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1 Pulmonary and Critical Care Medicine Section, University of Nebraska Medical Center, Omaha 68198-5125; 3 Veterans Affairs Medical Center, Omaha, Nebraska 68105; 2 University of Milan, Milan 20122, Italy; 4 First Department of Pathology, Nippon Medical School, Tokyo 113-0022; and 5 Third Department of Internal Medicine, University of Tokushima, Tokushima 770-8503, Japan
Fibroblasts are the major source of extracellular connective
tissue matrix, and the recruitment, accumulation, and stimulation of
these cells are thought to play important roles in both normal healing
and the development of fibrosis. Prostaglandin E2
(PGE2) can inhibit this process by blocking fibroblast
proliferation and collagen production. The aim of this study was to
investigate the inhibitory effect of PGE2 on human plasma
fibronectin (hFN)- and bovine bronchial epithelial cell-conditioned
medium (BBEC-CM)-induced chemotaxis of human fetal lung fibroblasts
(HFL1). Using the Boyden blind well chamber technique, PGE2
(10
7 M) inhibited chemotaxis to hFN 40.8 ± 5.3%
(P < 0.05) and to BBEC-CM 49.7 ± 11.7%
(P < 0.05). Checkerboard analysis demonstrated inhibition of both chemotaxis and chemokinesis. The effect of PGE2 was concentration dependent, and the inhibitory effect
diminished with time. Other agents that increased fibroblast cAMP
levels, including isoproterenol (105 M), dibutyryl cAMP
(105 M), and forskolin (3 × 105 M)
had similar effects and inhibited chemotaxis 54.1, 95.3, and 87.0%,
respectively. The inhibitory effect of PGE2 on HFL1 cell chemotaxis was inhibited by the cAMP-dependent protein kinase (PKA)
inhibitor KT-5720, which suggests a cAMP-dependent effect mediated by
PKA. In summary, PGE2 appears to inhibit fibroblast chemotaxis, perhaps by modulating the rate of fibroblast migration. Such an effect may contribute to regulation of the wound healing response after injury.
eicosanoids; adenosine 3',5'-cyclic monophosphate; fibronectin; fibrosis; repair
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