Extracellular MRP8/14 is a regulator of β2 integrin-dependent neutrophil slow rolling and adhesion.
(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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https://lup.lub.lu.se/record/5341247
- author
- organization
- publishing date
- 2015
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Nature Communications
- volume
- 6
- article number
- 6915
- publisher
- Nature Publishing Group
- external identifiers
-
- pmid:25892652
- wos:000353704100023
- scopus:84928486388
- pmid:25892652
- ISSN
- 2041-1723
- DOI
- 10.1038/ncomms7915
- language
- English
- LU publication?
- yes
- id
- 4bff7f96-0e64-4bda-9c41-08d4aaeff0af (old id 5341247)
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- http://www.ncbi.nlm.nih.gov/pubmed/25892652?dopt=Abstract
- date added to LUP
- 2016-04-01 14:33:49
- date last changed
- 2022-04-22 03:57:24
@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.}},
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 = {{https://lup.lub.lu.se/search/files/4038252/8227656}},
doi = {{10.1038/ncomms7915}},
volume = {{6}},
year = {{2015}},
}