2023 journal article

A myristoylated alanine-rich C-kinase substrate (MARCKS) inhibitor peptide attenuates neutrophil outside-in & beta;(2)-integrin activation and signaling

A myristoylated alanine-rich C-kinase substrate (MARCKS) inhibitor peptide attenuates neutrophil outside-in & beta;(2)-integrin activation and signaling. CELL ADHESION & MIGRATION, 17(1), 1–16.

By: H. Conley n, R. Till n, A. Berglund n, S. Jones n & M. Sheats n

co-author countries: United States of America 🇺🇸
author keywords: Beta2-integrin; ICAM-1; MARCKS; neutrophils; outside-in; >
MeSH headings : Alanine; CD18 Antigens / metabolism; Neutrophils; Peptides / pharmacology; Signal Transduction; Myristoylated Alanine-Rich C Kinase Substrate / antagonists & inhibitors
Source: Web Of Science
Added: July 31, 2023

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.