Slide-binding characterization and autoradiographic localization of delta opioid receptors in rat and mouse brains with the tetrapeptide antagonist [3H]TIPP

Lidia Bakota, Judit Szikra, Geza Toth, K. Gulya

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Slide-binding and autoradiographic studies were performed on cryostat sections from brains of adult Sprague-Dawley rats and BALB C mice to describe the binding characteristics of the tetrapeptide [3H]TIPP, an antagonist with high specificity and affinity for the delta opioid receptors. Steady-state binding of [3H]TIPP to cryostat sections of brain paste was reached in 120- 180 min of incubation. Specific [3H]TIPP binding resulted in maximal numbers of binding sites (B(max)) of 15.59 and 23.91 fmol/mg protein, and dissociation constants (K(d)) of 0.46 and 0.85 nM for rat and mouse brain paste sections, respectively. TIPP displayed the highest affinity for delta opioid receptors in inhibiting specific [3H]TIPP binding, with IC50 values of 0.82 nM and 0.14 nM in rat and mouse brain sections, respectively. While DPDPE was also effective in displacing the specific binding of [3H]TIPP (IC50 = 3.18 ± 0.53 nM and 0.63 ± 0.42 nM in rat and mouse brain paste sections, respectively), other subclass-selective or nonopioid ligands were much less effective, or ineffective. Autoradiographic localization of [3H]TIPP binding revealed the characteristic distribution of delta opioid receptors in both species. In consequence of its antagonistic nature, and of its unnatural amino acid residue, which makes this ligand more resistant to biodegradation, [3H]TIPP is a superior ligand for evaluation of the binding characteristics and autoradiogaphic distribution of the delta opioid receptors.

Original languageEnglish
Pages (from-to)1377-1385
Number of pages9
JournalLife Sciences
Volume63
Issue number15
DOIs
Publication statusPublished - Sep 4 1998

Fingerprint

delta Opioid Receptor
Rats
Brain
Ointments
Cryostats
Ligands
Inhibitory Concentration 50
Inbred BALB C Mouse
D-Penicillamine (2,5)-Enkephalin
tyrosyl-1,2,3,4-tetrahydro-3-isoquinolinecarbonyl-phenylalanyl-phenylalanine
Biodegradation
Sprague Dawley Rats
Binding Sites
Amino Acids

Keywords

  • Autoradiography
  • Delta opioid antagonist
  • Delta opioid receptor
  • Slide- binding

ASJC Scopus subject areas

  • Pharmacology

Cite this

Slide-binding characterization and autoradiographic localization of delta opioid receptors in rat and mouse brains with the tetrapeptide antagonist [3H]TIPP. / Bakota, Lidia; Szikra, Judit; Toth, Geza; Gulya, K.

In: Life Sciences, Vol. 63, No. 15, 04.09.1998, p. 1377-1385.

Research output: Contribution to journalArticle

@article{d52477903884488c88dbc7ae61239a2b,
title = "Slide-binding characterization and autoradiographic localization of delta opioid receptors in rat and mouse brains with the tetrapeptide antagonist [3H]TIPP",
abstract = "Slide-binding and autoradiographic studies were performed on cryostat sections from brains of adult Sprague-Dawley rats and BALB C mice to describe the binding characteristics of the tetrapeptide [3H]TIPP, an antagonist with high specificity and affinity for the delta opioid receptors. Steady-state binding of [3H]TIPP to cryostat sections of brain paste was reached in 120- 180 min of incubation. Specific [3H]TIPP binding resulted in maximal numbers of binding sites (B(max)) of 15.59 and 23.91 fmol/mg protein, and dissociation constants (K(d)) of 0.46 and 0.85 nM for rat and mouse brain paste sections, respectively. TIPP displayed the highest affinity for delta opioid receptors in inhibiting specific [3H]TIPP binding, with IC50 values of 0.82 nM and 0.14 nM in rat and mouse brain sections, respectively. While DPDPE was also effective in displacing the specific binding of [3H]TIPP (IC50 = 3.18 ± 0.53 nM and 0.63 ± 0.42 nM in rat and mouse brain paste sections, respectively), other subclass-selective or nonopioid ligands were much less effective, or ineffective. Autoradiographic localization of [3H]TIPP binding revealed the characteristic distribution of delta opioid receptors in both species. In consequence of its antagonistic nature, and of its unnatural amino acid residue, which makes this ligand more resistant to biodegradation, [3H]TIPP is a superior ligand for evaluation of the binding characteristics and autoradiogaphic distribution of the delta opioid receptors.",
keywords = "Autoradiography, Delta opioid antagonist, Delta opioid receptor, Slide- binding",
author = "Lidia Bakota and Judit Szikra and Geza Toth and K. Gulya",
year = "1998",
month = "9",
day = "4",
doi = "10.1016/S0024-3205(98)00402-0",
language = "English",
volume = "63",
pages = "1377--1385",
journal = "Life Sciences",
issn = "0024-3205",
publisher = "Elsevier Inc.",
number = "15",

