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Article ; Online: Computational Molecular Characterization of the Interaction of Acetylcholine and the NMDA Receptor to Explain the Direct Glycine-Competitive Potentiation of NMDA-Mediated Neuronal Currents.

Islas, Ángel A / Scior, Thomas / Torres-Ramirez, Oswaldo / Salinas-Stefanon, Eduardo M / Lopez-Lopez, Gustavo / Flores-Hernandez, Jorge

ACS chemical neuroscience

2022 Volume 13, Issue 2, Page(s) 229–244

Abstract: The activation ... ...

Abstract	The activation of
MeSH term(s)	Acetylcholine ; Glycine/pharmacology ; N-Methylaspartate ; Neurons ; Receptors, N-Methyl-D-Aspartate
Chemical Substances	Receptors, N-Methyl-D-Aspartate ; N-Methylaspartate (6384-92-5) ; Acetylcholine (N9YNS0M02X) ; Glycine (TE7660XO1C)
Language	English
Publishing date	2022-01-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1948-7193
ISSN (online)	1948-7193
DOI	10.1021/acschemneuro.1c00639
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Article ; Online: Inhibition of the Human Neuronal Sodium Channel Na

Marchese-Rojas, Mario / Islas, Ángel A / Mancilla-Simbro, Claudia / Millan-PerezPeña, Lourdes / León, Jorge S / Salinas-Stefanon, Eduardo M

Neuroscience

2022 Volume 511, Page(s) 39–52

Abstract: Cannabinoids regulate analgesia, which has aroused much interest in identifying new pharmacological therapies in the management of refractory pain. Voltage-gated Na+ channels ( ... ...

Abstract	Cannabinoids regulate analgesia, which has aroused much interest in identifying new pharmacological therapies in the management of refractory pain. Voltage-gated Na+ channels (Na
MeSH term(s)	Humans ; Arachidonic Acids/pharmacology ; Sodium Channels ; Pain ; Anesthetics, Local ; Cannabinoids ; Sodium Channel Blockers/pharmacology
Chemical Substances	anandamide (UR5G69TJKH) ; arachidonyl-2-chloroethylamide ; Arachidonic Acids ; Sodium Channels ; Anesthetics, Local ; Cannabinoids ; Sodium Channel Blockers
Language	English
Publishing date	2022-09-23
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	196739-3
ISSN	1873-7544 ; 0306-4522
ISSN (online)	1873-7544
ISSN	0306-4522
DOI	10.1016/j.neuroscience.2022.09.015
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Article ; Online: Characterization of specific allosteric effects of the Na

Sánchez-Solano, Alfredo / Islas, Angel A / Scior, Thomas / Paiz-Candia, Bertin / Millan-PerezPeña, Lourdes / Salinas-Stefanon, Eduardo M

European biophysics journal : EBJ

2017 Volume 46, Issue 5, Page(s) 485–494

Abstract: The mechanism of inactivation of mammalian voltage-gated ... ...

Abstract	The mechanism of inactivation of mammalian voltage-gated Na
MeSH term(s)	Allosteric Regulation ; Amino Acid Motifs ; Animals ; Electrophysiological Phenomena ; Intracellular Space/metabolism ; Kinetics ; Models, Molecular ; Mutation ; NAV1.4 Voltage-Gated Sodium Channel/chemistry ; NAV1.4 Voltage-Gated Sodium Channel/genetics ; NAV1.4 Voltage-Gated Sodium Channel/metabolism ; Rats ; Voltage-Gated Sodium Channel beta-1 Subunit/chemistry ; Voltage-Gated Sodium Channel beta-1 Subunit/metabolism
Chemical Substances	NAV1.4 Voltage-Gated Sodium Channel ; Voltage-Gated Sodium Channel beta-1 Subunit
Language	English
Publishing date	2017-07
Publishing country	Germany
Document type	Journal Article
ZDB-ID	283671-3
ISSN	1432-1017 ; 0175-7571
ISSN (online)	1432-1017
ISSN	0175-7571
DOI	10.1007/s00249-016-1193-3
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Article ; Online: A residue W756 in the P-loop segment of the sodium channel is critical for primaquine binding.

