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Book: Organic cation transporters

Ciarimboli, Giuliano / Gautron, Sophie / Schlatter, Eberhard

integration of physiology, pathology, and pharmacology

2016

Keywords	Molecular biology ; Cytoplasm ; Structural biology ; Cell Membrane ; Genetics
Language	English
Size	XIV, 264 S. : Ill., graph. Darst., 235 mm x 155 mm, 0 g
Publisher	Springer
Publishing place	Cham u.a.
Publishing country	Switzerland
Document type	Book
HBZ-ID	HT018861923
ISBN	978-3-319-23792-3 ; 978-3-319-23793-0 ; 3-319-23792-6 ; 3-319-23793-4
Database	Catalogue ZB MED Medicine, Health

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Shelf mark	Loan status	Location
2016 A 137	available for loan (reading room)	Lesesaal EG

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Article ; Online: Trace Amine-Associated Receptor 1 Regulates Central Effects of Monoamine Oxidase Inhibitors: Involvement of Tyramine and Glutamate.

Gautron, Sophie

Biological psychiatry

2021 Volume 90, Issue 1, Page(s) 2–3

MeSH term(s)	Glutamic Acid ; Monoamine Oxidase ; Monoamine Oxidase Inhibitors/pharmacology ; Receptors, G-Protein-Coupled ; Tyramine
Chemical Substances	Monoamine Oxidase Inhibitors ; Receptors, G-Protein-Coupled ; Glutamic Acid (3KX376GY7L) ; Monoamine Oxidase (EC 1.4.3.4) ; Tyramine (X8ZC7V0OX3) ; Trace amine-associated receptor 1 (XMC8VP6RI2)
Language	English
Publishing date	2021-06-17
Publishing country	United States
Document type	Journal Article ; Comment
ZDB-ID	209434-4
ISSN	1873-2402 ; 0006-3223
ISSN (online)	1873-2402
ISSN	0006-3223
DOI	10.1016/j.biopsych.2021.04.021
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Article ; Online: Les transporteurs de cations organiques, nouvelles cibles thérapeutiques contre la dépression.

Gautron, Sophie / Pietranscosta, Nicolas

Medecine sciences : M/S

2020 Volume 36, Issue 8-9, Page(s) 703–705

Title translation	Organic cation transporters as novel therapeutic targets for depression.
MeSH term(s)	Affect/drug effects ; Affect/physiology ; Animals ; Central Nervous System Agents/isolation & purification ; Central Nervous System Agents/pharmacology ; Central Nervous System Agents/therapeutic use ; Depression/drug therapy ; Dopaminergic Neurons/drug effects ; Dopaminergic Neurons/physiology ; Drug Development/methods ; Drug Development/trends ; Drug Evaluation, Preclinical ; Humans ; Molecular Targeted Therapy/methods ; Molecular Targeted Therapy/trends ; Organic Cation Transport Proteins/antagonists & inhibitors ; Organic Cation Transport Proteins/physiology ; Therapies, Investigational/methods ; Therapies, Investigational/trends
Chemical Substances	Central Nervous System Agents ; Organic Cation Transport Proteins
Language	French
Publishing date	2020-08-21
Publishing country	France
Document type	News
ZDB-ID	632733-3
ISSN	1958-5381 ; 0767-0974
ISSN (online)	1958-5381
ISSN	0767-0974
DOI	10.1051/medsci/2020143
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Article ; Online: Contrasting Functions of Mitogen- and Stress-activated Protein Kinases 1 and 2 in Recognition Memory and In Vivo Hippocampal Synaptic Transmission.

Morice, Elise / Enderlin, Valérie / Gautron, Sophie / Laroche, Serge

Neuroscience

2021 Volume 463, Page(s) 70–85

Abstract: The mitogen-activated protein kinases (MAPK) are major signaling components of intracellular pathways required for memory consolidation. Mitogen- and stress-activated protein kinases 1 and 2 (MSK1 and MSK2) mediate signal transduction downstream of MAPK. ...

