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Pulmonary and Critical Care Division, Department of Medicine, Tupper Research Institute, and New England Medical Center, Tufts University School of Medicine, Boston, Massachusetts 02111
Our previous studies have shown that, through an
active transport process, serotonin (5-HT) rapidly elevates
O
2· formation, stimulates protein
phosphorylation, and enhances proliferation of bovine pulmonary artery
smooth muscle cells (SMCs). We presently show that 1 µM 5-HT also
rapidly elevates phosphorylation and activation of the
mitogen-activated protein (MAP) kinases extracellular signal-regulated
kinase (ERK) 1 and ERK2 of SMCs, and the enhanced phosphorylation is
blocked by the antioxidants Tiron,
N-acetyl-L-cysteine (NAC),
and Ginkgo biloba extract. Inhibition
of MAP kinase with PD-98059 failed to block enhanced
O2· formation by 5-HT. Chinese
hamster lung fibroblasts (CCL-39 cells), which demonstrate both 5-HT
transporter and receptor activity, showed a similar response to 5-HT
(i.e., enhanced mitogenesis, O2· formation, and ERK1 and ERK2 phosphorylation and activation). Unlike
SMCs, they also responded to 5-HT receptor agonists. We conclude that
downstream signaling of MAP kinase is a generalized cellular response
to 5-HT that occurs secondary to
O2· formation and may be initiated
by either the 5-HT transporter or receptor depending on the cell type.
signal transduction; mitogen-activated protein kinase; superoxide; smooth muscle cell; fibroblast
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