Salinas-Stefanon, Eduardo M / Martinez-Morales, Evelyn / Scior, Thomas F / Millan-PerezPeña, Lourdes

European journal of pharmacology

2011 Volume 663, Issue 1-3, Page(s) 1–8

Abstract: Our study on the wild-type and mutants of the voltage-dependent sodium channel in the rat skeletal muscle Na(v) 1.4 was to examine the possible binding site of primaquine PQ by using an experimental approach. We used a standard voltage-clamp in oocytes. ... ...

Abstract	Our study on the wild-type and mutants of the voltage-dependent sodium channel in the rat skeletal muscle Na(v) 1.4 was to examine the possible binding site of primaquine PQ by using an experimental approach. We used a standard voltage-clamp in oocytes. Previously, we had demonstrated that PQ blocks the voltage-dependent sodium current in rat myocytes and that this blocking is concentration-dependent and voltage-independent. The direct-site mutagenesis in the P-loop segment W402C, W756C, W1239C, W1531A at the outer tryptophan-rich lip, and D400C, E758C, K1237C, A1529C of the DEKA locus helped us to identify residues playing a key role in aminoquinoline binding. In full agreement with our computed results, where a 1000-fold reduction of inhibition was measured, the tryptophan 756 is crucial for the reversible modulating effects of PQ. The W756C decreased the blocking effect of PQ in voltage-clamp assays. This new binding site may be important to the development of new drugs that modulate sodium inward currents.
MeSH term(s)	Animals ; Binding Sites ; Female ; Models, Molecular ; Mutagenesis, Site-Directed ; Primaquine/metabolism ; Protein Binding ; Protein Structure, Tertiary ; Rats ; Sodium Channels/chemistry ; Sodium Channels/genetics ; Sodium Channels/metabolism ; Substrate Specificity ; Tryptophan
Chemical Substances	Sodium Channels ; Tryptophan (8DUH1N11BX) ; Primaquine (MVR3634GX1)
Language	English
Publishing date	2011-08-01
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80121-5
ISSN	1879-0712 ; 0014-2999
ISSN (online)	1879-0712
ISSN	0014-2999
DOI	10.1016/j.ejphar.2011.04.025
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Article ; Online: Mefloquine inhibits voltage dependent Na

Paiz-Candia, Bertin / Islas, Angel A / Sánchez-Solano, Alfredo / Mancilla-Simbro, Claudia / Scior, Thomas / Millan-PerezPeña, Lourdes / Salinas-Stefanon, Eduardo M

European journal of pharmacology

2017 Volume 796, Page(s) 215–223

Abstract: Mefloquine constitutes a multitarget antimalaric that inhibits cation currents. However, the effect and the binding site of this compound on ... ...

Abstract	Mefloquine constitutes a multitarget antimalaric that inhibits cation currents. However, the effect and the binding site of this compound on Na
MeSH term(s)	Anesthetics, Local/metabolism ; Anesthetics, Local/pharmacology ; Animals ; Binding Sites ; Dose-Response Relationship, Drug ; Electrophysiological Phenomena/drug effects ; Lidocaine/metabolism ; Lidocaine/pharmacology ; Mefloquine/metabolism ; Mefloquine/pharmacology ; Molecular Docking Simulation ; Molecular Dynamics Simulation ; Mutagenesis, Site-Directed ; NAV1.4 Voltage-Gated Sodium Channel/chemistry ; NAV1.4 Voltage-Gated Sodium Channel/genetics ; NAV1.4 Voltage-Gated Sodium Channel/metabolism ; Protein Conformation ; Rats ; Voltage-Gated Sodium Channel Blockers/metabolism ; Voltage-Gated Sodium Channel Blockers/pharmacology
Chemical Substances	Anesthetics, Local ; NAV1.4 Voltage-Gated Sodium Channel ; Voltage-Gated Sodium Channel Blockers ; Lidocaine (98PI200987) ; Mefloquine (TML814419R)
Language	English
Publishing date	2017-02-05
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	80121-5
ISSN	1879-0712 ; 0014-2999
ISSN (online)	1879-0712
ISSN	0014-2999
DOI	10.1016/j.ejphar.2017.01.002
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Article: A residue W756 in the P-loop segment of the sodium channel is critical for primaquine binding

Salinas-Stefanon, Eduardo M / Martinez-Morales, Evelyn / Scior, Thomas F / Millan-PerezPeña, Lourdes

European journal of pharmacology. 2011 Aug. 1, v. 663, no. 1-3

2011

Abstract: Our study on the wild-type and mutants of the voltage-dependent sodium channel in the rat skeletal muscle Naᵥ 1.4 was to examine the possible binding site of primaquine PQ by using an experimental approach. We used a standard voltage-clamp in oocytes. ... ...

