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IL‐12 and IL‐18 induce MAP kinase‐dependent adhesion of T cells to extracellular matrix components
Author(s) -
Ariel Amiram,
Novick Daniela,
Rubinstein Menachem,
Dinarello Charles A.,
Lider Ofer,
Hershkoviz Rami
Publication year - 2002
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1189/jlb.72.1.192
Subject(s) - microbiology and biotechnology , fibronectin , biology , proinflammatory cytokine , extracellular matrix , cell adhesion molecule , cell adhesion , chemokine , integrin , inflammation , immunology , cell , biochemistry
Cytokines and chemokines play an essential role in recruiting leukocytes from the circulation to the peripheral sites of inflammation by modulating cellular interactions with endothelial cell ligands and extracellular matrix (ECM). Herein, we examined regulation of T cell adhesion to ECM ligands by two major proinflammatory cytokines, interleukin (IL)‐12 and IL‐18. IL‐12 and IL‐18 induced T cell adhesion to fibronectin (FN) and hyaluronic acid at low (pM) concentrations that were mediated by specific adhesion molecules expressed on the T cell surface, namely, β 1 integrins and CD44, respectively. The induction of adhesion by IL‐12 and IL‐18 was inhibited by extracellular signal‐regulated kinase and p38 mitogen‐activated protein kinase inhibitors (PD098059 and SB203580, respectively). In contrast, IL‐12‐ and IL‐18‐induced interferon‐γ (INF‐γ) secretion from T cells was inhibited by SB203580, but not by PD098059. It is interesting that low concentrations of IL‐12 and IL‐18 induced T cell adhesion to FN in a synergistic manner. Thus, in addition to the regulation of late inflammatory functions such as INF‐γ production, IL‐12 and IL‐18, alone or in combination, regulate early inflammatory events such as T cell adhesion to inflamed sites.