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Extracellular MRP8/14 is a regulator of β2 integrin-dependent neutrophil slow rolling and adhesion.

Pruenster, Monika; Kurz, Angela R M; Chung, Kyoung-Jin; Cao-Ehlker, Xiao; Bieber, Stephanie; Nussbaum, Claudia F; Bierschenk, Susanne; Eggersmann, Tanja K; Rohwedder, Ina and Heinig, Kristina, et al. (2015) In Nature Communications 6.
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 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... (More)
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 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. (Less)
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Nature Communications
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6
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Nature Publishing Group
external identifiers
  • pmid:25892652
  • wos:000353704100023
  • scopus:84928486388
ISSN
2041-1723
DOI
10.1038/ncomms7915
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English
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yes
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4bff7f96-0e64-4bda-9c41-08d4aaeff0af (old id 5341247)
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http://www.ncbi.nlm.nih.gov/pubmed/25892652?dopt=Abstract
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2015-05-04 19:55:55
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@article{4bff7f96-0e64-4bda-9c41-08d4aaeff0af,
  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 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.},
  articleno    = {6915},
  author       = {Pruenster, Monika and Kurz, Angela R M and Chung, Kyoung-Jin and Cao-Ehlker, Xiao and Bieber, Stephanie and Nussbaum, Claudia F and Bierschenk, Susanne and Eggersmann, Tanja K and Rohwedder, Ina and Heinig, Kristina and Immler, Roland and Moser, Markus and Koedel, Uwe and Gran, Sandra and McEver, Rodger P and Vestweber, Dietmar and Verschoor, Admar and Leanderson, Tomas and Chavakis, Triantafyllos and Roth, Johannes and Vogl, Thomas and Sperandio, Markus},
  issn         = {2041-1723},
  language     = {eng},
  publisher    = {Nature Publishing Group},
  series       = {Nature Communications},
  title        = {Extracellular MRP8/14 is a regulator of β2 integrin-dependent neutrophil slow rolling and adhesion.},
  url          = {http://dx.doi.org/10.1038/ncomms7915},
  volume       = {6},
  year         = {2015},
}