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B Transcription Factors in Mononuclear Phagocytes1
*
Pulmonary and Critical Care Medicine Division and
Hematology-Oncology Division, Department of Internal Medicine, University of Michigan, Ann Arbor, MI 48109
Adhesion to extracellular matrices is known to modulate leukocyte
activation, although the mechanisms are not fully understood.
Mononuclear phagocytes are exposed to fibrinous provisional matrix
throughout migration into inflammatory foci, so this study was
undertaken to determine whether fibrinogen triggers activation of
NF-
B transcription factors. U937 cells differentiated with PMA in
nonadherent culture were shown to express two fibrinogen-binding
integrins, predominately CD11b/CD18, and to a lesser extent,
CD11c/CD18. Cells stimulated with fibrinogen (10–100
µg/ml)/Mn2+ (50 µM) for 2 h were examined by
electrophoretic mobility shift assay. NF-B activation, minimal in
unstimulated cells, was substantially up-regulated by fibrinogen.
Fibrinogen also caused activation of AP-1, but not SP1 or cAMP response
element-binding protein (CREB) factors. Blocking mAbs against CD18 and
CD11b abrogated fibrinogen-induced NF-B activation. To determine the
effects on transcriptional regulation, U937 cells were transfected with
a plasmid containing the HIV-1 enhancer (bearing two NF-B sites)
coupled to a chloramphenicol acetyltransferase (CAT) reporter. Cells
were subsequently stimulated with 1) PMA for 24 h, inducing CAT
activity by 2.6-fold, 2) fibrinogen/Mn2+ for 2 h,
inducing CAT activity by 3.2-fold, or 3) costimulation with fibrinogen
and PMA, inducing 5.7-fold the CAT activity induced by PMA alone. We
conclude that contact with fibrinogen-derived proteins may contribute
to mononuclear phagocyte activation by signaling through CD11b/CD18,
resulting in selective activation of transcriptional regulatory
factors, including NF-B.
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