Enolase-1 Is a Key Regulator of Neutrophil Recruitment During Acute Inflammation
Journal
Immunology
Journal Issue
Online Version of Record before inclusion in an issue
ISSN
0019-2805
1365-2567
Date Issued
2025-09-09
Author(s)
Lu, Hsueh‐Yen
Huang, Ping‐Hsiang
Lee, Ting‐Wei
Chen, Nai‐Yu
Zhuang, Yu‐Jing
Yuan, Ta‐Tung
Abstract
Enolase-1 (ENO1) is a moonlighting protein with multiple functions. When expressed on the cell surface, ENO1 binds plasminogen (PLG) and promotes cell migration by facilitating plasmin (PLM)-mediated extracellular matrix degradation. Here, we observed that inflammatory stimulation significantly upregulated ENO1 expression on the neutrophil surface, both in vitro and in vivo. An anti-ENO1 monoclonal antibody (mAb), 7E5, which blocks the ENO1-PLG interaction, effectively suppressed neutrophil invasion in vitro. In mouse models of acute inflammation, including lipopolysaccharide (LPS)-induced lung injury and necrotic cell challenge, 7E5 treatment markedly reduced neutrophil recruitment and neutrophil extracellular trap (NET) formation. Similarly, the PLG inhibitor tranexamic acid (TXA) attenuated neutrophil recruitment, confirming the critical role of the PLG/PLM system in neutrophil migration. These findings highlight ENO1 as a key regulator of inflammation and neutrophil infiltration. Targeting ENO1 with antibodies could be a promising strategy to mitigate tissue damage caused by excessive neutrophilic inflammation.
Subjects
cell surface molecules
inflammation
neutrophil
SDGs
Publisher
Wiley
Type
journal article