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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

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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

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