Abstract	The mitogen-activated protein kinases (MAPK) are major signaling components of intracellular pathways required for memory consolidation. Mitogen- and stress-activated protein kinases 1 and 2 (MSK1 and MSK2) mediate signal transduction downstream of MAPK. MSKs are activated by Extracellular-signal Regulated Kinase 1/2 (ERK1/2) and p38 MAPK. In turn, they can activate cyclic AMP-response-element-binding protein (CREB), thereby modulating the expression of immediate early genes crucial for the formation of long-term memories. While MSK1 has been previously implicated in certain forms of learning and memory, little is known concerning MSK2. Our goal was to explore the respective contribution of MSK1 and MSK2 in hippocampal synaptic transmission and plasticity and hippocampal-dependent recognition memory. In Msk1- and Msk2-knockout mice, we evaluated object and object-place recognition memory, basal synaptic transmission, paired-pulse facilitation (PPF) and inhibition (PPI), and the capacity to induce and sustain long-term potentiation (LTP) in vivo. We also assessed the level of two proteins downstream in the MAPK/ERK1/2 pathway crucial for long-term memory, CREB and the immediate early gene (IEG) Early growth response 1 (EGR1). Loss of Msk1, but not of Msk2, affected excitatory synaptic transmission at perforant path-to-dentate granule cell synapses, altered short-term presynaptic plasticity, impaired selectively long-term spatial recognition memory, and decreased basal levels of CREB and its activated form. LTP in vivo and LTP-induced CREB phosphorylation and EGR1 expression were unchanged after Msk1 or Msk2 deletion. Our findings demonstrate a dissimilar contribution of MSKs proteins in cognitive processes and suggest that Msk1 loss-of-function only has a deleterious impact on neuronal activity and hippocampal-dependent memory consolidation.
MeSH term(s)	Animals ; Hippocampus/metabolism ; Long-Term Potentiation ; Memory ; Mice ; Mitogen-Activated Protein Kinase 11 ; Mitogen-Activated Protein Kinase 8 ; Ribosomal Protein S6 Kinases, 90-kDa/metabolism ; Synaptic Transmission ; p38 Mitogen-Activated Protein Kinases
Chemical Substances	Ribosomal Protein S6 Kinases, 90-kDa (EC 2.7.11.1) ; Mitogen-Activated Protein Kinase 11 (EC 2.7.11.24) ; Mitogen-Activated Protein Kinase 8 (EC 2.7.11.24) ; p38 Mitogen-Activated Protein Kinases (EC 2.7.11.24)
Language	English
Publishing date	2021-03-17
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.2021.03.004
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Book: Organic cation transporters

Ciarimboli, Giuliano / Gautron, Sophie / Schlatter, Eberhard

integration of physiology, pathology, and pharmacology

2016

Author's details	Giuliano Ciarimboli, Sophie Gautron, Eberhard Schlatter, editors
MeSH term(s)	Organic Cation Transport Proteins/physiology ; Organic Cation Transport Proteins/pharmacology
Language	English
Size	xv, 264 pages :, illustrations (chiefly color) ;, 25 cm
Document type	Book
ISBN	9783319237923 ; 3319237926 ; 9783319237930 ; 3319237934
Database	Catalogue of the US National Library of Medicine (NLM)

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Article ; Online: Role of organic cation transporters (OCTs) in the brain.

Couroussé, Thomas / Gautron, Sophie

Pharmacology & therapeutics

2015 Volume 146, Page(s) 94–103

Abstract: Organic cation transporters (OCTs) are polyspecific facilitated diffusion transporters that contribute to the absorption and clearance of various physiological compounds and xenobiotics in mammals, by mediating their vectorial transport in kidney, liver ... ...

