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The role of PECAM‐1 mediated signaling in neutrophil polarization.
Author(s) -
Khan Mohammed Azizuddin,
Shin JaeWon,
Komarova Yulia,
Malik Asrar
Publication year - 2017
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.31.1_supplement.827.8
Subject(s) - microbiology and biotechnology , cytoskeleton , rhoa , actin cytoskeleton , actin , fibronectin , cytochalasin d , neutrophil extracellular traps , chemistry , cell migration , vinculin , focal adhesion , signal transduction , biology , cell , immunology , inflammation , biochemistry , extracellular matrix
PECAM‐1, also known as CD31, is a 150kDA transmembrane glycoprotein comprised of six extracellular Ig repeats that form trans ‐interactions with PECAM‐1 on the cell surface of endothelial cells. Neutrophil trans‐endothelial migration (TEM) is critically dependent on these interactions. While the role of PECAM‐1‐mediated signaling in endothelial cells is well‐studied, and linked to activation of calcium flux, and re‐organization of actin cytoskeleton, the role of PECAM‐1 in neutrophils remains unclear. Hence, we investigated this question using PECAM‐1 coated biomimetic surfaces. We report here that PECAM‐1 homophillic ligation induces prompt nucleation of actin cytoskeleton and neutrophil polarization without the presence of a chemoattactant (fMLF). This was not seen when neutrophils were seated on biomimetic glass coated with fibronectin. We also observed an increase in SHP2 and RhoGTPase activity at the sites of PECAM‐1 homophilic interaction. We propose that PECAM‐1 induces SHP2/RhoA signaling and the resultant polymerization of actin cytoskeleton through the mDia2 pathway. Hence, our data suggests a novel role of PECAM‐1 in neutrophil TEM.