Key result
Endothelin-1 at low concentrations persistently activates a Ca2+-permeable non-selective cation channel coupled with ETA receptors, mediating sustained vasoconstriction without IP3 formation.
Answers are grounded in this paper and cite their sources.
This study identifies a novel mechanism for ET-1 induced sustained vasoconstriction via a Ca2+-permeable non-selective cation channel independent of IP3 formation.
Endothelin-1 (ET-1) induces persistent vasoconstriction via a sustained increase in intracellular free Ca2+ concentrations ([Ca2+]i). The mechanisms of the elevation of [Ca2+]i operating at physiologically low concentrations of ET-1 are controversial. Here we report that both native ETA receptors in vascular smooth-muscle cells and recombinant ET(A) receptors expressed in mouse fibroblasts (Ltk cells) are functionally coupled with a non-selective cation channel, which is permeable to Ca2+ and is blocked by mefenamic acid. The channel is persistently activated by a low concentration of ET-1 (10(-10) M) without stimulation of inositol triphosphate (IP3) formation and mediates sustained vasoconstriction.
No takes yet. Share an insight, caveat, or question.
Enoki et al. (1995) studied this question. Endothelin-1 (ET-1) was evaluated on Activation of non-selective cation channel and sustained vasoconstriction. Endothelin-1 at low concentrations persistently activates a Ca2+-permeable non-selective cation channel coupled with ETA receptors, mediating sustained vasoconstriction without IP3 formation.
Synapse has enriched 10 related papers. Consider them for comparative context: