Michel Lazdunski

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Michel Lazdunski
Born (1938-04-11) 11 April 1938 (age 84)
Marseille
EducationÉcole nationale supérieure de chimie de Clermont-Ferrand, Laval University (PhD chemistry-physics, 1962), University of Marseille (PhD biochemistry, 1964)
Known forIon channels
AwardsFrench Academy of sciences, CNRS Silver Medal
Scientific career
FieldsBiochemistry
InstitutionsCNRS, Nice/Sophia Antipolis
Doctoral advisor Ludovic Ouellet

Michel Lazdunski (born 11 April 1938, in Marseille) is a French biologist specializing in biochemistry, physiology, pathophysiology, molecular pharmacology and neuroscience. [1]

Contents

Biography

Michel Lazdunski is a chemical engineer (1955), graduate of the École nationale supérieure de chimie de Clermont-Ferrand, PhD in Chemistry-Physics from Laval University in Quebec City (1962) in Canada in the laboratory of Ludovic Ouellet, then PhD in Biochemistry (University of Marseille, 1964). He began his career at the CNRS in 1962 in Marseille where he became Professor of Biochemistry in 1965.He accepted the Chair of Biochemistry at the University of Nice in 1968. He founded the CNRS Biochemistry Centre there, which he managed until 1989, when he moved to the Sophia Antipolis science park to direct the CNRS Institute of Molecular and Cellular Pharmacology, which he had just created and which he managed until 2004. During his academic career in Nice/Sophia Antipolis, he was successively Professor of Biochemistry (Faculty of Sciences), Director of Research seconded to the CNRS and Professor of Pharmacology PU-PH (Faculty of Medicine).Michel Lazdunski was a member of the Scientific Council (1997–2001) and the Board of Directors (2001–2005) of the CNRS and the Council of the European Molecular Biology Organisation (1990–1995). He has chaired many committees including the UNECE Life Sciences Committee (Human Capital and Mobility Programme 1996–1997) and the National Coordinating Committee for Life Sciences (2001–2002).[ citation needed ]

He was elected a full member of the French Academy of sciences in 1991. [2] He was appointed senior member of the Institut universitaire de France in 1991 for a five-year term, [3] renewed in 1996. [4]

Scientific contribution

The first part of Michel Lazdunski's scientific career (awarded the CNRS Silver Medal) was devoted to enzymology. He then focused on exploring the molecular machines, the ion channels, that generate bioelectricity in the brain, peripheral nervous system, heart, muscles, vessels and hormone-secreting endocrine systems and are responsible for multiple pathologies. [5] [6] He played a pioneering role in the analysis of ion channels permeable to sodium, calcium and potassium. He played a pioneering role in the study of their pharmacology by introducing many toxins, many venoms and important drugs for hypertension (calcium blockers) or diabetes (antidiabetic sulfonylureas) [5] [6] [7] The most recent work of his team has completed these pharmacological studies and amplified the discovery of new substances from venom with strong potential therapeutic possibilities. They have also led to the discovery of several new classes of ion channels essential for the sensory perception of mechanical stimuli, heat, cold and acidity. TREK/TRAAK channels, TASK channels and ASIC channels. [5] [6] [8] These families of channels play an essential role in pain perception but also in synaptic transmission and neuroprotection at the cerebral level, particularly for polyunsaturated fatty acids of the ɯɜ type. TREK channels play a central role in depression. [9] The TASK and TREK channels are a major therapeutic target for gaseous anesthetics. [5] [6] [10]

Previously, Michel Lazdunski and his team had made pioneering discoveries on the CFTR [5] [11] channel associated with cystic fibrosis, which indicated the direction to follow for current therapeutic developments on some forms of this genetic disease.

Related Research Articles

Potassium channel Ion channel that selectively passes K+

Potassium channels are the most widely distributed type of ion channel and are found in virtually all living organisms. They form potassium-selective pores that span cell membranes. Potassium channels are found in most cell types and control a wide variety of cell functions.

