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Vol. 55, Issue 4, 726-734, April 1999
Divisions of Clinical Pharmacology and Cardiology,
Departments of Medicine and Pharmacology, Vanderbilt University,
Nashville, Tennessee
The endogenous nucleoside adenosine is thought to play a role in the
pathophysiology of asthma by stimulating mast cells. We previously
showed that the human mast cell line HMC-1 expresses A2A
and A2B receptors, and that both receptors activate
adenylate cyclase via Gs-protein but that only
A2B receptors are also coupled to phospholipase C via
Gq proteins. Stimulation of A2B but not A2A receptors induced production of interleukin-8 (IL-8)
from HMC-1 cells. The mechanism by which adenosine promotes IL-8
synthesis has not been defined. In this study, we tested the hypothesis that mitogen-activated protein kinase (MAPK) signaling pathways are
involved in this process. Stimulation of HMC-1 with the stable adenosine analog NECA (5'-N-ethylcarboxamidoadenosine) activated p21ras and both p42 and p44 isoforms of extracellular
signal-regulated kinase (ERK). NECA (10 µM) induced a 1.9 ± 0.06-fold increase in ERK activity, whereas 10 µM of the selective
A2A agonist CGS 21680 (4-((N-ethyl-5'-carbamoyladenos-2-yl)-aminoethyl)-phenylpropionic acid) had no effect. NECA, in parallel with the activation of ERK, also stimulated the p46 isoform of c-Jun N-terminal kinase (MEK)
and p38 MAPK. Furthermore, the selective MAPK/ERK kinase 1 inhibitor PD
98059 (2'-amino-3'-methoxyflavone), and p38 MAPK inhibitors SB 202190 (4-(4-fluorophenyl)-2-(4-hydroxyphenyl)-5-(4-pyridyl)1H-imidazole) and SB 203580 (4-(4-fluorophenyl)-2-(4-methylsulfinylphenyl)-5-(4-pyridyl)1H-imidazole) blocked A2B receptor-mediated production of IL-8. These
results indicate that extracellular adenosine can regulate ERK, c-Jun N-terminal kinase, and p38 MAPK signaling cascades and that activation of ERK and p38 MAPK pathways are essential steps in adenosine A2B receptor-dependent stimulation of IL-8 production in
HMC-1.
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