Works (1)

Updated: July 5th, 2023 15:42

2014 journal article

Myristoylated Alanine Rich C Kinase Substrate (MARCKS) is essential to β2-integrin dependent responses of equine neutrophils

Veterinary Immunology and Immunopathology, 160(3-4), 167–176.

By: M. Sheats*, K. Pescosolido, E. Hefner*, E. Sung, K. Adler* & S. Jones*

author keywords: Neutrophil; Migration; Adhesion; Respiratory burst; Beta2-integrin; Inflammation
MeSH headings : Amino Acid Sequence; Animals; Antigen-Antibody Complex / physiology; CD18 Antigens / immunology; CD18 Antigens / physiology; Cell Adhesion / drug effects; Cell Adhesion / physiology; Cell Movement / drug effects; Cell Movement / physiology; Conserved Sequence; Horses / immunology; Horses / physiology; In Vitro Techniques; Intracellular Signaling Peptides and Proteins / antagonists & inhibitors; Intracellular Signaling Peptides and Proteins / genetics; Intracellular Signaling Peptides and Proteins / physiology; Membrane Proteins / antagonists & inhibitors; Membrane Proteins / genetics; Membrane Proteins / physiology; Molecular Sequence Data; Myristoylated Alanine-Rich C Kinase Substrate; Neutrophil Infiltration / drug effects; Neutrophil Infiltration / immunology; Neutrophil Infiltration / physiology; Peptide Fragments / genetics; Peptide Fragments / pharmacology; Respiratory Burst / drug effects; Sequence Homology, Amino Acid; Tetradecanoylphorbol Acetate / pharmacology
TL;DR: It is demonstrated that inhibition of MARCKS function significantly attenuates β2-integrin-dependent neutrophil functions including migration, adhesion, and immune complex-mediated respiratory burst, and strongly implicate MARC KS as a potential regulator of β 2-integrins in neutrophils. (via Semantic Scholar)
Sources: Web Of Science, NC State University Libraries, Crossref, ORCID
Added: August 6, 2018

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