Rat RAMP domains involved in adrenomedullin binding specificity |
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Authors: | Kuwasako Kenji Kitamura Kazuo Onitsuka Hisamitsu Uemura Tomohiko Nagoshi Yasuko Kato Johji Eto Tanenao |
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Institution: | First Department of Internal Medicine, Miyazaki Medical College, 5200 Kihara, Kiyotake, Miyazaki, Japan. kuwasako@fc.miyazaki-med-ac.jp |
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Abstract: | When coexpressed with receptor activity-modifying protein (RAMP)2 or -3, calcitonin receptor-like receptor (CRLR) functions as an adrenomedullin (AM) receptor (CRLR/RAMP2 or -3). Coexpression of rat (r)CRLR with rRAMP deletion mutants in HEK293T cells revealed that deletion of residues 93-99 from rRAMP2 or residues 58-64 from rRAMP3 significantly inhibits high-affinity 125I]AM binding and AM-evoked cAMP production, despite full cell surface expression of the receptor heterodimer. Apparently, these two seven-residue segments are key determinants of high-affinity agonist binding to rAM receptors and of receptor functionality. Consequently, their deletion yields peptides that are able to serve as negative regulators of AM receptor function. |
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