Library Subscription: Guest
Begell Digital Portal Begell Digital Library eBooks Journals References & Proceedings Research Collections
International Journal of Physiology and Pathophysiology
SJR: 0.116

ISSN Print: 2155-014X
ISSN Online: 2155-0158

Archives: Volume 1, 2010 to Volume 9, 2018

International Journal of Physiology and Pathophysiology

DOI: 10.1615/IntJPhysPathophys.v8.i4.60
pages 337-345

Amino Acid Residues Involved in Positive Modulation of α1 Glycine Receptors by Ginkgolic Acid

Galina Maleeva
Aix Marseille University, INSERM UMR1106, INS, Inst Neurosci Syst, Marseille, France; Bogomolets Institute of Physiology, National Academy of Sciences of Ukraine, Kyiv, Ukraine
Svetlana Buldakova
Aix Marseille University, INSERM UMR1106, INS, Inst Neurosci Syst, Marseille, France
Galina G. Skibo
A. A. Bogomoletz Institute of Physiology, National Academy of Sciences of Ukraine, Kyiv, Ukraine
Piotr Bregestovski
Aix Marseille University, INSERM UMR1106, INS, Inst Neurosci Syst, Marseille, France

ABSTRACT

Previously, we have shown that ginkgolic acid has an ability to potentiate currents, mediated by α1 subunits of glycine receptor. In order to define the mechanism of the specific action of ginkgolic acid on α1 glycine receptors we have performed a comparative analysis of the amino acid sequences of α1 and α2 subunits of glycine receptor. Amino acids that contribute to the difference in interaction of ginkgolic acid with these subunits of glycine receptors were determined. Using whole-cell patch-clamp technique, we have demonstrated that mutation of three residues (T59/A26/A303) in α2 subunit for corresponding ones from α1 subunit makes α2 receptors sensitive to the potentiation by ginkgolic acid. Currents mediated by α2 mutant receptors increased by 89% ± 14 after application of ginkgolic acid. Similarly to α1 receptors, α2 mutant receptors have shown a decrease in EC50 for glycine under the action of ginkgolic acid. Thus, subunit selectivity of ginkgolic acid is strongly related to three amino acid residues that are different in α1 and α2 subunits of a glycine receptor.


Articles with similar content:

Subunit-Specific Modulation of α1 Glycine Receptors by Ginkgolic Acid
International Journal of Physiology and Pathophysiology, Vol.8, 2017, issue 4
Svetlana Buldakova, Galina Maleeva, Piotr Bregestovski
Contribution of Phosphoinositide Signaling Pathway to Opioid-Mediated Control of P2X3 Receptors in the Primary Sensory Neurons
International Journal of Physiology and Pathophysiology, Vol.7, 2016, issue 3
Igor V. Chizhmakov, Oleg O. Krishtal, Vyacheslav B. Kulyk, Oleksandr P. Maximyuk, Tetyana M. Volkova
Cocaine Inhibition of GABAA Current: Role of Dephosphorylation
Critical Reviews™ in Neurobiology, Vol.18, 2006, issue 1-2
Jun Ren, Jiang-Hong Ye
Contribution of Ca2+ Entry and Ca2+ Release Mechanisms to Purinergic Contraction of the Guinea-Pig Small Mesenteric Arteries
International Journal of Physiology and Pathophysiology, Vol.1, 2010, issue 1
Dmitri V. Gordienko, Vitali O. Bouryi, Khrystyna Yu. Sukhanova
Activation of TRPV1 by Nitric Oxide Donors Requires Co-Application of Sulfhydryl-Containing Reagent
International Journal of Physiology and Pathophysiology, Vol.9, 2018, issue 1
Bizhan R. Sharopov, Yaroslav M. Shuba