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Article ; Online: State-dependent energetics of GABA

Borghese, Cecilia M / Goldschen-Ohm, Marcel P

2024

Language	English
Publishing date	2024-02-01
Publishing country	United States
Document type	Journal Article
ZDB-ID	218078-9
ISSN	1542-0086 ; 0006-3495
ISSN (online)	1542-0086
ISSN	0006-3495
DOI	10.1016/j.bpj.2024.01.035
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Article: A potential cost of evolving epibatidine resistance in poison frogs.

York, Julia M / Borghese, Cecilia M / George, Andrew A / Cannatella, David C / Zakon, Harold H

bioRxiv : the preprint server for biology

2023

Abstract: Background: Some poison arrow frogs sequester the toxin epibatidine as a defense against predators. We previously identified a single amino acid substitution (S108C) at a highly conserved site in a neuronal nicotinic acetylcholine receptor (nAChR) ß2 ... ...

Abstract	Background: Some poison arrow frogs sequester the toxin epibatidine as a defense against predators. We previously identified a single amino acid substitution (S108C) at a highly conserved site in a neuronal nicotinic acetylcholine receptor (nAChR) ß2 subunit that prevents epibatidine from binding to this receptor. When placed in a homologous mammalian nAChR this substitution minimized epibatidine binding but also perturbed acetylcholine binding, a clear cost. However, in the nAChRs of poison arrow frogs, this substitution appeared to have no detrimental effect on acetylcholine binding and, thus, appeared cost-free. Results: The introduction of S108C into the α4β2 nAChRs of non-dendrobatid frogs also does not affect ACh sensitivity, when these receptors are expressed in Conclusions: While S108C protects these species against sequestered epibatidine, it incurs a potential physiological cost of disrupted α4β2 nAChR function. These results may explain the high conservation of a serine at this site in vertebrates, as well as provide an example of a tradeoff between beneficial and deleterious effects of an evolutionary change. They also provide important clues for future work on assembly and trafficking of this important neurotransmitter receptor.
Language	English
Publishing date	2023-01-04
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.01.04.522789
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Article ; Online: The molecular pharmacology of volatile anesthetics.

Borghese, Cecilia M

International anesthesiology clinics

2015 Volume 53, Issue 2, Page(s) 28–39

MeSH term(s)	Anesthetics, Inhalation/pharmacology ; Humans ; Molecular Biology ; Pharmacology
Chemical Substances	Anesthetics, Inhalation
Language	English
Publishing date	2015
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	210757-0
ISSN	1537-1913 ; 0020-5907
ISSN (online)	1537-1913
ISSN	0020-5907
DOI	10.1097/AIA.0000000000000060
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Article ; Online: A potential cost of evolving epibatidine resistance in poison frogs.

York, Julia M / Borghese, Cecilia M / George, Andrew A / Cannatella, David C / Zakon, Harold H

BMC biology

2023 Volume 21, Issue 1, Page(s) 144

Abstract: Background: Some dendrobatid poison frogs sequester the toxin epibatidine as a defense against predators. We previously identified an amino acid substitution (S108C) at a highly conserved site in a nicotinic acetylcholine receptor β2 subunit of ... ...

