Endothelin receptors in rat renal papilla with a high affinity for endothelin-3.
A high density of binding sites for endothelin has been described in rat renal papilla but the nature and significance of papillary endothelin receptors have not yet been evaluated. In the current study, the effect of endothelin peptides on phosphatidylinositol turnover in papillary tubules has been investigated. Endothelin-1, endothelin-3 and the endothelin-related peptide sarafatoxin S6b all stimulated the accumulation of inositol phosphates in [3H]inositol-labelled papillary tubule preparations. However, at these papillary receptors endothelin-3 was more potent than endothelin-1. In other tissues, endothelin-1 is more potent than endothelin-3 at endothelin receptors coupled to phosphatidylinositol turnover. The EC50 value for endothelin-3 expressed as the negative logarithm was 9.3 +/- 0.13 compared with 8.42 +/- 0.11 for endothelin-1 (mean +/- S.E.M., n = 5 in each case, P less than 0.01). The affinity of sarafatoxin S6b was similar to that for endothelin-3 (9.2 +/- 0.15, n = 3). These findings raise the possibility of a direct tubular function of endothelin and suggest that endothelin-3 rather than endothelin-1 may be the natural agonist for these papillary receptors.
Woodcock
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Baker Medical Research Institute, Prahran, Victoria, Australia.
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D000818:Animals; D001665:Binding Sites; D016232:Endothelins / Q000378:metabolism*; D007295:Inositol Phosphates / Q000378:metabolism; D007679:Kidney Medulla / Q000378:metabolism* / Q000648:ultrastructure; D007684:Kidney Tubules / Q000378:metabolism* / Q000648:ultrastructure; D008297:Male; D009399:Nephrons / Q000378:metabolism / Q000648:ultrastructure; D010455:Peptides / Q000494:pharmacology; D051381:Rats; D011919:Rats, Inbred Strains; D011956:Receptors, Cell Surface / Q000378:metabolism* / Q000502:physiology; D017466:Receptors, Endothelin
D016232:Endothelins; D007295:Inositol Phosphates; D010455:Peptides; D011956:Receptors, Cell Surface; D017466:Receptors, Endothelin