Activated protein C ligation of ApoER2 (LRP8) causes Dab1-dependent signaling in U937 cells

Binding of activated protein C (APC) to cells triggers multiple beneficial cytoprotective activities that suppress apoptosis, inflammation, and endothelial barrier breakdown. One paradigm for APC's signaling emphasizes its binding to endothelial cell protein C receptor (EPCR) and subsequent pro...

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Veröffentlicht in:Proceedings of the National Academy of Sciences - PNAS 2009-01, Vol.106 (1), p.274-279
Hauptverfasser: Yang, Xia V, Banerjee, Yajnavalka, Fernández, José A, Deguchi, Hiroshi, Xu, Xiao, Mosnier, Laurent O, Urbanus, Rolf.T, de Groot, Phillip G, White-Adams, Tara C, McCarty, Owen J.T, Griffin, John H
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container_title Proceedings of the National Academy of Sciences - PNAS
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creator Yang, Xia V
Banerjee, Yajnavalka
Fernández, José A
Deguchi, Hiroshi
Xu, Xiao
Mosnier, Laurent O
Urbanus, Rolf.T
de Groot, Phillip G
White-Adams, Tara C
McCarty, Owen J.T
Griffin, John H
description Binding of activated protein C (APC) to cells triggers multiple beneficial cytoprotective activities that suppress apoptosis, inflammation, and endothelial barrier breakdown. One paradigm for APC's signaling emphasizes its binding to endothelial cell protein C receptor (EPCR) and subsequent protease activated receptor (PAR)-1 activation. Here we used human monocytic-like U937 cells to evaluate apolipoprotein E receptor 2 (ApoER2)-dependent signaling by APC and found that APC initiated rapid phosphorylation of Tyr-220 in the adaptor protein disabled-1 (Dab1) and of Ser-473 in Akt. APC also induced phosphorylation of Ser-9 in glycogen synthase kinase 3β (GSK3β), which was blocked by the PI3K inhibitor LY294002. Receptor-associated protein (RAP), a general antagonist for binding of ligands to LDL receptor family members, inhibited APC-induced phosphorylation of Dab1 and GSK3β, whereas anti-EPCR or anti-PAR1 blocking antibodies did not. Knocking down ApoER2 by using siRNA-ablated APC induced Dab1 phosphorylation, suggesting that RAP-sensitive APC-induced signaling requires ApoER2. In surface plasmon resonance equilibrium binding studies, APC bound with high affinity to soluble (s) ApoER2 (apparent Kd, [almost equal to]30 nM) but not to soluble very low density lipoprotein receptor. RAP blocked APC binding to sApoER2 but not to sEPCR. RAP blocked binding of U937 cells to immobilized APC. RAP also blocked APC's ability to inhibit endotoxin-induced tissue factor pro-coagulant activity of U937 cells. Thus, we propose that ligation of ApoER2 by APC signals via Dab1 phosphorylation and subsequent activation of PI3K and Akt and inactivation of GSK3β, thereby contributing to APC's beneficial effects on cells.
doi_str_mv 10.1073/pnas.0807594106
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subjects Adaptor Proteins, Signal Transducing - metabolism
Binding sites
Biological Sciences
Blood Coagulation Factors
Cells
Glycogen Synthase Kinase 3 - metabolism
Humans
Kinases
LDL-Receptor Related Proteins
Monocytes - cytology
Nerve Tissue Proteins - metabolism
Phosphatidylinositol 3-Kinases - metabolism
Phosphorylation
Proteases
Protein Binding
Protein C - metabolism
Proteins
Proto-Oncogene Proteins c-akt - metabolism
Receptors, Cell Surface
Receptors, Lipoprotein - metabolism
Signal Transduction
U937 Cells
title Activated protein C ligation of ApoER2 (LRP8) causes Dab1-dependent signaling in U937 cells
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