Abstract	Background: Some dendrobatid poison frogs sequester the toxin epibatidine as a defense against predators. We previously identified an amino acid substitution (S108C) at a highly conserved site in a nicotinic acetylcholine receptor β2 subunit of dendrobatid frogs that decreases sensitivity to epibatidine in the brain-expressing α4β2 receptor. Introduction of S108C to the orthologous high-sensitivity human receptor similarly decreased sensitivity to epibatidine but also decreased sensitivity to acetylcholine, a potential cost if this were to occur in dendrobatids. This decrease in the acetylcholine sensitivity manifested as a biphasic acetylcholine concentration-response curve consistent with the addition of low-sensitivity receptors. Surprisingly, the addition of the β2 S108C into the α4β2 receptor of the dendrobatid Epipedobates anthonyi did not change acetylcholine sensitivity, appearing cost-free. We proposed that toxin-bearing dendrobatids may have additional amino acid substitutions protecting their receptors from alterations in acetylcholine sensitivity. To test this, in the current study, we compared the dendrobatid receptor to its homologs from two non-dendrobatid frogs. Results: The introduction of S108C into the α4β2 receptors of two non-dendrobatid frogs also does not affect acetylcholine sensitivity suggesting no additional dendrobatid-specific substitutions. However, S108C decreased the magnitude of neurotransmitter-induced currents in Epipedobates and the non-dendrobatid frogs. We confirmed that decreased current resulted from fewer receptors in the plasma membrane in Epipedobates using radiolabeled antibodies against the receptors. To test whether S108C alteration of acetylcholine sensitivity in the human receptor was due to (1) adding low-sensitivity binding sites by changing stoichiometry or (2) converting existing high- to low-sensitivity binding sites with no stoichiometric alteration, we made concatenated α4β2 receptors in stoichiometry with only high-sensitivity sites. S108C substitutions decreased maximal current and number of immunolabeled receptors but no longer altered acetylcholine sensitivity. Conclusions: The most parsimonious explanation of our current and previous work is that the S108C substitution renders the β2 subunit less efficient in assembling/trafficking, thereby decreasing the number of receptors in the plasma membrane. Thus, while β2 S108C protects dendrobatids against sequestered epibatidine, it incurs a potential physiological cost of disrupted α4β2 receptor function.
MeSH term(s)	Humans ; Acetylcholine/pharmacology ; Poisons ; Pyridines/pharmacology ; Bridged Bicyclo Compounds, Heterocyclic/pharmacology
Chemical Substances	epibatidine (M6K314F1XX) ; Acetylcholine (N9YNS0M02X) ; Poisons ; Pyridines ; Bridged Bicyclo Compounds, Heterocyclic
Language	English
Publishing date	2023-06-28
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, Non-U.S. Gov't
ZDB-ID	2133020-7
ISSN	1741-7007 ; 1741-7007
ISSN (online)	1741-7007
ISSN	1741-7007
DOI	10.1186/s12915-023-01637-8
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Article ; Online: A potential cost of evolving epibatidine resistance in poison frogs

Julia M. York / Cecilia M. Borghese / Andrew A. George / David C. Cannatella / Harold H. Zakon

BMC Biology, Vol 21, Iss 1, Pp 1-

2023 Volume 16

Abstract: Abstract Background Some dendrobatid poison frogs sequester the toxin epibatidine as a defense against predators. We previously identified an amino acid substitution (S108C) at a highly conserved site in a nicotinic acetylcholine receptor β2 subunit of ... ...

Abstract	Abstract Background Some dendrobatid poison frogs sequester the toxin epibatidine as a defense against predators. We previously identified an amino acid substitution (S108C) at a highly conserved site in a nicotinic acetylcholine receptor β2 subunit of dendrobatid frogs that decreases sensitivity to epibatidine in the brain-expressing α4β2 receptor. Introduction of S108C to the orthologous high-sensitivity human receptor similarly decreased sensitivity to epibatidine but also decreased sensitivity to acetylcholine, a potential cost if this were to occur in dendrobatids. This decrease in the acetylcholine sensitivity manifested as a biphasic acetylcholine concentration–response curve consistent with the addition of low-sensitivity receptors. Surprisingly, the addition of the β2 S108C into the α4β2 receptor of the dendrobatid Epipedobates anthonyi did not change acetylcholine sensitivity, appearing cost-free. We proposed that toxin-bearing dendrobatids may have additional amino acid substitutions protecting their receptors from alterations in acetylcholine sensitivity. To test this, in the current study, we compared the dendrobatid receptor to its homologs from two non-dendrobatid frogs. Results The introduction of S108C into the α4β2 receptors of two non-dendrobatid frogs also does not affect acetylcholine sensitivity suggesting no additional dendrobatid-specific substitutions. However, S108C decreased the magnitude of neurotransmitter-induced currents in Epipedobates and the non-dendrobatid frogs. We confirmed that decreased current resulted from fewer receptors in the plasma membrane in Epipedobates using radiolabeled antibodies against the receptors. To test whether S108C alteration of acetylcholine sensitivity in the human receptor was due to (1) adding low-sensitivity binding sites by changing stoichiometry or (2) converting existing high- to low-sensitivity binding sites with no stoichiometric alteration, we made concatenated α4β2 receptors in stoichiometry with only high-sensitivity sites. S108C ...
Keywords	Evolution ; Nicotinic acetylcholine receptor ; Poison frog ; Epibatidine ; Epipedobates anthonyi ; Xenopus tropicalis ; Biology (General) ; QH301-705.5
Subject code	572
Language	English
Publishing date	2023-06-01T00:00:00Z
Publisher	BMC
Document type	Article ; Online
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Article ; Online: (+)-Catharanthine potentiates the GABA

