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2014 ; 124
(15
): 2421-30
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Paired immunoglobulin-like receptor B regulates platelet activation
#MMPMID25075127
Fan X
; Shi P
; Dai J
; Lu Y
; Chen X
; Liu X
; Zhang K
; Wu X
; Sun Y
; Wang K
; Zhu L
; Zhang CC
; Zhang J
; Chen GQ
; Zheng J
; Liu J
Blood
2014[Oct]; 124
(15
): 2421-30
PMID25075127
show ga
Murine paired immunoglobulin-like receptors B (PIRB), as the ortholog of human
leukocyte immunoglobulin-like receptor B2 (LILRB2), is involved in a variety of
biological functions. Here, we found that PIRB and LILRB2 were expressed in mouse
and human platelets, respectively. PIRB intracellular domain deletion (PIRB-TM)
mice had thrombocythemia and significantly higher proportions of megakaryocytes
in bone marrow. Agonist-induced aggregation and spreading on immobilized
fibrinogen were facilitated in PIRB-TM platelets. The rate of clot retraction in
platelet-rich plasma containing PIRB-TM platelets was also increased.
Characterization of signaling confirmed that PIRB associated with phosphatases
Shp1/2 in platelets. The phosphorylation of Shp1/2 was significantly
downregulated in PIRB-TM platelets stimulated with collagen-related peptide (CRP)
or on spreading. The results further revealed that the phosphorylation levels of
the linker for activation of T cells, SH2 domain-containing leukocyte protein of
76kDa, and phospholipase C were enhanced in PIRB-TM platelets stimulated with
CRP. The phosphorylation levels of FAK Y397 and integrin ?3 Y759 were also
enhanced in PIRB-TM platelet spread on fibrinogen. The PIRB/LILRB2 ligand
angiopoietin-like-protein 2 (ANGPTL2) was expressed and stored in platelet
?-granules. ANGPTL2 inhibited agonist-induced platelet aggregation and spreading
on fibrinogen. The data presented here reveal that PIRB and its ligand ANGPTL2
possess an antithrombotic function by suppressing collagen receptor glycoprotein
VI and integrin ?IIb?3-mediated signaling.
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