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(Journal of Leukocyte Biology. 2000;68:737-747.)
© 2000 by Society for Leukocyte Biology

Fibronectin-bound TNF-{alpha} stimulates monocyte matrix metalloproteinase-9 expression and regulates chemotaxis

Gayle G. Vaday*, Rami Hershkoviz{dagger}, Michal A. Rahat{ddagger}, Nitza Lahat{ddagger}, Liora Cahalon* and Ofer Lider*

* Department of Immunology, The Weizmann Institute of Science, Rehovot;
{dagger} Department of Internal Medicine, Meir Hospital, Kfar Saba; and
{ddagger} Immunology Research Unit, Lady Davis Carmel Medical Center, Haifa, Israel

Correspondence: Ofer Lider, Ph.D., Dept. of Immunology, The Weizmann Institute of Science, Rehovot 76100, Israel. E-mail: ofer.lider{at}weizmann.ac.il

Tumor necrosis factor {alpha} (TNF-{alpha}) is a proinflammatory cytokine implicated in the stimulation of matrix metalloproteinase (MMP) production by several cell types. Our previous studies demonstrated that TNF-{alpha} avidly binds fibronectin (FN) and laminin, major adhesive glycoproteins of extracellular matrix (ECM) and basement membranes. These findings suggested that TNF-{alpha} complexing to insoluble ECM components may serve to concentrate its activities to distinct inflamed sites. Herein, we explored the bioactivity and possible function of ECM-bound TNF-{alpha} by examining its effects on MMP-9 secretion by monocytes. Immunofluorescent staining indicated that LPS-activated monocytes deposited newly synthesized TNF-{alpha} into ECM-FN. FN-bound TNF-{alpha} (FN/TNF-{alpha}) significantly up-regulated MMP-9 expression and secretion by the human monocytic cell line MonoMac-6 and peripheral blood monocytes. Such secretion could be inhibited by antibodies that block TNF-{alpha} activity and binding to its receptors TNF RI (p55) and TNF RII (p75). Chemotaxis through ECM gels in the presence of soluble or bound TNF-{alpha} was inhibited by a hydroxamic acid inhibitor of MMPs (GM6001). It is interesting that, although the adhesion of MonoMac-6 cells to FN/TNF-{alpha} required functional activated ß1 integrins, FN/TNF-{alpha}-induced MMP-9 secretion was independent of binding to ß1 integrins, since MMP-9 secretion was unaffected by: (1) neutralizing mAb to {alpha}4, {alpha}5, and ß1 subunits, which blocked cell adhesion; (2) a mAb that stimulated ß1 integrin-mediated adhesion; and (3) binding TNF-{alpha} to the 30-kDa amino-terminal fragment of FN, which lacks the major cell adhesive binding sites. Thus, in addition to their cell-adhesive roles, ECM glycoproteins, such as FN, may play a pivotal role in presenting proinflammatory cytokines to leukocytes within the actual inflamed tissue, thereby affecting their capacities to secrete ECM-degrading enzymes. These TNF-{alpha}-ECM interactions may serve to limit the cytokine’s availability and bioactivity to target areas of inflammation.

Key Words: inflammation • gelatinase • extracellular matrix




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