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@ARTICLE{Rathnakumar:130388,
author = {K. Rathnakumar and S. Savant and H. Giri and A. Ghosh and
B. Fisslthaler and I. Fleming and U. Ram and A. K. Bera and
H. Augustin$^*$ and M. Dixit},
title = {{A}ngiopoietin-2 mediates thrombin-induced monocyte
adhesion and endothelial permeability.},
journal = {Journal of thrombosis and haemostasis},
volume = {14},
number = {8},
issn = {1538-7933},
address = {Oxford},
publisher = {Wiley-Blackwell},
reportid = {DKFZ-2017-05467},
pages = {1655 - 1667},
year = {2016},
abstract = {Essentials Mechanism of thrombin-induced inflammation is
not fully understood. Thrombin induced monocyte adhesion and
barrier loss require Angiopoietin-2 (Ang-2). Ang-2 mediates
vessel leakage and monocyte adhesion through SHP-2/p38MAPK
pathway. Calcium dependent SHP2/p38MAPK activation regulates
Ang-2 expression through a feedback loop.Background Thrombin
imparts an inflammatory phenotype to the endothelium by
promoting increased monocyte adhesion and vascular
permeability. However, the molecular players that govern
these events are incompletely understood. Objective The aim
of this study was to determine whether Angiopoietin-2
(Ang-2) has a role, if any, in regulating inflammatory
signals initiated by thrombin. Methods Assessment of
vascular leakage by Miles assay was performed by
intra-dermal injection on the foot paw. Surface levels of
intercellular adhesion molecule-1 (ICAM-1) were determined
by flow cytometry. Overexpression, knockdown and
phosphorylation of proteins were determined by Western
blotting. Results In time-course experiments,
thrombin-stimulated Ang-2 up-regulation, peaked prior to the
expression of adhesion molecule ICAM-1 in human umbilical
vein-derived endothelial cells (HUVECs). Knockdown of Ang-2
blocked both thrombin-induced monocyte adhesion and ICAM-1
expression. In addition, Ang-2(-/-) mice displayed defective
vascular leakage when treated with thrombin. Introducing
Ang-2 protein in Ang-2(-/-) mice failed to recover a
wild-type phenotype. Mechanistically, Ang-2 appears to
regulate the thrombin-activated calcium spike that is
required for tyrosine phosphatase SHP2 and p38 MAPK
activation. Further, down-regulation of SHP2 attenuated both
thrombin-induced Ang-2 expression and monocyte adhesion.
Down-regulation of the adaptor protein Gab1, a co-activator
of SHP2, as well as overexpression of the Gab1 mutant
incapable of interacting with SHP2 (YFGab1), inhibited
thrombin-mediated effects, including downstream activation
of p38 MAPK, which in turn was required for Ang-2
expression. Conclusions The data establish an essential role
of the Gab1/SHP2/p38MAPK signaling pathway and Ang-2 in
regulating thrombin-induced monocyte adhesion and vascular
leakage.},
cin = {A190},
ddc = {610},
cid = {I:(DE-He78)A190-20160331},
pnm = {321 - Basic Concepts (POF3-321)},
pid = {G:(DE-HGF)POF3-321},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:27241812},
doi = {10.1111/jth.13376},
url = {https://inrepo02.dkfz.de/record/130388},
}