Arias, Hugo R / Borghese, Cecilia M / Germann, Allison L / Pierce, Spencer R / Bonardi, Alessandro / Nocentini, Alessio / Gratteri, Paola / Thodati, Thanvi M / Lim, Natalie J / Harris, R Adron / Akk, Gustav

Biochemical pharmacology

2022 Volume 199, Page(s) 114993

Abstract: Catharanthine, a coronaridine congener, potentiates the γ-aminobutyric acid type A receptor ( ... ...

Abstract	(+)-Catharanthine, a coronaridine congener, potentiates the γ-aminobutyric acid type A receptor (GABA
MeSH term(s)	Binding Sites ; Etomidate/chemistry ; Etomidate/pharmacology ; Molecular Docking Simulation ; Neurosteroids ; Receptors, GABA-A/metabolism ; Vinca Alkaloids ; gamma-Aminobutyric Acid/pharmacology
Chemical Substances	Neurosteroids ; Receptors, GABA-A ; Vinca Alkaloids ; gamma-Aminobutyric Acid (56-12-2) ; catharanthine (WT0YJV846J) ; Etomidate (Z22628B598)
Language	English
Publishing date	2022-03-15
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	208787-x
ISSN	1873-2968 ; 0006-2952
ISSN (online)	1873-2968
ISSN	0006-2952
DOI	10.1016/j.bcp.2022.114993
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Article ; Online: Modulation of α1β3γ2 GABA

Borghese, Cecilia M / Wang, Hua-Yu L / McHardy, Stanton F / Messing, Robert O / Trudell, James R / Harris, R Adron / Bertaccini, Edward J

Proceedings of the National Academy of Sciences of the United States of America

2021 Volume 118, Issue 8

Abstract: Tethered photoswitches are molecules with two photo-dependent isomeric forms, each with different actions on their biological targets. They include reactive chemical groups capable of covalently binding to their target. Our aim was to develop a β-subunit- ...

Abstract	Tethered photoswitches are molecules with two photo-dependent isomeric forms, each with different actions on their biological targets. They include reactive chemical groups capable of covalently binding to their target. Our aim was to develop a β-subunit-tethered propofol photoswitch (MAP20), as a tool to better study the mechanism of anesthesia through the GABA
MeSH term(s)	Anesthetics, Intravenous/pharmacology ; Animals ; Cell Membrane/drug effects ; Cell Membrane/metabolism ; Cell Membrane/radiation effects ; Humans ; Light ; Oocytes/drug effects ; Oocytes/metabolism ; Oocytes/radiation effects ; Propofol/pharmacology ; Protein Conformation ; Protein Domains ; Receptors, GABA-A/chemistry ; Receptors, GABA-A/drug effects ; Receptors, GABA-A/metabolism ; Receptors, GABA-A/radiation effects ; Xenopus laevis ; gamma-Aminobutyric Acid
Chemical Substances	Anesthetics, Intravenous ; Receptors, GABA-A ; gamma-Aminobutyric Acid (56-12-2) ; Propofol (YI7VU623SF)
Language	English
Publishing date	2021-02-08
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2008178118
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Article: Alcohol Dependence and Genes Encoding α2 and γ1 GABAA Receptor Subunits: Insights from Humans and Mice.

