Anti-microbial cetylpyridinium chloride suppresses mast cell function by targeting tyrosine phosphorylation of Syk kinase

Anti-microbial cetylpyridinium chloride suppresses mast cell function by targeting tyrosine phosphorylation of Syk kinase

Cetylpyridinium chloride (CPC) is a quaternary ammonium antimicrobial used in numerous personal care products, human food, cosmetic products, and cleaning solutions. Yet, there is minimal published data on CPC effects on eukaryotes, immune signaling, and human health. Previously, it was shown that l...

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Main Authors: Bright Obeng, Lucas J. Bennett, Bailey E. West, Dylan J. Wagner, Patrick J. Fleming, Morgan N. Tasker, Madeleine K. Lorenger, Dorothy R. Smith, Tetiana Systuk, Sydni M. Plummer, Jeongwon Eom, Marissa D. Paine, Collin T. Frangos, Michael P. Wilczek, Juyoung K. Shim, Melissa S. Maginnis, Julie A. Gosse
Format: Article
Language:English
Published: Taylor & Francis Group 2024-12-01
Series:Journal of Immunotoxicology
Subjects:
Mast cell
tyrosine phosphorylation
cetylpyridinium chloride
Syk kinase
LAT
Lyn
Online Access:https://www.tandfonline.com/doi/10.1080/1547691X.2024.2443397
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Summary:Cetylpyridinium chloride (CPC) is a quaternary ammonium antimicrobial used in numerous personal care products, human food, cosmetic products, and cleaning solutions. Yet, there is minimal published data on CPC effects on eukaryotes, immune signaling, and human health. Previously, it was shown that low-micromolar CPC inhibits rat mast cell function by inhibiting antigen (Ag)-stimulated Ca2+ mobilization, microtubule polymerization, and degranulation. In the current study, these findings are extended to human mast cells (LAD2); this paper presents data indicating that a mechanism of action for CPC might center on its positively-charged quaternary nitrogen in its pyridinium headgroup. The inhibitory effect of CPC was independent of signaling platform receptor architecture. Tyrosine phosphorylation events are a trigger of Ca2+ mobilization necessary for degranulation. CPC inhibits global tyrosine phosphorylation in Ag-stimulated mast cells. Specifically, CPC inhibits tyrosine phosphorylation of specific key players Syk kinase and LAT, a substrate of Syk. In contrast, CPC did not affect Lyn kinase phosphorylation. Thus, a root mechanism for CPC effect might be electrostatic disruption of particular tyrosine phosphorylation events essential for signaling. This work presented here outlines biochemical mechanisms underlying the effects of CPC on immune signaling.
ISSN:1547-691X
1547-6901

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