We found a match
Your institution may have rights to this item. Sign in to continue.
- Title
Myosin light chain kinase and Rho-kinase participate in P2Y receptor-mediated acceleration of permeability through the endothelial cell layer.
- Authors
Naoko Tanaka; Namie Nejime; Yoko Kubota; Satomi Kagota; Keiko Yudo; Kazuki Nakamura; Masaru Kunitomo; Koichi Takahashi; Michio Hashimoto; Kazumasa Shinozuka
- Abstract
We have shown that P2Y receptor stimulation accelerates macromolecular permeation through the endothelial cell layer. To elucidate the mechanism of this acceleration, we examined the effects of ML-9, a myosin light chain kinase inhibitor, and Y-27632, a Rho-kinase inhibitor, on fluorescein isothiocyanate dextran (FD-4) permeation across the human umbilical vein endothelial cell monolayer. FD-4 permeation was analysed by high-performance liquid chromatography fluorescence detection. A P2Y receptor agonist, 2meS-ATP, enhanced the permeability of FD-4, which was inhibited by pyridoxalphosphate-6-azophenyl-2',4'-disulfonic acid (PPADS), a P2Y-receptor antagonist. The 2meS-ATP-induced increase in the permeability of FD-4 was significantly inhibited by ML-9. Also, Y-27632 prevented the 2meS-ATP-induced increase in the permeability of FD-4. Neither ML-9 nor Y-27632 influenced the spontaneous permeation of FD-4. These results suggest that phosphorylation of the myosin light chain may play an important role in the purinergic regulation of macromolecular permeation through the vascular endothelium.
- Publication
Journal of Pharmacy & Pharmacology, 2005, Vol 57, Issue 3, p335
- ISSN
0022-3573
- Publication type
Article