Abstract	Organic cation transporters (OCTs) are polyspecific facilitated diffusion transporters that contribute to the absorption and clearance of various physiological compounds and xenobiotics in mammals, by mediating their vectorial transport in kidney, liver or placenta cells. Unexpectedly, a corpus of studies within the last decade has revealed that these transporters also fulfill important functions within the brain. The high-affinity monoamine reuptake transporters (SERT, NET and DAT) exert a crucial role in the control of aminergic transmission by ensuring the rapid clearance of the released transmitters from the synaptic cleft and their recycling into the nerve endings. Substantiated evidence indicate that OCTs may serve in the brain as a compensatory clearance system in case of monoamine spillover after high-affinity transporter blockade by antidepressants or psychostimulants, and in areas of lower high-affinity transporter density at distance from the aminergic varicosities. In spite of similar anatomical profiles, the two brain OCTs, OCT2 and OCT3, show subtle differences in their distribution in the brain and their functional properties. These transporters contribute to shape a variety of central functions related to mood such as anxiety, response to stress and antidepressant efficacy, but are also implicated in other processes like osmoregulation and neurotoxicity. In this review, we discuss the recent knowledge and emerging concepts on the role of OCTs in the uptake of aminergic neurotransmitters in the brain and in these various physiological functions, focusing on the implications for mental health.
MeSH term(s)	Affect/physiology ; Animals ; Biogenic Monoamines/metabolism ; Brain/metabolism ; Humans ; Organic Cation Transport Proteins/metabolism
Chemical Substances	Biogenic Monoamines ; Organic Cation Transport Proteins
Language	English
Publishing date	2015-02
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	194735-7
ISSN	1879-016X ; 0163-7258
ISSN (online)	1879-016X
ISSN	0163-7258
DOI	10.1016/j.pharmthera.2014.09.008
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Article ; Online: Organic cation transporter 2 contributes to SSRI antidepressant efficacy by controlling tryptophan availability in the brain.

Orrico-Sanchez, Alejandro / Guiard, Bruno P / Manta, Stella / Callebert, Jacques / Launay, Jean-Marie / Louis, Franck / Paccard, Antoine / Gruszczynski, Carole / Betancur, Catalina / Vialou, Vincent / Gautron, Sophie

Translational psychiatry

2023 Volume 13, Issue 1, Page(s) 302

Abstract: Selective serotonin reuptake inhibitors (SSRI) are common first-line treatments for major depression. However, a significant number of depressed patients do not respond adequately to these pharmacological treatments. In the present preclinical study, we ... ...

