Isolation of anti-endothelin receptor monoclonal antibodies for use in receptor characterization

Motohiro Kondoh; Hitoshi Miyazaki; Hirotoshi Watanabe; Takeshi Shibata; Masashi Yanagisawa; Tomoh Masaki; Kazuo Murakami

doi:10.1016/0006-291X(90)90701-N

Isolation of anti-endothelin receptor monoclonal antibodies for use in receptor characterization

Motohiro Kondoh, Hitoshi Miyazaki, Hirotoshi Watanabe, Takeshi Shibata, Masashi Yanagisawa, Tomoh Masaki, Kazuo Murakami

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9 Scopus citations

Abstract

Monoclonal antibodies reactive with endothelin (ET) receptors have been prepared by immunization of mice with rat lung membranes. Of four clones isolated, three clones preferentially recognized 32,000-dalton ET receptor and the other has a higher affinity for the 45,000-dalton receptor. The binding of ¹²⁵I-ET-1 to detergent-solubilized ET receptors which were adsorbed to the antibodies was displaced by increasing concentrations of unlabeled ET isopeptides. These results demonstrate that the four clones specific for the receptor have the potential to be a useful tool in the characterization of ET receptors.

Original language	English (US)
Pages (from-to)	503-510
Number of pages	8
Journal	Biochemical and Biophysical Research Communications
Volume	172
Issue number	2
DOIs	https://doi.org/10.1016/0006-291X(90)90701-N
State	Published - Oct 30 1990

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/0006-291X(90)90701-N

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title = "Isolation of anti-endothelin receptor monoclonal antibodies for use in receptor characterization",

abstract = "Monoclonal antibodies reactive with endothelin (ET) receptors have been prepared by immunization of mice with rat lung membranes. Of four clones isolated, three clones preferentially recognized 32,000-dalton ET receptor and the other has a higher affinity for the 45,000-dalton receptor. The binding of 125I-ET-1 to detergent-solubilized ET receptors which were adsorbed to the antibodies was displaced by increasing concentrations of unlabeled ET isopeptides. These results demonstrate that the four clones specific for the receptor have the potential to be a useful tool in the characterization of ET receptors.",

author = "Motohiro Kondoh and Hitoshi Miyazaki and Hirotoshi Watanabe and Takeshi Shibata and Masashi Yanagisawa and Tomoh Masaki and Kazuo Murakami",

note = "Funding Information: We would like to thank Dr. Yasuo Uchiyama for helpful comments in preparing monoclonal antibodies and Ms. Norma Foster for her help in preparing the manuscript. This work was supported by a Grant-in-Aid from the Ministry of Education, Science and Culture of Japan, and a grant from Chichibu Cement Co.",

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doi = "10.1016/0006-291X(90)90701-N",

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T1 - Isolation of anti-endothelin receptor monoclonal antibodies for use in receptor characterization

AU - Kondoh, Motohiro

AU - Miyazaki, Hitoshi

AU - Watanabe, Hirotoshi

AU - Shibata, Takeshi

AU - Yanagisawa, Masashi

AU - Masaki, Tomoh

AU - Murakami, Kazuo

N1 - Funding Information: We would like to thank Dr. Yasuo Uchiyama for helpful comments in preparing monoclonal antibodies and Ms. Norma Foster for her help in preparing the manuscript. This work was supported by a Grant-in-Aid from the Ministry of Education, Science and Culture of Japan, and a grant from Chichibu Cement Co.

PY - 1990/10/30

Y1 - 1990/10/30

N2 - Monoclonal antibodies reactive with endothelin (ET) receptors have been prepared by immunization of mice with rat lung membranes. Of four clones isolated, three clones preferentially recognized 32,000-dalton ET receptor and the other has a higher affinity for the 45,000-dalton receptor. The binding of 125I-ET-1 to detergent-solubilized ET receptors which were adsorbed to the antibodies was displaced by increasing concentrations of unlabeled ET isopeptides. These results demonstrate that the four clones specific for the receptor have the potential to be a useful tool in the characterization of ET receptors.

AB - Monoclonal antibodies reactive with endothelin (ET) receptors have been prepared by immunization of mice with rat lung membranes. Of four clones isolated, three clones preferentially recognized 32,000-dalton ET receptor and the other has a higher affinity for the 45,000-dalton receptor. The binding of 125I-ET-1 to detergent-solubilized ET receptors which were adsorbed to the antibodies was displaced by increasing concentrations of unlabeled ET isopeptides. These results demonstrate that the four clones specific for the receptor have the potential to be a useful tool in the characterization of ET receptors.

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Isolation of anti-endothelin receptor monoclonal antibodies for use in receptor characterization

Abstract

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