Beyond Pattern Recognition: TLR2 Promotes Chemotaxis, Cell Adhesion, and Migration in THP-1 Cells

The interaction between monocytes and endothelial cells in inflammation is central to chemoattraction, adhesion, and transendothelial migration. Key players, such as selectins and their ligands, integrins, and other adhesion molecules, and their functions in these processes are well studied. Toll-li...

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Bibliographic Details
Published in:Cells (Basel, Switzerland) Switzerland), 2023-05, Vol.12 (10), p.1425
Main Authors: Colleselli, Katrin, Ebeyer-Masotta, Marie, Neuditschko, Benjamin, Stierschneider, Anna, Pollhammer, Christopher, Potocnjak, Mia, Hundsberger, Harald, Herzog, Franz, Wiesner, Christoph
Format: Article
Language:English
Subjects:
Actin
Cancer cells
Cell Adhesion
Cell adhesion & migration
Cell culture
cell migration
Chemotaxis
E coli
Endothelial cells
Endothelial Cells - metabolism
Endothelium
Gene expression
Genetic aspects
Humans
Immune response
Inflammation
Integrins
Leukocyte migration
Ligands
Mass spectroscopy
Monocytes
Pattern recognition
Penicillin
Physiological aspects
Proteins
Selectins
String protein
THP-1
THP-1 Cells
TLR2 protein
Toll-like receptor 2
Toll-Like Receptor 2 - metabolism
Toll-like receptors
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Summary:The interaction between monocytes and endothelial cells in inflammation is central to chemoattraction, adhesion, and transendothelial migration. Key players, such as selectins and their ligands, integrins, and other adhesion molecules, and their functions in these processes are well studied. Toll-like receptor 2 (TLR2), expressed in monocytes, is critical for sensing invading pathogens and initiating a rapid and effective immune response. However, the extended role of TLR2 in monocyte adhesion and migration has only been partially elucidated. To address this question, we performed several functional cell-based assays using monocyte-like wild type (WT), TLR2 knock-out (KO), and TLR2 knock-in (KI) THP-1 cells. We found that TLR2 promotes the faster and stronger adhesion of monocytes to the endothelium and a more intense endothelial barrier disruption after endothelial activation. In addition, we performed quantitative mass spectrometry, STRING protein analysis, and RT-qPCR, which not only revealed the association of TLR2 with specific integrins but also uncovered novel proteins affected by TLR2. In conclusion, we show that unstimulated TLR2 influences cell adhesion, endothelial barrier disruption, migration, and actin polymerization.
ISSN:2073-4409
2073-4409
DOI:10.3390/cells12101425