| Autor: |
Chiou, W. J., Magnuson, S. R., Dixon, D., Sundy, S., Opgenorth, T. J., Wu-wong, J. R. |
| Zdroj: |
Endothelium: Journal of Endothelial Cell Research; 1997, Vol. 5 Issue: 3 p179-189, 11p |
| Abstrakt: |
The human type-B endothelin receptor (h-ETB) was cloned from human lung poly A+RNA and stably expressed in CHO cells. Endothelin (ET) receptor binding and stimulation of PI hydrolysis demonstrated that the cloned h-ETB receptor is functional and linked to intracellular signal transduction pathways in CHO cells. The molecular mass of the h-ETB receptor was determined to be 65 KDa, and Bmax and Kd were 0.36 pmol/mg and 80 pM, respectively. Competition studies employing receptor ligands revealed that the potencies of the test ligands (IRL1620, PD142893, and Ro46-2005) were dependent on the length of the incubation time, whereas the natural agonists (ET-1 and ET-3) were not. When competing with ET-1 in the h-ETB receptor binding, the IC50 increased from 1.2 nM to 8.2 nM for IRL1620,0.068 μM to 1.9 μM for PD142893, and 0.76 μM to 12.7 μM for Ro46-2005, as the incubation time increased from 1 hr to 24 hr. These time-induced changes are likely due to differences in the dissociation characteristics between the artificial ligands and the natural ligands. |
| Databáze: |
Supplemental Index |
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