Abstract	Selective serotonin reuptake inhibitors (SSRI) are common first-line treatments for major depression. However, a significant number of depressed patients do not respond adequately to these pharmacological treatments. In the present preclinical study, we demonstrate that organic cation transporter 2 (OCT2), an atypical monoamine transporter, contributes to the effects of SSRI by regulating the routing of the essential amino acid tryptophan to the brain. Contrarily to wild-type mice, OCT2-invalidated mice failed to respond to prolonged fluoxetine treatment in a chronic depression model induced by corticosterone exposure recapitulating core symptoms of depression, i.e., anhedonia, social withdrawal, anxiety, and memory impairment. After corticosterone and fluoxetine treatment, the levels of tryptophan and its metabolites serotonin and kynurenine were decreased in the brain of OCT2 mutant mice compared to wild-type mice and reciprocally tryptophan and kynurenine levels were increased in mutants' plasma. OCT2 was detected by immunofluorescence in several structures at the blood-cerebrospinal fluid (CSF) or brain-CSF interface. Tryptophan supplementation during fluoxetine treatment increased brain concentrations of tryptophan and, more discreetly, of 5-HT in wild-type and OCT2 mutant mice. Importantly, tryptophan supplementation improved the sensitivity to fluoxetine treatment of OCT2 mutant mice, impacting chiefly anhedonia and short-term memory. Western blot analysis showed that glycogen synthase kinase-3β (GSK3β) and mammalian/mechanistic target of rapamycin (mTOR) intracellular signaling was impaired in OCT2 mutant mice brain after corticosterone and fluoxetine treatment and, conversely, tryptophan supplementation recruited selectively the mTOR protein complex 2. This study provides the first evidence of the physiological relevance of OCT2-mediated tryptophan transport, and its biological consequences on serotonin homeostasis in the brain and SSRI efficacy.
MeSH term(s)	Animals ; Mice ; Anhedonia ; Antidepressive Agents/therapeutic use ; Brain/metabolism ; Corticosterone/pharmacology ; Depressive Disorder, Major/drug therapy ; Fluoxetine/pharmacology ; Kynurenine/metabolism ; Organic Cation Transporter 2/metabolism ; Selective Serotonin Reuptake Inhibitors/pharmacology ; Serotonin/metabolism ; Tryptophan/metabolism
Chemical Substances	Antidepressive Agents ; Corticosterone (W980KJ009P) ; Fluoxetine (01K63SUP8D) ; Kynurenine (343-65-7) ; Organic Cation Transporter 2 ; Selective Serotonin Reuptake Inhibitors ; Serotonin (333DO1RDJY) ; Tryptophan (8DUH1N11BX) ; Slc22a2 protein, mouse
Language	English
Publishing date	2023-09-29
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2609311-X
ISSN	2158-3188 ; 2158-3188
ISSN (online)	2158-3188
ISSN	2158-3188
DOI	10.1038/s41398-023-02596-y
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Article ; Online: Viral vector-mediated Cre recombinase expression in substantia nigra induces lesions of the nigrostriatal pathway associated with perturbations of dopamine-related behaviors and hallmarks of programmed cell death.

Rezai Amin, Sara / Gruszczynski, Carole / Guiard, Bruno P / Callebert, Jacques / Launay, Jean-Marie / Louis, Franck / Betancur, Catalina / Vialou, Vincent / Gautron, Sophie

Journal of neurochemistry

2019 Volume 150, Issue 3, Page(s) 330–340

Abstract: Cre/loxP recombination is a widely used approach to study gene function in vivo, using mice models expressing the Cre recombinase under the control of specific promoters or through viral delivery of Cre-expressing constructs. A profuse literature on ... ...

Abstract	Cre/loxP recombination is a widely used approach to study gene function in vivo, using mice models expressing the Cre recombinase under the control of specific promoters or through viral delivery of Cre-expressing constructs. A profuse literature on transgenic mouse lines points out the deleterious effects of Cre expression in various cell types and tissues, presumably by acting on illegitimate loxP-like sites present in the genome. However, most studies reporting the consequences of Cre-lox gene invalidation often omit adequate controls to exclude the potential toxic effects of Cre, compromising the interpretation of data. In this study, we report the anatomical, neurochemical, and behavioral consequences in mice of adeno-associated virus (AAV)-mediated Cre expression in the dopaminergic nuclei substantia nigra, at commonly used viral titers (3 × 10
MeSH term(s)	Animals ; Apoptosis/drug effects ; Dependovirus ; Dopamine/metabolism ; Genetic Vectors ; Integrases/administration & dosage ; Integrases/genetics ; Integrases/toxicity ; Locomotion/physiology ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Neurons/drug effects ; Neurons/metabolism ; Neurons/pathology ; Substantia Nigra/metabolism ; Substantia Nigra/pathology
Chemical Substances	Cre recombinase (EC 2.7.7.-) ; Integrases (EC 2.7.7.-) ; Dopamine (VTD58H1Z2X)
Language	English
Publishing date	2019-03-27
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80158-6
ISSN	1471-4159 ; 0022-3042 ; 1474-1644
ISSN (online)	1471-4159
ISSN	0022-3042 ; 1474-1644
DOI	10.1111/jnc.14684
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Article ; Online: Cartography of hevin-expressing cells in the adult brain reveals prominent expression in astrocytes and parvalbumin neurons.

