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Extracellular MRP8/14 is a regulator of beta 2 integrin-dependent neutrophil slow rolling and adhesion

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Moser,  Markus
Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Pruenster, M., Kurz, A. R. M., Chung, K.-J., Cao-Ehlker, X., Bieber, S., Nussbaum, C. F., et al. (2015). Extracellular MRP8/14 is a regulator of beta 2 integrin-dependent neutrophil slow rolling and adhesion. NATURE COMMUNICATIONS, 6: 6915. doi:10.1038/ncomms7915.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0027-1195-F
Abstract
Myeloid-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 beta 2 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.