Artigo Revisado por pares

Endothelin and structurally related analogs distinguish between endothelin receptor subtypes

1992; Elsevier BV; Volume: 183; Issue: 2 Linguagem: Inglês

10.1016/0006-291x(92)90519-q

ISSN

1090-2104

Autores

Robert L. Panek, Terry C. Major, Gary P. Hingorani, Annette M. Doherty, David G. Taylor, Stephen T. Rapundalo,

Tópico(s)

Electron Spin Resonance Studies

Resumo

The endothelin (ET) analog ET-1[1,3,11,15-Ala] was compared with ET-1, ET-2, ET-3 and sarafotoxins (SRTX) S6b and S6c for receptor binding and function. All the peptides exhibited high affinity binding and contracted rabbit pulmonary artery with near equal potency. In rat aorta both ET-3 and ET-1 [1,3,11,15-Ala] bound with much lower affinity than ET-1 while ET-3 displayed weak contractile potency and ET-1[1,3,11,15-Ala] and SRTX-c were inactive. In rat left atria, ET-1[1,3,11,15-Ala] and SRTX-c were weak inhibitors of binding and were also functionally inactive, whereas ET-1, ET-2, ET-3, and SRTX-b were equipotent in producing contractile responses. The data support the idea of there being a predominance of ETA receptors in rat aorta and ETB receptors in rabbit pulmonary artery. In rat left atria, the ET receptor could not be readily classified into ETA or ETB and suggests the existence of a new receptor subtype.

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