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Endothelin‐induced intracellular Ca 2+ mobilization through its specific receptors in murine peritoneal macrophages
Author(s) -
Kishino Junji,
Hanasaki Kohji,
Kato Toshiyuki,
Arita Hitoshi
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80214-n
Subject(s) - intracellular , receptor , cytosol , chemistry , gene isoform , binding site , microbiology and biotechnology , endothelin receptor , endothelin 1 , biophysics , biochemistry , biology , enzyme , gene
We studied the presence of specific binding sites for endothelin (ET) and the effect of ET on cytosolic free Ca 2+ concentration ([Ca 2+ ] i ) in murine thiogylcolate‐activated peritoneal macrophages. Scatchard analysis for binding experiments using [ 125 I]ET‐1 or [ 125 I]ET‐3 revealed the existence of a single class of binding sites. The binding parameters ( K ??? and B ???) for [ 125 I]ET‐1 were almost identical to those for [ 125 I]ET‐3. In addition, unlabeled 3 ET isopeptides (ET‐1, ET‐2 and ET‐3) inhibited the specific binding of both ET‐1 and ET‐3 with similar inhibitory potencies. All 3 ET isopeptides caused an increase in [Ca 2+ ] i in the same dose‐dependent manner (0.01–100nM). These results demonstrate the existence of an ET receptor with the same affinity for all isoforms that mediates the ET‐induced intracellular Ca 2+ mobilization in murine peritoneal macrophages.