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Your search keyword '"Xu, Jingsong"' showing total 5 results
Start Over Author "Xu, Jingsong" Journal nature immunology
5 results on '"Xu, Jingsong"'

1. Bidirectional Regulation of Neutrophil Migration by MAP Kinases

Author

Liu, Xiaowen, Ma, Bo, Malik, Asrar B., Tang, Haiyang, Yang, Tao, Sun, Bo, Wang, Gang, Minshall, Richard D., Li, Yan, Zhao, Yong, Ye, Richard D., and Xu, Jingsong

Subjects
Flavonoids, Mice, Knockout, G-Protein-Coupled Receptor Kinase 2, Neutrophils, Pyridines, Imidazoles, HL-60 Cells, Receptors, Formyl Peptide, p38 Mitogen-Activated Protein Kinases, Article, N-Formylmethionine Leucyl-Phenylalanine, Chemotaxis, Leukocyte, Mice, HEK293 Cells, Animals, Humans, Extracellular Signal-Regulated MAP Kinases, Signal Transduction
Abstract

To kill invading bacteria, neutrophils must interpret spatial cues, migrate and reach target sites. Although the initiation of chemotactic migration has been extensively studied, little is known about its termination. Here we found that two mitogen-activated protein kinases (MAPKs) had opposing roles in neutrophil trafficking. The extracellular signal-regulated kinase Erk potentiated activity of the G protein-coupled receptor kinase GRK2 and inhibited neutrophil migration, whereas the MAPK p38 acted as a noncanonical GRK that phosphorylated the formyl peptide receptor FPR1 and facilitated neutrophil migration by blocking GRK2 function. Therefore, the dynamic balance between Erk and p38 controlled neutrophil 'stop' and 'go' activity, which ensured that neutrophils reached their final destination as the first line of host defense.

Published
2012

4. Nonmuscle myosin light-chain kinase mediates neutrophil transmigration in sepsis-induced lung inflammation by activating β2 integrins.

Author

Xu, Jingsong, Gao, Xiao-Pei, Ramchandran, Ramaswamy, Zhao, You-Yang, Vogel, Stephen M, and Malik, Asrar B

Abstract

Nonmuscle myosin light-chain kinase (MYLK) mediates increased lung vascular endothelial permeability in lipopolysaccharide-induced lung inflammatory injury, the chief cause of the acute respiratory distress syndrome. In a lung injury model, we demonstrate here that MYLK was also essential for neutrophil transmigration, but that this function was mostly independent of myosin II regulatory light chain, the only known substrate of MYLK. Instead, MYLK in neutrophils was required for the recruitment and activation of the tyrosine kinase Pyk2, which mediated full activation of β2 integrins. Our results demonstrate that MYLK-mediated activation of β2 integrins through Pyk2 links β2 integrin signaling to the actin motile machinery of neutrophils. [ABSTRACT FROM AUTHOR]

Published
2008
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5. Nonmuscle myosin light-chain kinase mediates neutrophil transmigration in sepsis-induced lung inflammation by activating beta2 integrins.

Author

Xu J, Gao XP, Ramchandran R, Zhao YY, Vogel SM, and Malik AB

Subjects
Animals, Mice, Pneumonia pathology, Pneumonia physiopathology, Sepsis genetics, Sepsis physiopathology, CD18 Antigens metabolism, Myosin-Light-Chain Kinase genetics, Neutrophils pathology, Pneumonia metabolism, Sepsis immunology
Abstract

Nonmuscle myosin light-chain kinase (MYLK) mediates increased lung vascular endothelial permeability in lipopolysaccharide-induced lung inflammatory injury, the chief cause of the acute respiratory distress syndrome. In a lung injury model, we demonstrate here that MYLK was also essential for neutrophil transmigration, but that this function was mostly independent of myosin II regulatory light chain, the only known substrate of MYLK. Instead, MYLK in neutrophils was required for the recruitment and activation of the tyrosine kinase Pyk2, which mediated full activation of beta(2) integrins. Our results demonstrate that MYLK-mediated activation of beta(2) integrins through Pyk2 links beta(2) integrin signaling to the actin motile machinery of neutrophils.

Published
2008
Full Text
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