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A myristoylated alanine-rich C-kinase substrate (MARCKS) inhibitor peptide attenuates neutrophil outside-in β(2)-integrin activation and signaling
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 β(2)-integrins. We hyp...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Taylor & Francis
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10348033/ https://www.ncbi.nlm.nih.gov/pubmed/37439125 http://dx.doi.org/10.1080/19336918.2023.2233204 |
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author | Conley, Haleigh Till, Rebecca L. Berglund, Alix K. Jones, Samuel L. Sheats, M. Katie |
author_facet | Conley, Haleigh Till, Rebecca L. Berglund, Alix K. Jones, Samuel L. Sheats, M. Katie |
author_sort | Conley, Haleigh |
collection | PubMed |
description | 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 β(2)-integrins. We hypothesized that MARCKS inhibition would alter neutrophil β(2)-integrin activation and signaling. We utilized a MARCKS-targeting peptide to inhibit MARCKS in inside-out and outside-in β(2)-integrin activation in neutrophils. MANS-mediated MARCKS inhibition had no significant effect on inside-out β(2)-integrin activation. MANS treatment significantly attenuated ICAM-1/Mn(2+)-stimulated static adhesion, cell spreading and β(2)-integrin clustering, suggesting a role for MARCKS function in outside-in β(2)-integrin activation. Additional work is needed to better understand the molecular mechanisms of MARCKS role in outside-in β(2)-integrin activation and signaling. |
format | Online Article Text |
id | pubmed-10348033 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Taylor & Francis |
record_format | MEDLINE/PubMed |
spelling | pubmed-103480332023-07-15 A myristoylated alanine-rich C-kinase substrate (MARCKS) inhibitor peptide attenuates neutrophil outside-in β(2)-integrin activation and signaling Conley, Haleigh Till, Rebecca L. Berglund, Alix K. Jones, Samuel L. Sheats, M. Katie Cell Adh Migr Research Paper 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 β(2)-integrins. We hypothesized that MARCKS inhibition would alter neutrophil β(2)-integrin activation and signaling. We utilized a MARCKS-targeting peptide to inhibit MARCKS in inside-out and outside-in β(2)-integrin activation in neutrophils. MANS-mediated MARCKS inhibition had no significant effect on inside-out β(2)-integrin activation. MANS treatment significantly attenuated ICAM-1/Mn(2+)-stimulated static adhesion, cell spreading and β(2)-integrin clustering, suggesting a role for MARCKS function in outside-in β(2)-integrin activation. Additional work is needed to better understand the molecular mechanisms of MARCKS role in outside-in β(2)-integrin activation and signaling. Taylor & Francis 2023-07-13 /pmc/articles/PMC10348033/ /pubmed/37439125 http://dx.doi.org/10.1080/19336918.2023.2233204 Text en © 2023 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group. https://creativecommons.org/licenses/by-nc/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (http://creativecommons.org/licenses/by-nc/4.0/ (https://creativecommons.org/licenses/by-nc/4.0/) ), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The terms on which this article has been published allow the posting of the Accepted Manuscript in a repository by the author(s) or with their consent. |
spellingShingle | Research Paper Conley, Haleigh Till, Rebecca L. Berglund, Alix K. Jones, Samuel L. Sheats, M. Katie A myristoylated alanine-rich C-kinase substrate (MARCKS) inhibitor peptide attenuates neutrophil outside-in β(2)-integrin activation and signaling |
title | A myristoylated alanine-rich C-kinase substrate (MARCKS) inhibitor peptide attenuates neutrophil outside-in β(2)-integrin activation and signaling |
title_full | A myristoylated alanine-rich C-kinase substrate (MARCKS) inhibitor peptide attenuates neutrophil outside-in β(2)-integrin activation and signaling |
title_fullStr | A myristoylated alanine-rich C-kinase substrate (MARCKS) inhibitor peptide attenuates neutrophil outside-in β(2)-integrin activation and signaling |
title_full_unstemmed | A myristoylated alanine-rich C-kinase substrate (MARCKS) inhibitor peptide attenuates neutrophil outside-in β(2)-integrin activation and signaling |
title_short | A myristoylated alanine-rich C-kinase substrate (MARCKS) inhibitor peptide attenuates neutrophil outside-in β(2)-integrin activation and signaling |
title_sort | myristoylated alanine-rich c-kinase substrate (marcks) inhibitor peptide attenuates neutrophil outside-in β(2)-integrin activation and signaling |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10348033/ https://www.ncbi.nlm.nih.gov/pubmed/37439125 http://dx.doi.org/10.1080/19336918.2023.2233204 |
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