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2017 ; 8
(ä): 15196
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L-selectin mechanochemistry restricts neutrophil priming in vivo
#MMPMID28497779
Liu Z
; Yago T
; Zhang N
; Panicker SR
; Wang Y
; Yao L
; Mehta-D'souza P
; Xia L
; Zhu C
; McEver RP
Nat Commun
2017[May]; 8
(ä): 15196
PMID28497779
show ga
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.