Borghese, Cecilia M / Harris, R Adron

Alcohol research : current reviews

2012 Volume 34, Issue 3, Page(s) 345–353

Abstract: One approach to identifying the causes of alcoholism, particularly without crossing ethical boundaries in human subjects, is to look at the person's genome (and particularly at the variations that naturally arise in the DNA) to identify those variations ... ...

Abstract	One approach to identifying the causes of alcoholism, particularly without crossing ethical boundaries in human subjects, is to look at the person's genome (and particularly at the variations that naturally arise in the DNA) to identify those variations that seem to be found more commonly in people with the disease. Some of these analyses have focused on the genes that encode subunits of the receptor for the brain chemical (i.e., neurotransmitter) γ-aminobutyric acid (GABA). Different epidemiological genetic studies have provided evidence that variations in certain GABAA receptor (GABAA-R) subunits, particularly subunits α2 and γ1, are correlated with alcohol dependence. Manipulations of these genes and their expression in mice and rats also are offering clues as to the role of specific GABAA-Rs in the molecular mechanisms underlying alcoholism and suggest possibilities for new therapeutic approaches.
MeSH term(s)	Alcoholism/genetics ; Animals ; Brain/metabolism ; Genome ; Humans ; Mice ; Receptors, GABA-A ; gamma-Aminobutyric Acid
Chemical Substances	Receptors, GABA-A ; gamma-Aminobutyric Acid (56-12-2)
Language	English
Publishing date	2012-11-06
Publishing country	United States
Document type	Editorial
ISSN	2168-3492
ISSN	2168-3492
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Article ; Online: Apremilast regulates acute effects of ethanol and other GABAergic drugs via protein kinase A-dependent signaling.

Blednov, Yuri A / Borghese, Cecilia M / Dugan, Michael P / Pradhan, Swetak / Thodati, Thanvi M / Kichili, Nikhita R / Harris, R Adron / Messing, Robert O

Neuropharmacology

2020 Volume 178, Page(s) 108220

Abstract: Phosphodiesterase type 4 (PDE4) inhibitors prevent hydrolysis of cyclic adenosine monophosphate and increase protein kinase A (PKA)-mediated phosphorylation. PDE4 inhibitors also regulate responses to ethanol and GABAergic drugs. We investigated ... ...