Mongrédien, Raphaële / Erdozain, Amaia M / Dumas, Sylvie / Cutando, Laura / Del Moral, Amaia Nuñez / Puighermanal, Emma / Rezai Amin, Sara / Giros, Bruno / Valjent, Emmanuel / Meana, J Javier / Gautron, Sophie / Callado, Luis F / Fabre, Véronique / Vialou, Vincent

Brain structure & function

2019 Volume 224, Issue 3, Page(s) 1219–1244

Abstract: Hevin, also known as SPARC-like 1, is a member of the secreted protein acidic and rich in cysteine family of matricellular proteins, which has been implicated in neuronal migration and synaptogenesis during development. Unlike previously characterized ... ...

Abstract	Hevin, also known as SPARC-like 1, is a member of the secreted protein acidic and rich in cysteine family of matricellular proteins, which has been implicated in neuronal migration and synaptogenesis during development. Unlike previously characterized matricellular proteins, hevin remains strongly expressed in the adult brain in both astrocytes and neurons, but its precise pattern of expression is unknown. The present study provides the first systematic description of hevin mRNA distribution in the adult mouse brain. Using isotopic in situ hybridization, we showed that hevin is strongly expressed in the cortex, hippocampus, basal ganglia complex, diverse thalamic nuclei and brainstem motor nuclei. To identify the cellular phenotype of hevin-expressing cells, we used double fluorescent in situ hybridization in mouse and human adult brains. In the mouse, hevin mRNA was found in the majority of astrocytes but also in specific neuronal populations. Hevin was expressed in almost all parvalbumin-positive projection neurons and local interneurons. In addition, hevin mRNA was found in: (1) subsets of other inhibitory GABAergic neuronal subtypes, including calbindin, cholecystokinin, neuropeptide Y, and somatostatin-positive neurons; (2) subsets of glutamatergic neurons, identified by the expression of the vesicular glutamate transporters VGLUT1 and VGLUT2; and (3) the majority of cholinergic neurons from motor nuclei. Hevin mRNA was absent from all monoaminergic neurons and cholinergic neurons of the ascending pathway. A similar cellular profile of expression was observed in human, with expression of hevin in parvalbumin interneurons and astrocytes in the cortex and caudate nucleus as well as in cortical glutamatergic neurons. Furthermore, hevin transcript was enriched in ribosomes of astrocytes and parvalbumin neurons providing a direct evidence of hevin mRNAs translation in these cell types. This study reveals the unique and complex expression profile of the matricellular protein hevin in the adult brain. This distribution is compatible with a role of hevin in astrocytic-mediated adult synaptic plasticity and in the regulation of network activity mediated by parvalbumin-expressing neurons.
MeSH term(s)	Adult ; Aged ; Aged, 80 and over ; Animals ; Astrocytes/metabolism ; Brain/cytology ; Brain Mapping ; Calcium-Binding Proteins/genetics ; Calcium-Binding Proteins/metabolism ; Excitatory Amino Acid Transporter 1/metabolism ; Extracellular Matrix Proteins/genetics ; Extracellular Matrix Proteins/metabolism ; Female ; Humans ; Male ; Mice ; Mice, Inbred C57BL ; Middle Aged ; Nerve Tissue Proteins/metabolism ; Neurons/metabolism ; Parvalbumins/metabolism ; Postmortem Changes ; RNA, Messenger/metabolism ; Vesicular Glutamate Transport Proteins/metabolism ; Young Adult
Chemical Substances	Calcium-Binding Proteins ; Excitatory Amino Acid Transporter 1 ; Extracellular Matrix Proteins ; Nerve Tissue Proteins ; Parvalbumins ; RNA, Messenger ; SPARCL1 protein, human ; Vesicular Glutamate Transport Proteins
Language	English
Publishing date	2019-01-17
Publishing country	Germany
Document type	Journal Article
ZDB-ID	2273162-3
ISSN	1863-2661 ; 1863-2653
ISSN (online)	1863-2661
ISSN	1863-2653
DOI	10.1007/s00429-019-01831-x
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Article ; Online: Interaction of antidepressant and antipsychotic drugs with the human organic cation transporters hOCT1, hOCT2 and hOCT3.