}

TY - JOUR

T1 - Slide-binding characterization and autoradiographic localization of delta opioid receptors in rat and mouse brains with the tetrapeptide antagonist [3H]TIPP

AU - Bakota, Lidia

AU - Szikra, Judit

AU - Toth, Geza

AU - Gulya, K.

PY - 1998/9/4

Y1 - 1998/9/4

N2 - Slide-binding and autoradiographic studies were performed on cryostat sections from brains of adult Sprague-Dawley rats and BALB C mice to describe the binding characteristics of the tetrapeptide [3H]TIPP, an antagonist with high specificity and affinity for the delta opioid receptors. Steady-state binding of [3H]TIPP to cryostat sections of brain paste was reached in 120- 180 min of incubation. Specific [3H]TIPP binding resulted in maximal numbers of binding sites (B(max)) of 15.59 and 23.91 fmol/mg protein, and dissociation constants (K(d)) of 0.46 and 0.85 nM for rat and mouse brain paste sections, respectively. TIPP displayed the highest affinity for delta opioid receptors in inhibiting specific [3H]TIPP binding, with IC50 values of 0.82 nM and 0.14 nM in rat and mouse brain sections, respectively. While DPDPE was also effective in displacing the specific binding of [3H]TIPP (IC50 = 3.18 ± 0.53 nM and 0.63 ± 0.42 nM in rat and mouse brain paste sections, respectively), other subclass-selective or nonopioid ligands were much less effective, or ineffective. Autoradiographic localization of [3H]TIPP binding revealed the characteristic distribution of delta opioid receptors in both species. In consequence of its antagonistic nature, and of its unnatural amino acid residue, which makes this ligand more resistant to biodegradation, [3H]TIPP is a superior ligand for evaluation of the binding characteristics and autoradiogaphic distribution of the delta opioid receptors.

AB - Slide-binding and autoradiographic studies were performed on cryostat sections from brains of adult Sprague-Dawley rats and BALB C mice to describe the binding characteristics of the tetrapeptide [3H]TIPP, an antagonist with high specificity and affinity for the delta opioid receptors. Steady-state binding of [3H]TIPP to cryostat sections of brain paste was reached in 120- 180 min of incubation. Specific [3H]TIPP binding resulted in maximal numbers of binding sites (B(max)) of 15.59 and 23.91 fmol/mg protein, and dissociation constants (K(d)) of 0.46 and 0.85 nM for rat and mouse brain paste sections, respectively. TIPP displayed the highest affinity for delta opioid receptors in inhibiting specific [3H]TIPP binding, with IC50 values of 0.82 nM and 0.14 nM in rat and mouse brain sections, respectively. While DPDPE was also effective in displacing the specific binding of [3H]TIPP (IC50 = 3.18 ± 0.53 nM and 0.63 ± 0.42 nM in rat and mouse brain paste sections, respectively), other subclass-selective or nonopioid ligands were much less effective, or ineffective. Autoradiographic localization of [3H]TIPP binding revealed the characteristic distribution of delta opioid receptors in both species. In consequence of its antagonistic nature, and of its unnatural amino acid residue, which makes this ligand more resistant to biodegradation, [3H]TIPP is a superior ligand for evaluation of the binding characteristics and autoradiogaphic distribution of the delta opioid receptors.

KW - Autoradiography

KW - Delta opioid antagonist

KW - Delta opioid receptor

KW - Slide- binding

UR - http://www.scopus.com/inward/record.url?scp=0032483238&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032483238&partnerID=8YFLogxK

U2 - 10.1016/S0024-3205(98)00402-0

DO - 10.1016/S0024-3205(98)00402-0

M3 - Article

C2 - 9768876

AN - SCOPUS:0032483238

VL - 63

SP - 1377

EP - 1385

JO - Life Sciences

JF - Life Sciences

SN - 0024-3205

IS - 15

ER -