Published online before print January 21, 2009
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, PKC-
, ERK-1/2, and p38 MAPK in migration of human asthmatic eosinophils
* Unité de Recherche en Pneumologie, Centre de Recherche de lHôpital Laval, Institut Universitaire de Cardiologie et de Pneumologie de lUniversité Laval, Québec City, Quebec, Canada; and
Immunology Division, Department of Pediatrics, Faculty of Medicine, Université de Sherbrooke, Sherbrooke, Quebec, Canada
1 Correspondence: Hôpital Laval, 2725 Chemin Sainte-Foy, Québec City, Quebec, Canada, G1V 4G5. E-mail: michel.laviolette{at}med.ulaval.ca
Asthma is associated with an eosinophil infiltration into the bronchial mucosa. 5-Oxo-6,8,11,14(E,Z,Z,Z)-eicosatetraenoic acid (5-oxo-ETE), a potent eosinophil chemotactic factor, activates cell motility, adherence, and proteolysis, notably, by promoting CD11b expression, matrix metalloproteinase (MMP)-9 secretion, and plasmin generation. We investigated the intracellular signaling pathways implicated in these various steps by using different, selective inhibitors. Human eosinophil migration through a reconstituted basement membrane in response to 5-oxo-ETE was greatly inhibited (
72%) by the protein kinase C (PKC)-
, PKC-
, ERK-1/2, and p38 inhibitors. Our findings indicate that PKC-
mediates cell motility, CD11b expression, and MMP-9 granule release. PKC-
is also largely involved in eosinophil migration, although its specific targets remain undefined. ERK-1/2 and p38 modulate CD11b expression; ERK-1/2 is also involved in long-term MMP-9 secretion and p38 in the plasmin activation system. We demonstrated the crucial implication of PKC-
, PKC-
, ERK-1/2, and p38 in human blood eosinophil migration through extracellular matrix components. Targeting specific pathways may have therapeutic potential for the treatment of allergic airway inflammation.
Key Words: matrix metalloproteinase urokinase plasminogen activator plasmin 5-oxo-6 8 11 14(E,Z,Z,Z)-eicosatetraenoic acid mitogen-activated protein kinase