[3H]desGly-NH29-d(CH2)5[D-Ileu2,Ileu4]AVP: An AVP V2 receptor antagonist radioligand

D. Trinder; J. M. Stephenson; X. Gao; P. A. Phillips; J. Risvanis; C. I. Johnston

doi:10.1016/0196-9781(91)90194-T

[³H]desGly-NH₂⁹-d(CH₂)₅[D-Ileu²,Ileu⁴]AVP: An AVP V₂ receptor antagonist radioligand

D. Trinder, J. M. Stephenson, X. Gao, P. A. Phillips, J. Risvanis, C. I. Johnston

Research output: Contribution to journal › Article › peer-review

21 Citations (Scopus)

Abstract

Binding characteristics of the selective V₂ antagonist radioligand [³H]desGly-NH₂⁹-d(CH₂)₅[D-Ileu²,Ileu⁴]AVP to rat kidney were determined. Binding was specific, saturable and reversible. The peptide bound to a single class of high-affinity binding sites with B_max 69.4±6.8 fmol/mg protein and K_D 2.8±0.3 nM. AVP and other related peptides displaced [³H]desGly-NH₂⁹-d(CH₂)₅[D-Ileu²,Ileu⁴]AVP binding. The order of potency of inhibition was desamino-D-AVP > AVP > d(CH₂)₅[D-Ileu²,Ileu⁴]AVP > oxytocin > d(CH₂)₃[Tyr(Me)²]AVP > d(CH₂)₅[sarcosine⁷]AVP, which is typical of a selective V₂ radioligand. Autoradiographic localization of [³H]desGly-NH₂⁹-d(CH₂)₅[D-Ileu²,Ileu⁴]AVP binding sites in kidney showed dense binding in the inner and outer medulla with less binding in the cortex, which is consistent with known renal V₂ receptor distribution.

Original language	English
Pages (from-to)	1195-1200
Number of pages	6
Journal	Peptides
Volume	12
Issue number	6
DOIs	https://doi.org/10.1016/0196-9781(91)90194-T
Publication status	Published - 1991
Externally published	Yes

Keywords

AVP antagonist
Kidney
V receptor
Vasopressin

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title = "[3H]desGly-NH29-d(CH2)5[D-Ileu2,Ileu4]AVP: An AVP V2 receptor antagonist radioligand",

abstract = "Binding characteristics of the selective V2 antagonist radioligand [3H]desGly-NH29-d(CH2)5[D-Ileu2,Ileu4]AVP to rat kidney were determined. Binding was specific, saturable and reversible. The peptide bound to a single class of high-affinity binding sites with Bmax 69.4±6.8 fmol/mg protein and KD 2.8±0.3 nM. AVP and other related peptides displaced [3H]desGly-NH29-d(CH2)5[D-Ileu2,Ileu4]AVP binding. The order of potency of inhibition was desamino-D-AVP > AVP > d(CH2)5[D-Ileu2,Ileu4]AVP > oxytocin > d(CH2)3[Tyr(Me)2]AVP > d(CH2)5[sarcosine7]AVP, which is typical of a selective V2 radioligand. Autoradiographic localization of [3H]desGly-NH29-d(CH2)5[D-Ileu2,Ileu4]AVP binding sites in kidney showed dense binding in the inner and outer medulla with less binding in the cortex, which is consistent with known renal V2 receptor distribution.",

keywords = "AVP antagonist, Kidney, V receptor, Vasopressin",

author = "D. Trinder and Stephenson, {J. M.} and X. Gao and Phillips, {P. A.} and J. Risvanis and Johnston, {C. I.}",

year = "1991",

doi = "10.1016/0196-9781(91)90194-T",

language = "English",

volume = "12",

pages = "1195--1200",

journal = "Peptides",

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T1 - [3H]desGly-NH29-d(CH2)5[D-Ileu2,Ileu4]AVP

T2 - An AVP V2 receptor antagonist radioligand

AU - Trinder, D.

AU - Stephenson, J. M.

AU - Gao, X.

AU - Phillips, P. A.

AU - Risvanis, J.

AU - Johnston, C. I.

PY - 1991

Y1 - 1991

N2 - Binding characteristics of the selective V2 antagonist radioligand [3H]desGly-NH29-d(CH2)5[D-Ileu2,Ileu4]AVP to rat kidney were determined. Binding was specific, saturable and reversible. The peptide bound to a single class of high-affinity binding sites with Bmax 69.4±6.8 fmol/mg protein and KD 2.8±0.3 nM. AVP and other related peptides displaced [3H]desGly-NH29-d(CH2)5[D-Ileu2,Ileu4]AVP binding. The order of potency of inhibition was desamino-D-AVP > AVP > d(CH2)5[D-Ileu2,Ileu4]AVP > oxytocin > d(CH2)3[Tyr(Me)2]AVP > d(CH2)5[sarcosine7]AVP, which is typical of a selective V2 radioligand. Autoradiographic localization of [3H]desGly-NH29-d(CH2)5[D-Ileu2,Ileu4]AVP binding sites in kidney showed dense binding in the inner and outer medulla with less binding in the cortex, which is consistent with known renal V2 receptor distribution.

AB - Binding characteristics of the selective V2 antagonist radioligand [3H]desGly-NH29-d(CH2)5[D-Ileu2,Ileu4]AVP to rat kidney were determined. Binding was specific, saturable and reversible. The peptide bound to a single class of high-affinity binding sites with Bmax 69.4±6.8 fmol/mg protein and KD 2.8±0.3 nM. AVP and other related peptides displaced [3H]desGly-NH29-d(CH2)5[D-Ileu2,Ileu4]AVP binding. The order of potency of inhibition was desamino-D-AVP > AVP > d(CH2)5[D-Ileu2,Ileu4]AVP > oxytocin > d(CH2)3[Tyr(Me)2]AVP > d(CH2)5[sarcosine7]AVP, which is typical of a selective V2 radioligand. Autoradiographic localization of [3H]desGly-NH29-d(CH2)5[D-Ileu2,Ileu4]AVP binding sites in kidney showed dense binding in the inner and outer medulla with less binding in the cortex, which is consistent with known renal V2 receptor distribution.

KW - AVP antagonist

KW - Kidney

KW - V receptor

KW - Vasopressin

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DO - 10.1016/0196-9781(91)90194-T

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JO - Peptides

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ER -

[³H]desGly-NH₂⁹-d(CH₂)₅[D-Ileu²,Ileu⁴]AVP: An AVP V₂ receptor antagonist radioligand

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