Abstract	Our study on the wild-type and mutants of the voltage-dependent sodium channel in the rat skeletal muscle Naᵥ 1.4 was to examine the possible binding site of primaquine PQ by using an experimental approach. We used a standard voltage-clamp in oocytes. Previously, we had demonstrated that PQ blocks the voltage-dependent sodium current in rat myocytes and that this blocking is concentration-dependent and voltage-independent. The direct-site mutagenesis in the P-loop segment W402C, W756C, W1239C, W1531A at the outer tryptophan-rich lip, and D400C, E758C, K1237C, A1529C of the DEKA locus helped us to identify residues playing a key role in aminoquinoline binding. In full agreement with our computed results, where a 1000-fold reduction of inhibition was measured, the tryptophan 756 is crucial for the reversible modulating effects of PQ. The W756C decreased the blocking effect of PQ in voltage-clamp assays. This new binding site may be important to the development of new drugs that modulate sodium inward currents.
Keywords	binding sites ; loci ; mutagenesis ; mutants ; myocytes ; new drugs ; oocytes ; rats ; skeletal muscle ; sodium ; sodium channels ; tryptophan
Language	English
Dates of publication	2011-0801
Size	p. 1-8.
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	80121-5
ISSN	1879-0712 ; 0014-2999
ISSN (online)	1879-0712
ISSN	0014-2999
DOI	10.1016/j.ejphar.2011.04.025
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Article ; Online: Identification of Navβ1 residues involved in the modulation of the sodium channel Nav1.4.

Islas, Angel A / Sánchez-Solano, Alfredo / Scior, Thomas / Millan-PerezPeña, Lourdes / Salinas-Stefanon, Eduardo M

PloS one

2013 Volume 8, Issue 12, Page(s) e81995

Abstract: Voltage-gated sodium channels (VGSCs) are heteromeric protein complexes that initiate action potentials in excitable cells. The voltage-gated sodium channel accessory subunit, Navβ1, allosterically modulates the α subunit pore structure upon binding. To ... ...

Abstract	Voltage-gated sodium channels (VGSCs) are heteromeric protein complexes that initiate action potentials in excitable cells. The voltage-gated sodium channel accessory subunit, Navβ1, allosterically modulates the α subunit pore structure upon binding. To date, the molecular determinants of the interface remain unknown. We made use of sequence, knowledge and structure-based methods to identify residues critical to the association of the α and β1 Nav1.4 subunits. The Navβ1 point mutant C43A disrupted the modulation of voltage dependence of activation and inactivation and delayed the peak current decay, the recovery from inactivation, and induced a use-dependent decay upon depolarisation at 1 Hz. The Navβ1 mutant R89A selectively delayed channel inactivation and recovery from inactivation and had no effect on voltage dependence or repetitive depolarisations. Navβ1 mutants Y32A and G33M selectively modified the half voltage of inactivation without altering the kinetics. Despite low sequence identity, highly conserved structural elements were identified. Our models were consistent with published data and may help relate pathologies associated with VGSCs to the Navβ1 subunit.
MeSH term(s)	Action Potentials/physiology ; Animals ; Female ; Ion Channel Gating/physiology ; Models, Molecular ; Mutagenesis, Site-Directed ; Oocytes/metabolism ; Patch-Clamp Techniques ; Protein Conformation ; Protein Subunits/genetics ; Protein Subunits/metabolism ; Sodium Channels/genetics ; Sodium Channels/metabolism ; Xenopus laevis
Chemical Substances	Protein Subunits ; Sodium Channels
Language	English
Publishing date	2013-12-16
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0081995
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Article: A mutation in the local anaesthetic binding site abolishes toluene effects in sodium channels.