The two-pore-domain or tandem pore domain potassium channels are a family of 15 members that form what is known as leak channels which possess Goldman-Hodgkin-Katz (open) rectification. These channels are regulated by several mechanisms including signaling lipids, oxygen tension, pH, mechanical stretch, and G-proteins. Their name is derived from the fact that the α subunits consist of four transmembrane segments, and each pair of transmembrane segments contains a pore loop between the two transmembrane segments. Thus, each subunit has two pore loops. As such, they structurally correspond to two inward-rectifier α subunits and thus form dimers in the membrane.

KvLQT2

Kv7.2 (KvLQT2) is a voltage- and lipid-gated potassium channel protein coded for by the gene KCNQ2.

ASIC1 Protein-coding gene in the species Homo sapiens

Acid-sensing ion channel 1 (ASIC1) also known as amiloride-sensitive cation channel 2, neuronal (ACCN2) or brain sodium channel 2 (BNaC2) is a protein that in humans is encoded by the ASIC1 gene. The ASIC1 gene is one of the five paralogous genes that encode proteins that form trimeric acid-sensing ion channels (ASICs) in mammals. The cDNA of this gene was first cloned in 1996. The ASIC genes have splicing variants that encode different proteins that are called isoforms.

KCNK2

Potassium channel subfamily K member 2 is a protein that in humans is encoded by the KCNK2 gene.

KCNK3

Potassium channel subfamily K member 3 is a protein that in humans is encoded by the KCNK3 gene.

KCNK4

Potassium channel subfamily K member 4 is a protein that in humans is encoded by the KCNK4 gene. KCNK4 protein channels are also called TRAAK channels.

ASIC2

Acid-sensing ion channel 2 (ASIC2) also known as amiloride-sensitive cation channel 1, neuronal (ACCN1) or brain sodium channel 1 (BNaC1) is a protein that in humans is encoded by the ASIC2 gene. The ASIC2 gene is one of the five paralogous genes that encode proteins that form trimeric acid-sensing ion channels (ASICs) in mammals. The cDNA of this gene was first cloned in 1996. The ASIC genes have splicing variants that encode different proteins that are called isoforms.

KCNB2 Protein-coding gene in the species Homo sapiens

Potassium voltage-gated channel subfamily B member 2 is a protein that in humans is encoded by the KCNB2 gene. The protein encoded by this gene is a voltage-gated potassium channel subunit.

KCNV1 Protein-coding gene in the species Homo sapiens

Potassium voltage-gated channel subfamily V member 1 is a protein that in humans is encoded by the KCNV1 gene. The protein encoded by this gene is a voltage-gated potassium channel subunit.

KCNS2 Protein-coding gene in the species Homo sapiens

Potassium voltage-gated channel subfamily S member 2 is a protein that in humans is encoded by the KCNS2 gene. The protein encoded by this gene is a voltage-gated potassium channel subunit.

KCNK10

Potassium channel, subfamily K, member 10, also known as KCNK10 is a human gene. The protein encoded by this gene, K2P10.1, is a potassium channel containing two pore-forming P domains.

Potassium channel blocker Several medications that disrupt movement of K+ ions

Potassium channel blockers are agents which interfere with conduction through potassium channels.

A potassium channel opener is a type of drug which facilitates ion transmission through potassium channels.

Mechanosensitive channels, mechanosensitive ion channels or stretch-gated ion channels (not to be confused with mechanoreceptors). They are present in the membranes of organisms from the three domains of life: bacteria, archaea, and eukarya. They are the sensors for a number of systems including the senses of touch, hearing and balance, as well as participating in cardiovascular regulation and osmotic homeostasis (e.g. thirst). The channels vary in selectivity for the permeating ions from nonselective between anions and cations in bacteria, to cation selective allowing passage Ca2+, K+ and Na+ in eukaryotes, and highly selective K+ channels in bacteria and eukaryotes.

Psalmotoxin

Psalmotoxin (PcTx1) is a spider toxin from the venom of the Trinidad tarantula Psalmopoeus cambridgei. It selectively blocks Acid Sensing Ion Channel 1-a (ASIC1a), which is a proton-gated sodium channel.

