Identification of the Subunit Structure of Rat Pineal Adrenergic Receptors by Photoaffinity Labeling
(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.
(Less)
- author
- Dickinson, Kenneth E.J. ; Leeb‐Lundberg, L. M.Fredrik LU ; Strasser, Ruth H. ; Caron, Marc G. and Lefkowitz, Robert J.
- publishing date
- 1986-01-01
- 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}}, }