Gauthereau, Marcia Y / Salinas-Stefanon, Eduardo M / Cruz, Silvia L

European journal of pharmacology

2005 Volume 528, Issue 1-3, Page(s) 17–26

Abstract: Toluene is a solvent of abuse that inhibits cardiac sodium channels in a manner that resembles the action of local anaesthetics. The purpose of this work was to analyze toluene effects on skeletal muscle sodium channels with and without beta1 subunit ( ... ...

Abstract	Toluene is a solvent of abuse that inhibits cardiac sodium channels in a manner that resembles the action of local anaesthetics. The purpose of this work was to analyze toluene effects on skeletal muscle sodium channels with and without beta1 subunit (Nav1.4+beta1 and Nav1.4-beta1, respectively) expressed in Xenopus laevis oocytes and to compare them with those produced in the F1579A mutant channel lacking a local anaesthetic binding site. Toluene inhibited Nav1.4 sodium currents (IC50=2.7 mM in Nav1.4+beta1 and 2.2 mM in Nav1.4-beta1 in a concentration dependent way. Toluene (3 mM) blocked sodium currents in Nav1.4 channels proportionally throughout the entire current-voltage relationship producing inactivation at more negative potentials. Minimal inhibition was produced by 3 mM toluene in F1579A mutant channels. Recovery from inactivation was slower both in Nav1.4 and F1579A channels in the presence of 3 mM toluene. The solvent blocked sodium currents in a use-dependent and frequency-dependent manner in Nav1.4 channels. A single mutation in the local anaesthetic binding site of Nav1.4 channels almost abolished toluene effects. These results suggest that this site is important for toluene action.
MeSH term(s)	Anesthetics, Local/metabolism ; Animals ; Binding Sites/genetics ; Dose-Response Relationship, Drug ; Humans ; Inhibitory Concentration 50 ; Kinetics ; Lidocaine/metabolism ; Membrane Potentials/drug effects ; Muscle Proteins/drug effects ; Muscle Proteins/genetics ; Muscle Proteins/metabolism ; Muscle, Skeletal/drug effects ; Muscle, Skeletal/metabolism ; Mutation ; NAV1.4 Voltage-Gated Sodium Channel ; Oocytes ; Sodium/pharmacology ; Sodium Channels/drug effects ; Sodium Channels/genetics ; Sodium Channels/metabolism ; Solvents/pharmacology ; Toluene/pharmacology ; Transfection ; Xenopus laevis
Chemical Substances	Anesthetics, Local ; Muscle Proteins ; NAV1.4 Voltage-Gated Sodium Channel ; SCN4A protein, human ; Sodium Channels ; Solvents ; Toluene (3FPU23BG52) ; Lidocaine (98PI200987) ; Sodium (9NEZ333N27)
Language	English
Publishing date	2005-12-28
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80121-5
ISSN	1879-0712 ; 0014-2999
ISSN (online)	1879-0712
ISSN	0014-2999
DOI	10.1016/j.ejphar.2005.10.069
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Article: Predicting a double mutant in the twilight zone of low homology modeling for the skeletal muscle voltage-gated sodium channel subunit beta-1 (Nav1.4 β1).

Scior, Thomas / Paiz-Candia, Bertin / Islas, Ángel A / Sánchez-Solano, Alfredo / Millan-Perez Peña, Lourdes / Mancilla-Simbro, Claudia / Salinas-Stefanon, Eduardo M

Computational and structural biotechnology journal

2015 Volume 13, Page(s) 229–240

Abstract: The molecular structure modeling of the β1 subunit of the skeletal muscle voltage-gated sodium channel (Nav1.4) was carried out in the twilight zone of very low homology. Structural significance can per se be confounded with random sequence similarities. ...

