Extracellular MRP8/14 is a regulator of β2 integrin-dependent neutrophil slow rolling and adhesion
Copyright policy )Extracellular MRP8/14 is a regulator of β2 integrin-dependent neutrophil slow rolling and adhesion
AbstractMyeloid-related proteins (MRPs) 8 and 14 are cytosolic proteins secreted from myeloid cells as proinflammatory mediators. Currently, the functional role of circulating extracellular MRP8/14 is unclear. Our present study identifies extracellular MRP8/14 as an autocrine player in the leukocyte adhesion cascade. We show that E-selectin–PSGL-1 interaction during neutrophil rolling triggers Mrp8/14 secretion. Released MRP8/14 in turn activates a TLR4-mediated, Rap1-GTPase-dependent pathway of rapid β2 integrin activation in neutrophils. This extracellular activation loop reduces leukocyte rolling velocity and stimulates adhesion. Thus, we identify Mrp8/14 and TLR4 as important modulators of the leukocyte recruitment cascade during inflammation in vivo.
- Technical University of Munich Germany
- Max Planck Society Germany
- Institut für Immunologie Germany
- TU Dresden Germany
- Oklahoma Medical Research Foundation United States
Inflammation, Male, Mice, Knockout, Neutrophils, Macrophages, Immunology in the medical area, Article, Mice, Hyaluronan Receptors, Gene Expression Regulation, CD18 Antigens, Immunology in the Medical Area (including Cell and Immunotherapy), Cell Adhesion, Animals, Calgranulin B, Calgranulin A, Leukocyte Rolling, Protein Binding, ddc: ddc:
Inflammation, Male, Mice, Knockout, Neutrophils, Macrophages, Immunology in the medical area, Article, Mice, Hyaluronan Receptors, Gene Expression Regulation, CD18 Antigens, Immunology in the Medical Area (including Cell and Immunotherapy), Cell Adhesion, Animals, Calgranulin B, Calgranulin A, Leukocyte Rolling, Protein Binding, ddc: ddc:
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