Endothelin‐receptor interactions

FEBS Letters

Wilken, Philip¹  Magazine, Harold I.¹  Catena, John A.¹  Healy, Matthew S.¹  Andersen, Thomas T.¹  Spinella, Michael J.¹  Kottke, Rebecca¹ 

[1] Department of Biochemistry and Molecular Biology, Albany Medical College, Albany, NY 12208, USA

关键词: Endothelin;    Eendothelin receptor;    Antagonist;    Mechanism;   

DOI  :  10.1016/0014-5793(93)80970-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The mechanism of action of endothelin-receptor interactions was studied, using radioligand binding assays and SDS-PAGE, to investigate the possibility of disulfide interchange. Electrophoretic analysis suggested involvement of disulfide bond(s) in the receptor-ligand complex. Treatment of Et receptors with sulfhydryl-specific alkylating reagents (NEM or others) resulted in decreased ability to bind [¹²⁵I]Et-1. [Dpr¹-Asp¹⁵]Et-1, an antagonist homologous to Et but with an amide link replacing one of the disulfides, bound to Et receptors reversibly, but binding of Et-1 was less reversible. Preincubation of receptors with Et-L, but not with [Dpr¹-Asp¹⁵]Et-L, protected receptors from alkylation with [¹⁴C]NEM. The data suggest that the Et receptor has a sulfhydryl group at or near the Et binding site. A model is proposed in which the role of the putative sulfhydryl group is discussed.

【 授权许可】

Unknown