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Structural requirements for the interaction of sheep insulin-like factor 3 with relaxin receptors in rat atria.

Tan, Yean Yeow, Dawson, Nicola F., Kompa, Andrew R., Bond, Courtney P., Claasz, Antonia, Wade, John D., Tregear, Geoffrey W. and Summers, Roger J. (2002). Structural requirements for the interaction of sheep insulin-like factor 3 with relaxin receptors in rat atria. . European Journal of Pharmacology,457(2-3):153-160.

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Title Structural requirements for the interaction of sheep insulin-like factor 3 with relaxin receptors in rat atria.
Author Tan, Yean Yeow
Dawson, Nicola F.
Kompa, Andrew R.
Bond, Courtney P.
Claasz, Antonia
Wade, John D.
Tregear, Geoffrey W.
Summers, Roger J.
Journal Name European Journal of Pharmacology
Publication Date 2002
Volume Number 457
Issue Number 2-3
ISSN 0014-2999   (check CDU catalogue open catalogue search in new window)
Start Page 153
End Page 160
Total Pages 8
Place of Publication Netherlands
Publisher Elsevier BV
Language English
Field of Research 1115 - Pharmacology and Pharmaceutical Sciences
Abstract Relaxin is a peptide with various reproductive and nonreproductive functions. The site for the peptide–receptor interaction contains two arginines (Arg) and an isoleucine (Ile) or valine (Val) residue in the B-chain with a configuration of -Arg-X-X-X-Arg-X-X-Ile/Val-X-. The sheep insulin-like peptide 3 (INSL3), a structural homologue of relaxin, also contains the n, n+4 arginines in the B-chain but they are displaced towards the carboxyl terminus by four residues (-X-X-X-X-Arg-X-X-Val-Arg-). Human INSL3 increases the activity of human relaxin in mouse bioassays. Here, we investigated whether sheep synthetic INSL3 affects the relaxin activity in rat atria. INSL3 lacked relaxin-like agonist activity but blocked the activity of relaxin and competed for relaxin binding sites at high concentrations. We also synthesized analogues of INSL3, with amino acid substitutions in the arginine-binding region. Analogues A, D and E, which have the arginines in positions identical to relaxin, showed weak relaxin-like agonist activity. These results suggest that other sites in the relaxin molecule are involved in high-affinity peptide–receptor interaction for the production of the relaxin biological responses.
Keywords Relaxin
(INSL3) Insulin-like peptide 3
Atria
Rat
Chronotropic
Inotropic
Receptor autoradiagraphy
DOI http://dx.doi.org/10.1016/S0014-2999(02)02662-6   (check subscription with CDU E-Gateway service for CDU Staff and Students  check subscription with CDU E-Gateway in new window)
Description for Link Link to publisher's version
URL http://www.sciencedirect.com/science/article/pii/S0014299902026626
 
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Created: Mon, 08 Dec 2014, 14:45:27 CST by Yean Tan