Haenisch, Britta / Drescher, Eva / Thiemer, Lidia / Xin, Hu / Giros, Bruno / Gautron, Sophie / Bönisch, Heinz

Naunyn-Schmiedeberg's archives of pharmacology

2012 Volume 385, Issue 10, Page(s) 1017–1023

Abstract: Besides the three antidepressant-sensitive, Na(+)- and Cl(-)-dependent monoamine transporters, Na(+)-independent organic cation transporters (OCTs) are known to transport monoamines. However, little is known about the interactions of psychotropic drugs ... ...

Abstract	Besides the three antidepressant-sensitive, Na(+)- and Cl(-)-dependent monoamine transporters, Na(+)-independent organic cation transporters (OCTs) are known to transport monoamines. However, little is known about the interactions of psychotropic drugs with human (h) OCTs. In the present study, a series of diverse antidepressant and antipsychotic drugs were examined for their inhibitory potency at hOCT1, hOCT2 and hOCT3 by measuring inhibition of [(3)H]-MPP(+) uptake into HEK293 cells stably expressing one of the three hOCTs. The inhibitory potencies (IC(50)s) ranged from 1 to 900 μM. Most of the examined drugs showed highest inhibitory potency at hOCT1 which is very sparsely expressed in the brain and mainly involved in renal and hepatic clearance of cationic drugs. At their upper therapeutic plasma concentrations, several drugs are expected to inhibit by more than 20 % hOCT1 and could thus interfere with the pharmacokinetics of hOCT1-transported drugs in the kidney and liver, namely trimipramine, desipramine and fluoxetine (by about 37 %), levomepromazine and nefazodone (by about 32 %), and clozapine and amitriptyline (by about 22 %). At hOCT2 and hOCT3, which are involved in monoamine homeostasis in the brain, IC(50)s of most psychoactive drugs were in the high micromolar range. At their upper plasma concentrations, only three compounds, bupropion, nefazodone and clozapine, showed potential for inhibition, of about 18 % at hOCT2 (bupropion), about 22 % at hOCT3 (nefazodone) and of approximately 10 % at hOCT2 and hOCT3 (clozapine). Thus, under the assumption of a tenfold accumulation in the brain, bupropion, nefazodone and clozapine may notably inhibit the corresponding hOCTs. It remains to be shown whether such a direct inhibition plays a role in the clinical effects of these three drugs.
MeSH term(s)	1-Methyl-4-phenylpyridinium/pharmacokinetics ; Antidepressive Agents/pharmacology ; Antipsychotic Agents/pharmacology ; Cell Culture Techniques ; HEK293 Cells ; Humans ; Octamer Transcription Factor-3/antagonists & inhibitors ; Octamer Transcription Factor-3/genetics ; Organic Cation Transport Proteins/antagonists & inhibitors ; Organic Cation Transport Proteins/genetics ; Organic Cation Transporter 1/antagonists & inhibitors ; Organic Cation Transporter 1/genetics ; Organic Cation Transporter 2 ; Regression Analysis ; Transfection
Chemical Substances	Antidepressive Agents ; Antipsychotic Agents ; Octamer Transcription Factor-3 ; Organic Cation Transport Proteins ; Organic Cation Transporter 1 ; Organic Cation Transporter 2 ; POU5F1 protein, human ; SLC22A2 protein, human ; 1-Methyl-4-phenylpyridinium (R865A5OY8J)
Language	English
Publishing date	2012-07-18
Publishing country	Germany
Document type	Journal Article
ZDB-ID	121471-8
ISSN	1432-1912 ; 0028-1298
ISSN (online)	1432-1912
ISSN	0028-1298
DOI	10.1007/s00210-012-0781-8
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