L-selectin mechanochemistry restricts neutrophil priming in vivo View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2017-05-12

AUTHORS

Zhenghui Liu, Tadayuki Yago, Nan Zhang, Sumith R. Panicker, Ying Wang, Longbiao Yao, Padmaja Mehta-D’souza, Lijun Xia, Cheng Zhu, Rodger P. McEver

ABSTRACT

Circulating neutrophils must avoid premature activation to prevent tissue injury. The leukocyte adhesion receptor L-selectin forms bonds with P-selectin glycoprotein ligand-1 (PSGL-1) on other leukocytes and with peripheral node addressin (PNAd) on high endothelial venules. Mechanical forces can strengthen (catch) or weaken (slip) bonds between biological molecules. How these mechanochemical processes influence function in vivo is unexplored. Here we show that mice expressing an L-selectin mutant (N138G) have altered catch bonds and prolonged bond lifetimes at low forces. Basal lymphocyte homing and neutrophil recruitment to inflamed sites are normal. However, circulating neutrophils form unstable aggregates and are unexpectedly primed to respond robustly to inflammatory mediators. Priming requires signals transduced through L-selectin N138G after it engages PSGL-1 or PNAd. Priming enhances bacterial clearance but increases inflammatory injury and enlarges venous thrombi. Thus, L-selectin mechanochemistry limits premature activation of neutrophils. Our results highlight the importance of probing how mechanochemistry functions in vivo. More... »

PAGES

15196

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/ncomms15196

DOI

http://dx.doi.org/10.1038/ncomms15196

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1085390174

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/28497779


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