P, Delneste Y. Augusto JF, et al. Am J Respir Crit Care Med. 2023 Jul 15;208(2):176-187. doi: 10.1164/rccm.202207-1253OC. Am J Respir Crit Care Med. 2023. PMID: 37141109

References

    1. Joffre J, Hellman J, Ince C, Ait-Oufella H. Endothelial responses in sepsis. Am J Respir Crit Care Med . 2020;202:361–370. - PubMed
    1. Ma KC, Schenck EJ, Pabon MA, Choi AMK. The role of danger signals in the pathogenesis and perpetuation of critical illness. Am J Respir Crit Care Med . 2018;197:300–309. - PMC - PubMed
    1. Chen B, Miller AL, Rebelatto M, Brewah Y, Rowe DC, Clarke L, et al. S100A9 induced inflammatory responses are mediated by distinct damage associated molecular patterns (DAMP) receptors in vitro and in vivo. PLoS One . 2015;10:e0115828. - PMC - PubMed
    1. Venkatesh S, Workman JL. Histone exchange, chromatin structure and the regulation of transcription. Nat Rev Mol Cell Biol . 2015;16:178–189. - PubMed
    1. Felsenfeld G, Groudine M. Controlling the double helix. Nature . 2003;421:448–453. - PubMed

LinkOut - more resources