Daniel Choquet French neuroscientist

Daniel Choquet is a French neuroscientist.

Colin Nichols English academic

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Côte dAzur University

Côte d'Azur University is a public research university located in Nice, France and neighboring areas. In 2019, it replaced the University of Nice Sophia Antipolis and the community (ComUE) that was created in 2013. On 9 January 2020, Jeanick Brisswalter was elected as president of Côte d'Azur University.

Gabriella Gobbi is a Canadian psychiatrist and neuroscientist whose research explores the potential effects of cannabis use in the treatment of mood disorders. Gobbi is a professor at McGill University's Department of Psychiatry and a Canada Research Chair in Therapeutics for Mental Health.

References

  1. ↑ "Université côte d'Azur".
  2. ↑ "Académie des sciences".
  3. ↑ "Arrêté du 2 décembre 1991 portant nomination à l'Institut universitaire de France". Legifrance. Retrieved 8 March 2020.
  4. ↑ "Arrêté du 8 août 1996 portant nomination des membres seniors et juniors de l'Institut universitaire de France". Legifrance. Retrieved 8 March 2020.
  5. 1 2 3 4 5 "Michel Lazdunski-Research gate".
  6. 1 2 3 4 Michel Lazdunski publications indexed by Google Scholar
  7. ↑ Amoroso, Salvatore; Schmid-Antomarchi, Heidy; Fosset, Michel; Lazdunski, Michel (16 February 1990). "Glucose, Sulfonylureas, and Neurotransmitter Release: Role of ATP-Sensitive K + Channels". Science. American Association for the Advancement of Science (AAAS). 247 (4944): 852–854. Bibcode:1990Sci...247..852A. doi:10.1126/science.2305257. ISSN   0036-8075. PMID   2305257.
  8. ↑ Waldmann, Rainer; Champigny, Guy; Bassilana, Frédéric; Heurteaux, Catherine; Lazdunski, Michel (1997). "A proton-gated cation channel involved in acid-sensing". Nature. Springer Science and Business Media LLC. 386 (6621): 173–177. Bibcode:1997Natur.386..173W. doi:10.1038/386173a0. ISSN   0028-0836. PMID   9062189. S2CID   4361943.
  9. ↑ Heurteaux, Catherine; Lucas, Guillaume; Guy, Nicolas; El Yacoubi, Malika; Thümmler, Susanne; Peng, Xiao-Dong; Noble, Florence; Blondeau, Nicolas; Widmann, Catherine; Borsotto, Marc; Gobbi, Gabriella; Vaugeois, Jean-Marie; Debonnel, Guy; Lazdunski, Michel (13 August 2006). "Deletion of the background potassium channel TREK-1 results in a depression-resistant phenotype". Nature Neuroscience. Springer Science and Business Media LLC. 9 (9): 1134–1141. doi:10.1038/nn1749. ISSN   1097-6256. PMID   16906152. S2CID   22729624.
  10. ↑ Patel, Amanda J.; Honoré, Eric; Lesage, Florian; Fink, Michel; Romey, Georges; Lazdunski, Michel (1999). "Inhalational anesthetics activate two-pore-domain background K+ channels". Nature Neuroscience. Springer Science and Business Media LLC. 2 (5): 422–426. doi:10.1038/8084. ISSN   1097-6256. PMID   10321245. S2CID   23092576.
  11. ↑ Dalemans, Wilfried; Barbry, Pascal; Champigny, Guy; Jallat, Sophie; Jallat, Sophie; Dott, Karin; Dreyer, Dominique; Crystal, Ronald G.; Pavirani, Andréa; Lecocq, Jean-Pierre; Lazdunski, Michel (1991). "Altered chloride ion channel kinetics associated with the ΔF508 cystic fibrosis mutation". Nature. Springer Science and Business Media LLC. 354 (6354): 526–528. Bibcode:1991Natur.354..526D. doi:10.1038/354526a0. ISSN   0028-0836. PMID   1722027. S2CID   4233457.
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