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Am J Physiol Regul Integr Comp Physiol 279: R1043-R1049, 2000;
0363-6119/00 $5.00
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Vol. 279, Issue 3, R1043-R1049, September 2000

Macrophage migration inhibitory factor antagonizes hydrocortisone-induced increases in cytosolic Ikappa Balpha

Jane M. Daun and Joseph G. Cannon

Intercollege Physiology Program, Noll Physiological Research Center, Pennsylvania State University, University Park, Pennsylvania 16802

Macrophage migration inhibitory factor (MIF) is an inflammatory cytokine secreted by several cell types, including mononuclear and pituitary cells. It has also been shown to counteract cortisol-induced inhibition of inflammatory cytokine secretion. The purpose of this study was to determine whether MIF antagonized the effect of hydrocortisone on the NF-kappa B/Ikappa B signal transduction pathway in lipopolysaccharide (LPS)-stimulated human peripheral blood mononuclear cells. Physiological doses of hydrocortisone (50-200 ng/ml) diminished both the LPS-stimulated decrease in cytosolic Ikappa Balpha levels and the subsequent increase in nuclear NF-kappa B DNA binding. In the presence of both LPS and hydrocortisone, 1 ng/ml of MIF antagonized the effects of hydrocortisone, resulting in decreased cytosolic Ikappa Balpha levels (P < 0.05) and increased nuclear NF-kappa B DNA binding (P < 0.05). In the absence of hydrocortisone, MIF had no effect on LPS-induced decreases in Ikappa Balpha . In the absence of LPS, MIF inhibited hydrocortisone-induced increases in Ikappa Balpha (P = 0.03). Thus the mechanism by which MIF antagonizes the effect of hydrocortisone on the NF-kB/Ikappa B signal transduction pathway is through inhibiting the ability of hydrocortisone to increase cytosolic Ikappa Balpha .

monocytes; glucocorticoids; NF-kappa B


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