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• W4384120411 startingPage "1" @default.
• W4384120411 abstract "MARCKS is an actin and PIP2-binding protein that plays an essential role in neutrophil migration and adhesion; however, the molecular details regarding MARCKS function in these processes remains unclear. Neutrophil adhesion and migration also require the cell surface receptors β2-integrins. We hypothesized that MARCKS inhibition would alter neutrophil β2-integrin activation and signaling. We utilized a MARCKS-targeting peptide to inhibit MARCKS in inside-out and outside-in β2-integrin activation in neutrophils. MANS-mediated MARCKS inhibition had no significant effect on inside-out β2-integrin activation. MANS treatment significantly attenuated ICAM-1/Mn2+-stimulated static adhesion, cell spreading and β2-integrin clustering, suggesting a role for MARCKS function in outside-in β2-integrin activation. Additional work is needed to better understand the molecular mechanisms of MARCKS role in outside-in β2-integrin activation and signaling." @default.
• W4384120411 created "2023-07-14" @default.
• W4384120411 creator A5005628118 @default.
• W4384120411 creator A5008681306 @default.
• W4384120411 creator A5022199193 @default.
• W4384120411 creator A5047008308 @default.
• W4384120411 creator A5056519418 @default.
• W4384120411 date "2023-07-13" @default.
• W4384120411 modified "2023-09-27" @default.
• W4384120411 title "A myristoylated alanine-rich C-kinase substrate (MARCKS) inhibitor peptide attenuates neutrophil outside-in β₂-integrin activation and signaling" @default.
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