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Identification of the Subunit Structure of Rat Pineal Adrenergic Receptors by Photoaffinity Labeling

Dickinson, Kenneth E.J. ; Leeb‐Lundberg, L. M.Fredrik LU ; Strasser, Ruth H. ; Caron, Marc G. and Lefkowitz, Robert J. (1986) In Journal of Neurochemistry 46(4). p.1153-1160
Abstract

Abstract: The adrenergic receptors of rat pineal gland were investigated using radiolabeled ligand binding and photoaffinity labeling techniques. 125I‐2‐[β‐(4‐hydroxyphenyl)ethylaminomethyl]tetralone (125I‐HEAT) and 125I‐cyanopindolol (125I‐CYP) labeled specific sites on rat pineal gland membranes with equilibrium dissociation constants (KD) of 48 (±5) pM and 30 (±5) pM, respectively. Binding site maxima were 481 (±63) and 1,020 (±85) fmol/mg protein. The sites labeled by 125I‐HEAT had the pharmacological characteristics of α1‐adrenergic receptors. 125I‐CYP‐labeled β‐adrenergic receptors were characterized as a homogeneous population of... (More)

Abstract: The adrenergic receptors of rat pineal gland were investigated using radiolabeled ligand binding and photoaffinity labeling techniques. 125I‐2‐[β‐(4‐hydroxyphenyl)ethylaminomethyl]tetralone (125I‐HEAT) and 125I‐cyanopindolol (125I‐CYP) labeled specific sites on rat pineal gland membranes with equilibrium dissociation constants (KD) of 48 (±5) pM and 30 (±5) pM, respectively. Binding site maxima were 481 (±63) and 1,020 (±85) fmol/mg protein. The sites labeled by 125I‐HEAT had the pharmacological characteristics of α1‐adrenergic receptors. 125I‐CYP‐labeled β‐adrenergic receptors were characterized as a homogeneous population of β1‐adrenergic receptors. The α1‐ and β1‐adrenergic receptors were covalently labeled with the specific photoaffinity probes 4‐amino‐6,7‐dimethoxy‐2‐{4‐[5‐(4‐azido‐3‐[125I]iodo‐phenyl) pentanoyl]‐1‐piperazinyl}quinazoline (125I‐APDQ) and 125I‐p‐azidobenzylcarazolol (125I‐pABC). 125I‐APDQ labeled an α1‐adrenergic receptor peptide of Mr= 74,000 (±4,000), which was similar to peptides labeled in rat cerebral cortex, liver, and spleen. 125I‐pABC labeled a single β1‐adrenergic receptor peptide with a Mr= 42,000 (±1,500), which differed from the 60–65,000 peptide commonly seen in mammalian tissues. Possible reasons for these differences are discussed.

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author
; ; ; and
publishing date
type
Contribution to journal
publication status
published
subject
keywords
I‐pABC, 125I‐APDQ, Photoaffinity labeling, α ‐Adrenergic receptors, β ‐Adrenergic receptors
in
Journal of Neurochemistry
volume
46
issue
4
pages
1153 - 1160
publisher
Wiley-Blackwell
external identifiers
  • pmid:3005506
  • scopus:0022453530
ISSN
0022-3042
DOI
10.1111/j.1471-4159.1986.tb00630.x
language
English
LU publication?
no
id
1a76d7af-0c0b-4140-9a69-8e49c8e18e21
date added to LUP
2019-06-04 14:41:07
date last changed
2024-01-01 09:17:30
@article{1a76d7af-0c0b-4140-9a69-8e49c8e18e21,
  abstract     = {{<p>Abstract:  The adrenergic receptors of rat pineal gland were investigated using radiolabeled ligand binding and photoaffinity labeling techniques. <sup>125</sup>I‐2‐[β‐(4‐hydroxyphenyl)ethylaminomethyl]tetralone (<sup>125</sup>I‐HEAT) and <sup>125</sup>I‐cyanopindolol (<sup>125</sup>I‐CYP) labeled specific sites on rat pineal gland membranes with equilibrium dissociation constants (K<sub>D</sub>) of 48 (±5) pM and 30 (±5) pM, respectively. Binding site maxima were 481 (±63) and 1,020 (±85) fmol/mg protein. The sites labeled by <sup>125</sup>I‐HEAT had the pharmacological characteristics of α<sub>1</sub>‐adrenergic receptors. <sup>125</sup>I‐CYP‐labeled β‐adrenergic receptors were characterized as a homogeneous population of β<sub>1</sub>‐adrenergic receptors. The α<sub>1</sub>‐ and β<sub>1</sub>‐adrenergic receptors were covalently labeled with the specific photoaffinity probes 4‐amino‐6,7‐dimethoxy‐2‐{4‐[5‐(4‐azido‐3‐[<sup>125</sup>I]iodo‐phenyl) pentanoyl]‐1‐piperazinyl}quinazoline (<sup>125</sup>I‐APDQ) and <sup>125</sup>I‐p‐azidobenzylcarazolol (<sup>125</sup>I‐pABC). <sup>125</sup>I‐APDQ labeled an α<sub>1</sub>‐adrenergic receptor peptide of M<sub>r</sub>= 74,000 (±4,000), which was similar to peptides labeled in rat cerebral cortex, liver, and spleen. <sup>125</sup>I‐pABC labeled a single β<sub>1</sub>‐adrenergic receptor peptide with a M<sub>r</sub>= 42,000 (±1,500), which differed from the 60–65,000 peptide commonly seen in mammalian tissues. Possible reasons for these differences are discussed.</p>}},
  author       = {{Dickinson, Kenneth E.J. and Leeb‐Lundberg, L. M.Fredrik and Strasser, Ruth H. and Caron, Marc G. and Lefkowitz, Robert J.}},
  issn         = {{0022-3042}},
  keywords     = {{I‐pABC; 125I‐APDQ; Photoaffinity labeling; α ‐Adrenergic receptors; β ‐Adrenergic receptors}},
  language     = {{eng}},
  month        = {{01}},
  number       = {{4}},
  pages        = {{1153--1160}},
  publisher    = {{Wiley-Blackwell}},
  series       = {{Journal of Neurochemistry}},
  title        = {{Identification of the Subunit Structure of Rat Pineal Adrenergic Receptors by Photoaffinity Labeling}},
  url          = {{http://dx.doi.org/10.1111/j.1471-4159.1986.tb00630.x}},
  doi          = {{10.1111/j.1471-4159.1986.tb00630.x}},
  volume       = {{46}},
  year         = {{1986}},
}