Enolase-1 is essential for neutrophil recruitment during acute inflammation
Lu, H.-Y.; Huang, P.-H.; Lee, T.-W.; Chang, H.-W.; Chen, N.-Y.; Zhuang, Y.-J.; Yuan, T.-T.; Chen, C.-J.
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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 transmigration. 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. Moreover, 7E5 neutralized the immunostimulatory activity of soluble ENO1, which was significantly elevated in circulation during acute inflammation. 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.
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