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- Title
Staurosporine aglycone bilaterally regulates ERK1/2 phosphorylation in rat pulmonary arterial smooth muscle cells.
- Authors
Jianing Zhang; Xiaobo Tang; Changlian Lu; Lei Guo; Shuang Zhang; Xiaojie Chu; Daling Zhu
- Abstract
Staurosporine, a protein kinase C (PKC) inhibitor, has been reported to regulate the phosphorylation of ERK1/2 in several cell lines. It is still unknown, however, whether its derivative staurosporine aglycone (SA) has the same effect on ERK1/2 activation. In this study, we investigated the effect of SA on ERK1/2 activity in rat pulmonary arteries and pulmonary arterial smooth muscle cells (PASMCs). The pulmonary arteries and PASMCs were treated with SA at different time points and concentrations, and the activation of ERK1/2 was analyzed by Western blotting. The results showed that SA at nanomolar concentrations suppressed ERK1/2 phosphorylation through the PKC pathway alone, but SA at 30 µmol/L for 2 h enhanced the phosphorylation of ERK1/2. The activation of ERK1/2 was inhibited by the MAPK/ERK kinase inhibitor PD98059 or the protein kinase A (PKA) activator isoproterenol. Together, these results suggest that SA has a strong dual regulating effect on ERK1/2 through the PKC and (or) PKA pathways in rat PASMCs.
- Subjects
PROTEIN kinase C; PHOSPHORYLATION; SMOOTH muscle; CELL lines; LABORATORY rats
- Publication
Canadian Journal of Physiology & Pharmacology, 2008, Vol 86, Issue 7, p424
- ISSN
0008-4212
- Publication type
Article
- DOI
10.1139/Y08-061