Extracellular MRP8/14 is a regulator of β22 integrin-dependent neutrophil slow rolling and adhesion

Monika Pruenster, Angela R.M. Kurz, Kyoung Jin Chung, Xiao Cao-Ehlker, Stephanie Bieber, Claudia F. Nussbaum, Susanne Bierschenk, Tanja K. Eggersmann, Ina Rohwedder, Kristina Heinig, Roland Immler, Markus Moser, Uwe Koedel, Sandra Gran, Rodger P. McEver, Dietmar Vestweber, Admar Verschoor, Tomas Leanderson, Triantafyllos Chavakis, Johannes RothThomas Vogl, Markus Sperandio*

*Corresponding author for this work
81 Citations (Scopus)


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 β 22 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.

Original languageEnglish
Article number6915
JournalNature Communications
Publication statusPublished - 20.04.2015

Research Areas and Centers

  • Academic Focus: Center for Infection and Inflammation Research (ZIEL)


Dive into the research topics of 'Extracellular MRP8/14 is a regulator of β22 integrin-dependent neutrophil slow rolling and adhesion'. Together they form a unique fingerprint.

Cite this