Abstract	Phosphodiesterase type 4 (PDE4) inhibitors prevent hydrolysis of cyclic adenosine monophosphate and increase protein kinase A (PKA)-mediated phosphorylation. PDE4 inhibitors also regulate responses to ethanol and GABAergic drugs. We investigated mechanisms by which the PDE4 inhibitor, apremilast, regulates acute effects of ethanol and GABAergic drugs in male and female mice. Apremilast prolonged the sedative-hypnotic effects of gaboxadol, zolpidem, and propofol but did not alter etomidate effects, and unexpectedly shortened the sedative-hypnotic effects of diazepam. Apremilast prolonged rotarod ataxia induced by zolpidem, propofol, and loreclezole, shortened recovery from diazepam, but had no effect on ataxia induced by gaboxadol or etomidate. The PKA inhibitor H-89 blocked apremilast's ability to prolong the sedative-hypnotic effects of ethanol, gaboxadol, and propofol and to prolong ethanol- and propofol-induced ataxia. H-89 also blocked apremilast's ability to shorten the sedative-hypnotic and ataxic effects of diazepam. The β1-specific antagonist, salicylidene salicylhydrazide (SCS), produced faster recovery from ethanol- and diazepam-induced ataxia, but did not alter propofol- or etomidate-induced ataxia. SCS shortened the sedative-hypnotic effects of ethanol and diazepam but not of propofol. In Xenopus oocytes, a phosphomimetic (aspartate) mutation at the PKA phosphorylation site in β1 subunits decreased the maximal GABA current in receptors containing α1 or α3, but not α2 subunits. In contrast, phosphomimetic mutations at PKA sites in β3 subunits increased the maximal GABA current in receptors containing α1 or α2, but not α3 subunits. The GABA potency and allosteric modulation by ethanol, propofol, etomidate, zolpidem, flunitrazepam, or diazepam were not altered by these mutations. We propose a model whereby apremilast increases PKA-mediated phosphorylation of β1-and β3-containing GABA
MeSH term(s)	Animals ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Dose-Response Relationship, Drug ; Ethanol/administration & dosage ; Female ; GABA Agonists/administration & dosage ; GABA Modulators/administration & dosage ; Male ; Mice ; Mice, Inbred C57BL ; Phosphodiesterase 4 Inhibitors/administration & dosage ; Receptors, GABA-A/physiology ; Reflex, Righting/drug effects ; Reflex, Righting/physiology ; Signal Transduction/drug effects ; Signal Transduction/physiology ; Thalidomide/administration & dosage ; Thalidomide/analogs & derivatives ; Xenopus laevis
Chemical Substances	GABA Agonists ; GABA Modulators ; Phosphodiesterase 4 Inhibitors ; Receptors, GABA-A ; Ethanol (3K9958V90M) ; Thalidomide (4Z8R6ORS6L) ; Cyclic AMP-Dependent Protein Kinases (EC 2.7.11.11) ; apremilast (UP7QBP99PN)
Language	English
Publishing date	2020-07-29
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	218272-5
ISSN	1873-7064 ; 0028-3908
ISSN (online)	1873-7064
ISSN	0028-3908
DOI	10.1016/j.neuropharm.2020.108220
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Article: Studies of ethanol actions on recombinant delta-containing gamma-aminobutyric acid type A receptors yield contradictory results.

Borghese, Cecilia M / Harris, R Adron

Alcohol (Fayetteville, N.Y.)

2007 Volume 41, Issue 3, Page(s) 155–162

Abstract: The gamma-aminobutyric acid type A receptors (GABAA-Rs) display a wide variety of subunit combinations. Drugs such as benzodiazepines have shown differential effects based on GABAA-R subunit composition. Actions of alcohols and volatile anesthetics ... ...

Abstract	The gamma-aminobutyric acid type A receptors (GABAA-Rs) display a wide variety of subunit combinations. Drugs such as benzodiazepines have shown differential effects based on GABAA-R subunit composition. Actions of alcohols and volatile anesthetics generally do not vary markedly with subunit composition, with low concentrations of ethanol being poor modulators of these receptors. Recent studies showed alpha(4/6)- and delta-containing GABAA-Rs (located extrasynaptically and responsible for tonic currents in selective brain regions) presenting high sensitivity to low concentrations of ethanol, but these results have not been obtained in other laboratories. We carried out additional experiments varying the receptor level of expression, and GABA and ethanol concentration, but no sensitivity to low concentrations of ethanol was detected. We will discuss these results and attempt an analysis of the possible causes for the discrepancies.
MeSH term(s)	Animals ; Central Nervous System Depressants/pharmacology ; Ethanol/pharmacology ; Humans ; Mice ; Mice, Knockout ; Receptors, GABA-A/drug effects ; Receptors, GABA-A/genetics ; Zinc/pharmacology ; gamma-Aminobutyric Acid/metabolism
Chemical Substances	Central Nervous System Depressants ; Receptors, GABA-A ; Ethanol (3K9958V90M) ; gamma-Aminobutyric Acid (56-12-2) ; Zinc (J41CSQ7QDS)
Language	English
Publishing date	2007-05-23
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	605912-0
ISSN	0741-8329
ISSN	0741-8329
DOI	10.1016/j.alcohol.2007.03.006
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