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Honokiol and Magnolol Selectively Interact with GABAA Receptor Subtypes in vitro

Honokiol and Magnolol Selectively Interact with GABAA Receptor Subtypes in vitro Honokiol and magnolol have been identified as modulators of the GABA<sub>A</sub> receptors in vitro. Our previous study suggested a possible selectivity of honokiol and magnolol on GABA<sub>A </sub>receptor subtypes. This possibility was examined in the current study by <sup>3</sup>H-muscimol and <sup>3</sup>H-flunitrazepam binding assays on various rat brain membrane preparations and human recombinant GABA<sub>A</sub> receptor subunit combinations expressed by the Sf-9/baculovirus system. Generally, honokiol and magnolol have a similar enhancing effect on <sup>3</sup>H-muscimol binding to various membrane preparations in nonsaturation binding assays. Honokiol and magnolol preferentially increased <sup>3</sup>H-muscimol binding to hippocampus compared to cortex and cerebellum (with a maximum enhancement of 400% of control). As for subunit combinations, honokiol and magnolol have a more potent enhancing effect on α<sub>2</sub> subunit containing combinations (with a maximum enhancement of 400–450% of control). This action was independent of the γ subunit. In saturation binding assays, magnolol affected either the number of binding sites (ca. 4-fold on α<sub>2</sub> containing combinations) or the binding affinity (on α<sub>1</sub> containing combinations) of <sup>3</sup>H-muscimol binding to various GABA<sub>A</sub> receptor subunit combinations. In contrast, honokiol increased only binding sites on α<sub>2</sub>β<sub>3</sub>γ<sub>2s</sub> and α<sub>2</sub>β<sub>3</sub> combinations, but both the number of binding sites and the binding affinity on α<sub>1</sub>β<sub>2</sub>γ<sub>2S</sub> and α<sub>1</sub>β<sub>2</sub> combinations. These results indicate that honokiol and magnolol have some selectivity on different GABA<sub>A</sub> receptor subtypes. The property of interacting with GABA<sub>A</sub> receptors and their selectivity could be responsible for the reported in vivo effects of these two compounds. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Pharmacology Karger

Honokiol and Magnolol Selectively Interact with GABAA Receptor Subtypes in vitro

Ai, Jinglu; Wang, Xiaomei; Nielsen, Mogens
Pharmacology , Volume 63 (1): 8 – Jul 1, 2001
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References (27)

Publisher
Karger
Copyright
© 2001 S. Karger AG, Basel
ISSN
0031-7012
eISSN
1423-0313
DOI
10.1159/000056110
Publisher site
See Article on Publisher Site

Abstract

Honokiol and magnolol have been identified as modulators of the GABA<sub>A</sub> receptors in vitro. Our previous study suggested a possible selectivity of honokiol and magnolol on GABA<sub>A </sub>receptor subtypes. This possibility was examined in the current study by <sup>3</sup>H-muscimol and <sup>3</sup>H-flunitrazepam binding assays on various rat brain membrane preparations and human recombinant GABA<sub>A</sub> receptor subunit combinations expressed by the Sf-9/baculovirus system. Generally, honokiol and magnolol have a similar enhancing effect on <sup>3</sup>H-muscimol binding to various membrane preparations in nonsaturation binding assays. Honokiol and magnolol preferentially increased <sup>3</sup>H-muscimol binding to hippocampus compared to cortex and cerebellum (with a maximum enhancement of 400% of control). As for subunit combinations, honokiol and magnolol have a more potent enhancing effect on α<sub>2</sub> subunit containing combinations (with a maximum enhancement of 400–450% of control). This action was independent of the γ subunit. In saturation binding assays, magnolol affected either the number of binding sites (ca. 4-fold on α<sub>2</sub> containing combinations) or the binding affinity (on α<sub>1</sub> containing combinations) of <sup>3</sup>H-muscimol binding to various GABA<sub>A</sub> receptor subunit combinations. In contrast, honokiol increased only binding sites on α<sub>2</sub>β<sub>3</sub>γ<sub>2s</sub> and α<sub>2</sub>β<sub>3</sub> combinations, but both the number of binding sites and the binding affinity on α<sub>1</sub>β<sub>2</sub>γ<sub>2S</sub> and α<sub>1</sub>β<sub>2</sub> combinations. These results indicate that honokiol and magnolol have some selectivity on different GABA<sub>A</sub> receptor subtypes. The property of interacting with GABA<sub>A</sub> receptors and their selectivity could be responsible for the reported in vivo effects of these two compounds.

Journal

Pharmacology – Karger

Published: Jul 1, 2001

Keywords: Subtype selectivity; Honokiol; Magnolol; GABA A receptors

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