Abstract:
:The family of endothelins, endothelin-1 (ET-1), ET-2 and ET-3, act on two subtypes of receptors called ETA and ETB receptors. BQ123 is an ETA-selective competitive antagonist. In this study, however, BQ123 inhibited ET-1-induced transients of cytosolic Ca2+ concentrations ([Ca2+]i) in an apparently noncompetitive manner in mouse L cell stably expressing cloned human ETA receptor. BQ123 (3-30 nM) did not change the EC50 of ET-1 (6.6 nM), but reduced the maximum responses down to 15.0%. In an non-equilibrium binding assay which mimicks the conditions of [Ca2+]i transient assay (cells were incubated with [125I]ET-1 only for 30 s), BQ123 (30 nM) constantly decreased the specific [125I]ET-1 binding to approximately 13% of that without the antagonist. Thus, the apparent noncompetitive antagonism by BQ123 of ETA receptor-mediated [Ca2+]i transient is due to the assay condition where the interactions of the agonist, antagonist and receptor remained non-equilibrium state.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Sakamoto A,Yanagisawa M,Tsujimoto G,Nakao K,Toyo-oka T,Masaki Tdoi
10.1006/bbrc.1994.1504subject
Has Abstractpub_date
1994-04-29 00:00:00pages
679-86issue
2eissn
0006-291Xissn
1090-2104pii
S0006291X8471504Xjournal_volume
200pub_type
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