ArticleScientific reports2025
Proteinase 3 is involved in presepsin production through neutrophil extracellular trap phagocytosis by macrophages.
Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Presepsin (P-SEP), a soluble subtype of CD14, is widely recognized as a diagnostic biomarker for sepsis. However, the molecular mechanisms underlying its production remain poorly understood. In this study, we investigated whether M1 macrophages (M1 MΦs) contribute to P-SEP generation by phagocytosing neutrophil extracellular traps (NETs) and degrading NET-derived CD14 through intracellular proteinase 3 (PR3). M1 MΦs were differentiated from peripheral blood mononuclear cells obtained from healthy donors, and NETs were induced in neutrophils stimulated with Escherichia coli or phorbol 12-myristate 13-acetate PMA. Co-cultures of M1 MΦs and NETs were analyzed by immunofluorescence staining, flow cytometry, ELISA, and Western blotting. The effects of PR3 inhibition (phenylmethylsulfonyl fluoride or elafin) and phagocytosis inhibition (cytochalasin D or wortmannin) on P-SEP production were also evaluated. Recombinant CD14 (rCD14) was used in an in vitro cleavage assay to confirm PR3-dependent CD14 fragmentation. M1 MΦs actively phagocytosed citrullinated histone H3–positive NETs and produced intracellular P-SEP. P-SEP levels strongly correlated with the percentage of NETs (r = 0.907). Inhibition of PR3 activity or phagocytosis significantly reduced P-SEP production. Furthermore, incubation of rCD14 with PR3 produced P-SEP, and this effect was blocked by PR3 inhibitors. These findings demonstrate that PR3 contributes to P-SEP production through CD14 cleavage following NET phagocytosis by M1 MΦs. This study provides new mechanistic insight into the P-SEP biogenesis and advances the understanding of its role as a biomarker in sepsis.
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