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Blood, 1 August 2001, Vol. 98, No. 3, pp. 667-673
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
The p38 mitogen-activated protein kinase pathway plays a critical
role in thrombin-induced endothelial chemokine production and
leukocyte recruitment
Valérie Marin,
Catherine Farnarier,
Sandra Grès,
Solange Kaplanski,
Michael S.-S. Su,
Charles A. Dinarello, and
Gilles Kaplanski
From the Laboratoire d'Immunologie-INSERM U387,
Hôpital Sainte- Marguerite, Marseille, France; Vertex
Pharmaceutical, Cambridge, MA; and Division of Infectious Diseases,
University of Colorado Health Sciences Center, Denver.
Thrombin, the terminal serine protease in the coagulation cascade,
is a proinflammatory molecule in vivo and induces endothelial activation in vitro. The cellular signaling mechanisms involved in this
function are unknown. The role of the p38 mitogen-activated protein
kinase (MAPK) signaling pathway in thrombin-induced chemokine production was studied. Phosphorylation of both p38 MAPK and its substrate, ATF-2, was observed in human umbilical vein endothelial cells (HUVECs) stimulated with thrombin, with a maximum after 5 minutes
of stimulation. Using the selective p38 MAPK inhibitor SB203580, there
was a significant decrease in thrombin-induced interleukin-8 (IL-8) and
monocyte chemotactic protein-1 (MCP-1) protein production and messenger
RNA steady-state levels. In addition, SB203580 decreased IL-8 and MCP-1
production induced by the thrombin receptor-1 agonist peptide (TRAP),
suggesting functional links between the thrombin G protein-coupled
receptor and the p38 MAPK pathway. Furthermore, endothelial activation
in the presence of SB203580 decreased the chemotactic activity of
thrombin-stimulated HUVEC supernatant on neutrophils and monocytic
cells. In contrast, the p42/p44 MAPK pathway did not appear to be
involved in thrombin- or TRAP-induced endothelial chemokine production,
because there was no reduction in the presence of the p42/p44-specific
inhibitor PD98059. These results demonstrate that the p38 rather than
p42/44 MAPK signaling pathway plays an important role in
thrombin-induced endothelial proinflammatory activation and suggest
that inhibition of p38 MAPK may be an interesting target for
anti-inflammatory strategies in vascular diseases combining thrombosis
and inflammation.
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