Pressor-type vasopressin receptors in the adrenal cortex

Properties of binding, effects on phosphoinositide metabolism and aldosterone secretion

T. Balla, P. Enyedi, A. Spät, F. A. Antoni

Research output: Contribution to journalArticle

53 Citations (Scopus)

Abstract

Specific, high affinity sites that bound tritium-labeled arginine-vasopressin (3H-AVP) were detected in a crude membrane fraction of rat adrenal capsules (chiefly zona glomerulosa). Binding displacement experiments with peptide analogs of AVP suggested that the binding site is a pressor (V1) type receptor for AVP. When added to dispersed rat adrenal glomerulosa cells, vasopressin (10-8-10-6M) stimulated the incorportion of 32P-phosphate into phosphatidylinositol, and the effect was blocked by the AVP receptor antagonist peptide d(CH2)5 Tyr(Me)AVP. Vasopressin also increased the breakdown of phosphatidylinositol-4,5-bisphosphate within 1 min after its addition to the incubation medium. Superfused zona glomerulosa cells responded to AVP(10-8-10-6 M) by increasing their aldosterone production. The response could be blocked by the antagonist peptide. These data show that functionally active V1 receptors are present in rat glomerulosa cells, and suggest that vasopressin may regulate the function of the adrenal glomerulosa.

Original languageEnglish
Pages (from-to)421-423
Number of pages3
JournalEndocrinology
Volume117
Issue number1
Publication statusPublished - 1985

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Zona Glomerulosa
Vasopressin Receptors
Adrenal Cortex
Phosphatidylinositols
Aldosterone
Vasopressins
Phosphatidylinositol Phosphates
Peptides
Peptide Receptors
Tritium
Arginine Vasopressin
Capsules
Binding Sites
Membranes

ASJC Scopus subject areas

  • Endocrinology
  • Endocrinology, Diabetes and Metabolism

Cite this

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abstract = "Specific, high affinity sites that bound tritium-labeled arginine-vasopressin (3H-AVP) were detected in a crude membrane fraction of rat adrenal capsules (chiefly zona glomerulosa). Binding displacement experiments with peptide analogs of AVP suggested that the binding site is a pressor (V1) type receptor for AVP. When added to dispersed rat adrenal glomerulosa cells, vasopressin (10-8-10-6M) stimulated the incorportion of 32P-phosphate into phosphatidylinositol, and the effect was blocked by the AVP receptor antagonist peptide d(CH2)5 Tyr(Me)AVP. Vasopressin also increased the breakdown of phosphatidylinositol-4,5-bisphosphate within 1 min after its addition to the incubation medium. Superfused zona glomerulosa cells responded to AVP(10-8-10-6 M) by increasing their aldosterone production. The response could be blocked by the antagonist peptide. These data show that functionally active V1 receptors are present in rat glomerulosa cells, and suggest that vasopressin may regulate the function of the adrenal glomerulosa.",
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T2 - Properties of binding, effects on phosphoinositide metabolism and aldosterone secretion

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AU - Enyedi, P.

AU - Spät, A.

AU - Antoni, F. A.

PY - 1985

Y1 - 1985

N2 - Specific, high affinity sites that bound tritium-labeled arginine-vasopressin (3H-AVP) were detected in a crude membrane fraction of rat adrenal capsules (chiefly zona glomerulosa). Binding displacement experiments with peptide analogs of AVP suggested that the binding site is a pressor (V1) type receptor for AVP. When added to dispersed rat adrenal glomerulosa cells, vasopressin (10-8-10-6M) stimulated the incorportion of 32P-phosphate into phosphatidylinositol, and the effect was blocked by the AVP receptor antagonist peptide d(CH2)5 Tyr(Me)AVP. Vasopressin also increased the breakdown of phosphatidylinositol-4,5-bisphosphate within 1 min after its addition to the incubation medium. Superfused zona glomerulosa cells responded to AVP(10-8-10-6 M) by increasing their aldosterone production. The response could be blocked by the antagonist peptide. These data show that functionally active V1 receptors are present in rat glomerulosa cells, and suggest that vasopressin may regulate the function of the adrenal glomerulosa.

AB - Specific, high affinity sites that bound tritium-labeled arginine-vasopressin (3H-AVP) were detected in a crude membrane fraction of rat adrenal capsules (chiefly zona glomerulosa). Binding displacement experiments with peptide analogs of AVP suggested that the binding site is a pressor (V1) type receptor for AVP. When added to dispersed rat adrenal glomerulosa cells, vasopressin (10-8-10-6M) stimulated the incorportion of 32P-phosphate into phosphatidylinositol, and the effect was blocked by the AVP receptor antagonist peptide d(CH2)5 Tyr(Me)AVP. Vasopressin also increased the breakdown of phosphatidylinositol-4,5-bisphosphate within 1 min after its addition to the incubation medium. Superfused zona glomerulosa cells responded to AVP(10-8-10-6 M) by increasing their aldosterone production. The response could be blocked by the antagonist peptide. These data show that functionally active V1 receptors are present in rat glomerulosa cells, and suggest that vasopressin may regulate the function of the adrenal glomerulosa.

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