Anne Baron

Dr. Anne Baron

Université Côte d'Azur, Nice, Provence-Alpes-Côte d’Azur, France
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Research Focus & Metrics

Academic Career Length

30Years (1997-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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3 October 2012 in Nature
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Journal Article
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SDSylvie Diochot
Sylvie Diochot
ABAnne Baron
Anne Baron
MSMiguel SALINAS
Miguel SALINAS
DDDominique Douguet
Dominique Douguet
SSSabine Scarzello
Sabine Scarzello
ELEric Lingueglia
Eric Lingueglia

25 March 2004 in The EMBO Journal
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Journal Article
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SDSylvie Diochot
Sylvie Diochot
ABAnne Baron
Anne Baron
LRLachlan Rash
Lachlan Rash
EDEmmanuel Deval
Emmanuel Deval
PEPierre Escoubas
Pierre Escoubas
MLMichel Lazdunski
Michel Lazdunski
From a systematic screening of animal venoms, we isolated a new toxin (APETx2) from the sea anemone Anthopleura elegantissima , which inhibits ASIC3 homomeric channels and ASIC3‐containing heteromeric channels both in heterologous expression systems and in primary cultures of rat sensory neurons. APETx2 is a 42 amino‐acid peptide crosslinked by three disulfide bridges, with a structural organization similar to that of other sea anemone toxins that inhibit voltage‐sensitive Na+ and K+ channels. APETx2 reversibly inhibits rat ASIC3 (IC50=63 nM), without any effect on ASIC1a, ASIC1b, and ASIC2a. APETx2 directly inhibits the ASIC3 channel by acting at its external side, and it does not modify the channel unitary conductance. APETx2 also inhibits heteromeric ASIC2b+3 current (IC50=117 nM), while it has less affinity for ASIC1b+3 (IC50=0.9 μM), ASIC1a+3 (IC50=2 μM), and no effect on the ASIC2a+3 current. The ASIC3‐like current in primary cultured sensory neurons is partly and reversibly inhibited by APETx2 with an IC50 of 216 nM, probably due to the mixed inhibitions of various co‐expressed ASIC3‐containing channels.

1 December 2010 in Pharmacology & Therapeutics
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Journal Article
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EDEmmanuel Deval
Emmanuel Deval
Xavier GasullXavier Gasull
Xavier Gasull
JNJacques Noël
Jacques Noël
MSMiguel SALINAS
Miguel SALINAS
ABAnne Baron
Anne Baron
ELEric Lingueglia
Eric Lingueglia

15 December 2002 in The Journal of Neuroscience
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JMJulien Mamet
Julien Mamet
ABAnne Baron
Anne Baron
MLMichel Lazdunski
Michel Lazdunski
NVNicolas Voilley
Nicolas Voilley
Tissue acidosis is an important feature of inflammation. It is a direct cause of pain and hyperalgesia. Protons activate sensory neurons mainly through acid-sensing ion channels (ASICs) and the subsequent membrane depolarization that leads to action potential generation. We had previously shown that ASIC transcript levels were increased in inflammatory conditions in vivo. We have now found that this increase is caused by the proinflammatory mediators NGF, serotonin, interleukin-1, and bradykinin. A mixture of these mediators increases ASIC-like current amplitude on sensory neurons as well as the number of ASIC-expressing neurons and leads to a higher sensory neuron excitability. An analysis of the promoter region of the ASIC3 encoding gene, an ASIC specifically expressed in sensory neurons and associated with chest pain that accompanies cardiac ischemia, reveals that gene transcription is controlled by NGF and serotonin.

15 July 2007 in Nature Neuroscience
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MMMichel Mazzuca
Michel Mazzuca
CHCatherine Heurteaux
Catherine Heurteaux
AAAbdelkrim Alloui
Abdelkrim Alloui
SDSylvie Diochot
Sylvie Diochot
ABAnne Baron
Anne Baron
MLMichel Lazdunski
Michel Lazdunski

1 September 2001 in Journal of Biological Chemistry
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Journal Article
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ABAnne Baron
Anne Baron
LSLionel Schaefer
Lionel Schaefer
ELEric Lingueglia
Eric Lingueglia
GCGuy Champigny
Guy Champigny
MLMichel Lazdunski
Michel Lazdunski
Acid-sensing ion channels (ASICs) are cationic channels activated by extracellular protons. They are expressed in sensory neurons, where they are thought to be involved in pain perception associated with tissue acidosis. They are also expressed in brain. A number of brain regions, like the hippocampus, contain large amounts of chelatable vesicular Zn2+. This paper shows that Zn2+ potentiates the acid activation of homomeric and heteromeric ASIC2a-containing channels (i.e.ASIC2a, ASIC1a+2a, ASIC2a+3), but not of homomeric ASIC1a and ASIC3. The EC50 for Zn2+ potentiation is 120 and 111 μm for the ASIC2a and ASIC1a+2a current, respectively. Zn2+ shifts the pH dependence of activation of the ASIC1a+2a current from a pH0.5 of 5.5 to 6.0. Systematic mutagenesis of the 10 extracellular histidines of ASIC2a leads to the identification of two residues (His-162 and His-339) that are essential for the Zn2+ potentiating effect. Mutation of another histidine residue, His-72, abolishes the pH sensitivity of ASIC2a. This residue, which is located just after the first transmembrane domain, seems to be an essential component of the extracellular pH sensor of ASIC2a.