Adrenergic receptors in rat spinal cord

D. J. Jones; D. E. Kendall; S. J. Enna

doi:10.1016/0028-3908(82)90162-9

Adrenergic receptors in rat spinal cord

D. J. Jones, D. E. Kendall, S. J. Enna

Anesthesiology

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

35 Scopus citations

Abstract

Radioligand binding assays were used to demonstrate the presence of α₁, α(2) and β receptora in rat spinal cord. Specific and saturable binding was exhibited for [³H-WB 4101 (α₁), [³H]-aminoclonldine (α₂) and [³H]-dihydroalprenolol(β). Binding was of high affinity and the total number of binding sites (B_maxwere: α₁, 66.5 ± 1.0 fmol/mg protein; α₂, 20.0 ± 0.6 fmol/mg protein; β, 10.2 ± 0.3 fmol/mg protein. The data confirms the existence of adrenergic receptors in spinal cord and provides further evidence of the role of catecholaminergic neurons in regulating spinal cord physiology.

Original language	English (US)
Pages (from-to)	191-195
Number of pages	5
Journal	Neuropharmacology
Volume	21
Issue number	2
DOIs	https://doi.org/10.1016/0028-3908(82)90162-9
State	Published - Feb 1982

ASJC Scopus subject areas

Pharmacology
Cellular and Molecular Neuroscience

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title = "Adrenergic receptors in rat spinal cord",

abstract = "Radioligand binding assays were used to demonstrate the presence of α1, α(2) and β receptora in rat spinal cord. Specific and saturable binding was exhibited for [3H-WB 4101 (α1), [3H]-aminoclonldine (α2) and [3H]-dihydroalprenolol(β). Binding was of high affinity and the total number of binding sites (Bmaxwere: α1, 66.5 ± 1.0 fmol/mg protein; α2, 20.0 ± 0.6 fmol/mg protein; β, 10.2 ± 0.3 fmol/mg protein. The data confirms the existence of adrenergic receptors in spinal cord and provides further evidence of the role of catecholaminergic neurons in regulating spinal cord physiology.",

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AU - Enna, S. J.

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AB - Radioligand binding assays were used to demonstrate the presence of α1, α(2) and β receptora in rat spinal cord. Specific and saturable binding was exhibited for [3H-WB 4101 (α1), [3H]-aminoclonldine (α2) and [3H]-dihydroalprenolol(β). Binding was of high affinity and the total number of binding sites (Bmaxwere: α1, 66.5 ± 1.0 fmol/mg protein; α2, 20.0 ± 0.6 fmol/mg protein; β, 10.2 ± 0.3 fmol/mg protein. The data confirms the existence of adrenergic receptors in spinal cord and provides further evidence of the role of catecholaminergic neurons in regulating spinal cord physiology.

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