Endothelin-receptor interactions. Role of a putative sulfhydryl on the endothelin receptor

Michael J. Spinella, Rebecca Kottke, Harold I. Magazine, Matthew S. Healy, John A. Catena, Philip Wilken, Thomas T. Andersen

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish (US)
Pages (from-to)82-88
Number of pages7
JournalFEBS Letters
Issue number1-2
StatePublished - Aug 9 1993
Externally publishedYes


  • Antagonist
  • Eendothelin receptor
  • Endothelin
  • Mechanism

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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