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2015 ; 126
(12
): 1483-93
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Platelets induce apoptosis via membrane-bound FasL
#MMPMID26232171
Schleicher RI
; Reichenbach F
; Kraft P
; Kumar A
; Lescan M
; Todt F
; Göbel K
; Hilgendorf I
; Geisler T
; Bauer A
; Olbrich M
; Schaller M
; Wesselborg S
; O'Reilly L
; Meuth SG
; Schulze-Osthoff K
; Gawaz M
; Li X
; Kleinschnitz C
; Edlich F
; Langer HF
Blood
2015[Sep]; 126
(12
): 1483-93
PMID26232171
show ga
After tissue injury, both wound sealing and apoptosis contribute to restoration
of tissue integrity and functionality. Although the role of platelets (PLTs) for
wound closure and induction of regenerative processes is well established, the
knowledge about their contribution to apoptosis is incomplete. Here, we show that
PLTs present the death receptor Fas ligand (FasL) on their surface after
activation. Activated PLTs as well as the isolated membrane fraction of activated
PLTs but not of resting PLTs induced apoptosis in a dose-dependent manner in
primary murine neuronal cells, human neuroblastoma cells, and mouse embryonic
fibroblasts. Membrane protein from PLTs lacking membrane-bound FasL (FasL(?m/?m))
failed to induce apoptosis. Bax/Bak-mediated mitochondrial apoptosis signaling in
target cells was not required for PLT-induced cell death, but increased the
apoptotic response to PLT-induced Fas signaling. In vivo, PLT depletion
significantly reduced apoptosis in a stroke model and an inflammation-independent
model of N-methyl-d-aspartic acid-induced retinal apoptosis. Furthermore,
experiments using PLT-specific PF4Cre(+) FasL(fl/fl) mice demonstrated a role of
PLT-derived FasL for tissue apoptosis. Because apoptosis secondary to injury
prevents inflammation, our findings describe a novel mechanism on how PLTs
contribute to tissue homeostasis.
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