Abstract	The molecular structure modeling of the β1 subunit of the skeletal muscle voltage-gated sodium channel (Nav1.4) was carried out in the twilight zone of very low homology. Structural significance can per se be confounded with random sequence similarities. Hence, we combined (i) not automated computational modeling of weakly homologous 3D templates, some with interfaces to analogous structures to the pore-bearing Nav1.4 α subunit with (ii) site-directed mutagenesis (SDM), as well as (iii) electrophysiological experiments to study the structure and function of the β1 subunit. Despite the distant phylogenic relationships, we found a 3D-template to identify two adjacent amino acids leading to the long-awaited loss of function (inactivation) of Nav1.4 channels. This mutant type (T109A, N110A, herein called TANA) was expressed and tested on cells of hamster ovary (CHO). The present electrophysiological results showed that the double alanine substitution TANA disrupted channel inactivation as if the β1 subunit would not be in complex with the α subunit. Exhaustive and unbiased sampling of "all β proteins" (Ig-like, Ig) resulted in a plethora of 3D templates which were compared to the target secondary structure prediction. The location of TANA was made possible thanks to another "all β protein" structure in complex with an irreversible bound protein as well as a reversible protein-protein interface (our "Rosetta Stone" effect). This finding coincides with our electrophysiological data (disrupted β1-like voltage dependence) and it is safe to utter that the Nav1.4 α/β1 interface is likely to be of reversible nature.
Language	English
Publishing date	2015-03-27
Publishing country	Netherlands
Document type	Journal Article
ISSN	2001-0370
ISSN	2001-0370
DOI	10.1016/j.csbj.2015.03.005
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Article: Inhibition of cardiac Na+ current by primaquine.

Orta-Salazar, Gerardo / Bouchard, Ron A / Morales-Salgado, Fernando / Salinas-Stefanon, Eduardo M

British journal of pharmacology

2002 Volume 135, Issue 3, Page(s) 751–763

Abstract: The electrophysiological effects of the anti-malarial drug primaquine on cardiac Na(+) channels were examined in isolated rat ventricular muscle and myocytes. In isolated ventricular muscle, primaquine produced a dose-dependent and reversible depression ... ...

Abstract	The electrophysiological effects of the anti-malarial drug primaquine on cardiac Na(+) channels were examined in isolated rat ventricular muscle and myocytes. In isolated ventricular muscle, primaquine produced a dose-dependent and reversible depression of dV/dt during the upstroke of the action potential. In ventricular myocytes, primaquine blocked I(Na)(+) in a dose-dependent manner, with a K(d) of 8.2 microM. Primaquine (i) increased the time to peak current, (ii) depressed the slow time constant of I(Na)(+) inactivation, and (iii) slowed the fast component for recovery of I(Na)(+) from inactivation. Primaquine had no effect on: (i) the shape of the I - V curve, (ii) the reversal potential for Na(+), (iii) the steady-state inactivation and g(Na)(+) curves, (iv) the fast time constant of inactivation of I(Na)(+), and (v) the slow component of recovery from inactivation. Block of I(Na)(+) by primaquine was use-dependent. Data obtained using a post-rest stimulation protocol suggested that there was no closed channel block of Na(+) channels by primaquine. These results suggest that primaquine blocks cardiac Na(+) channels by binding to open channels and unbinding either when channels move between inactivated states or from an inactivated state to a closed state. Cardiotoxicity observed in patients undergoing malaria therapy with aminoquinolines may therefore be due to block of Na(+) channels, with subsequent disturbances of impulse conductance and contractility.
MeSH term(s)	Action Potentials/drug effects ; Action Potentials/physiology ; Animals ; Antimalarials/pharmacology ; Dose-Response Relationship, Drug ; Heart Ventricles/cytology ; Heart Ventricles/drug effects ; Myocardium/cytology ; Myocardium/metabolism ; Papillary Muscles/cytology ; Papillary Muscles/drug effects ; Papillary Muscles/physiology ; Potassium Channel Blockers ; Potassium Channels/physiology ; Primaquine/pharmacology ; Rats ; Rats, Sprague-Dawley ; Sodium Channel Blockers ; Sodium Channels/physiology ; Ventricular Function
Chemical Substances	Antimalarials ; Potassium Channel Blockers ; Potassium Channels ; Sodium Channel Blockers ; Sodium Channels ; Primaquine (MVR3634GX1)
Language	English
Publishing date	2002-01-22
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80081-8
ISSN	1476-5381 ; 0007-1188
ISSN (online)	1476-5381
ISSN	0007-1188
DOI	10.1038/sj.bjp.0704460
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