TY - JOUR
T1 - Two distinct types of endothelin receptors are present on chick cardiac membranes
AU - Watanabe, Hirotoshi
AU - Miyazaki, Hitoshi
AU - Kondoh, Motohiro
AU - Masuda, Yasushi
AU - Kimura, Sadao
AU - Yanagisawa, Masashi
AU - Masaki, Tomoh
AU - Murakami, Kazuo
N1 - Funding Information:
ACKNOWLEDGMENTS We would like to thank Dr. Naoto Ueno and Miss Miranda Mirfakhraifor for helpful comments and discussions to prepare the manuscript, and the Peptide Institute, Inc. for kind gifts of ET-l, -2, and - 3. This work was supported by a grant from Chichibu Cement Co.
PY - 1989/6/30
Y1 - 1989/6/30
N2 - Competitive displacement experiments of 125I-endothelin (ET)-1, -2, or -3 binding to chick cardiac membranes were performed with unlabeled ET-1, -2, -3, and sarafotoxin S6b (STX) as competitors. 125I-ET-1 and -2 binding was competitively inhibited by increasing concentrations of these unlabeled peptides in the same order; i.e. ET-2 ≥ ET-1 > ET-3 > STX. In contrast, the order of potency in displacing 125I-ET-3 binding was ET-3 > ET-2 ≥ ET-1 > STX. Affinity labeling of the membranes by cross-linking with 125I-ET-1 and -2 via disuccinimidyl tartarate yielded one major specific band with an apparent Mr=53,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis followed by autoradiography. On the other hand, affinity labeling with 125I-ET-3 showed that two major and one minor bands of Mr=34,000, 46,000, and 53,000, respectively, were specifically labeled. These results indicate the presence of two distinct types of ET receptors, one of which has higher affinity for ET-1 and -2 than ET-3 and the other is conversely ET-3-preferring.
AB - Competitive displacement experiments of 125I-endothelin (ET)-1, -2, or -3 binding to chick cardiac membranes were performed with unlabeled ET-1, -2, -3, and sarafotoxin S6b (STX) as competitors. 125I-ET-1 and -2 binding was competitively inhibited by increasing concentrations of these unlabeled peptides in the same order; i.e. ET-2 ≥ ET-1 > ET-3 > STX. In contrast, the order of potency in displacing 125I-ET-3 binding was ET-3 > ET-2 ≥ ET-1 > STX. Affinity labeling of the membranes by cross-linking with 125I-ET-1 and -2 via disuccinimidyl tartarate yielded one major specific band with an apparent Mr=53,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis followed by autoradiography. On the other hand, affinity labeling with 125I-ET-3 showed that two major and one minor bands of Mr=34,000, 46,000, and 53,000, respectively, were specifically labeled. These results indicate the presence of two distinct types of ET receptors, one of which has higher affinity for ET-1 and -2 than ET-3 and the other is conversely ET-3-preferring.
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U2 - 10.1016/0006-291X(89)91377-6
DO - 10.1016/0006-291X(89)91377-6
M3 - Article
C2 - 2545198
AN - SCOPUS:0024318815
SN - 0006-291X
VL - 161
SP - 1252
EP - 1259
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -