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• W3104828519 abstract "Abstract Neutrophil activation has a pathogenic effect in inflammatory diseases. Protein kinase B (PKB)/AKT regulates diverse cellular responses. However, the significance of AKT in neutrophilic inflammation is still not well understood. Here, we identified CLLV-1 as a novel AKT inhibitor. CLLV-1 inhibited respiratory burst, degranulation, chemotaxis, and AKT phosphorylation in activated human neutrophils and dHL-60 cells. Significantly, CLLV-1 blocked AKT activity and covalently reacted with AKT Cys310 in vitro . The AKT 309-313 peptide-CLLV-1 adducts were determined by NMR or mass spectrometry assay. The alkylation agent-conjugated AKT (reduced form) level was also inhibited by CLLV-1. Additionally, CLLV-1 ameliorated lipopolysaccharide (LPS)-induced acute lung injury (ALI) in mice. CLLV-1 acts as a covalent allosteric AKT inhibitor by targeting AKT Cys310 to restrain inflammatory responses in human neutrophils and LPS-induced ALI in vivo . Our findings provide a mechanistic framework for redox modification of AKT that may serve as a novel pharmacological target to alleviate neutrophilic inflammation." @default.
• W3104828519 created "2020-11-23" @default.
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• W3104828519 date "2018-02-13" @default.
• W3104828519 modified "2023-10-14" @default.
• W3104828519 title "Targeting redox regulatory site of protein kinase B impedes neutrophilic inflammation in lung injury" @default.
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• W3104828519 doi "https://doi.org/10.1101/264184" @default.
• W3104828519 hasPublicationYear "2018" @default.
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