Michel Lazdunski

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Michel Lazdunski
Born (1938-04-11) 11 April 1938 (age 86)
Marseille, France
EducationÉcole nationale supérieure de chimie de Clermont-Ferrand, Laval University (PhD chemistry-physics, 1962), University of Marseille (PhD biochemistry, 1964)
Known forIon channels
AwardsCNRS 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

General anaesthetics are often defined as compounds that induce a loss of consciousness in humans or loss of righting reflex in animals. Clinical definitions are also extended to include an induced coma that causes lack of awareness to painful stimuli, sufficient to facilitate surgical applications in clinical and veterinary practice. General anaesthetics do not act as analgesics and should also not be confused with sedatives. General anaesthetics are a structurally diverse group of compounds whose mechanisms encompass multiple biological targets involved in the control of neuronal pathways. The precise workings are the subject of some debate and ongoing research.

<span class="mw-page-title-main">Theories of general anaesthetic action</span> How drugs induce reversible suppression of consciousness

A general anaesthetic is a drug that brings about a reversible loss of consciousness. These drugs are generally administered by an anaesthetist/anesthesiologist to induce or maintain general anaesthesia to facilitate surgery.

<span class="mw-page-title-main">Potassium channel</span> Ion channel that selectively passes K+

Potassium channels are the most widely distributed type of ion channel found in virtually all 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.

<span class="mw-page-title-main">Two-pore-domain potassium channel</span> Class of transport proteins

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. Two-pore-domain potassium channels correspond structurally to a inward-rectifier potassium channel α-subunits. Each inward-rectifier potassium channel α-subunit is composed of two transmembrane α-helices, a pore helix and a potassium ion selectivity filter sequence and assembles into a tetramer forming the complete channel. The two-pore domain potassium channels instead are dimers where each subunit is essentially two α-subunits joined together.

<span class="mw-page-title-main">KvLQT2</span> Protein-coding gene in humans

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

<span class="mw-page-title-main">ASIC1</span> Protein-coding gene in humans

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.

<span class="mw-page-title-main">KCNK2</span> Protein-coding gene in the species Homo sapiens

Potassium channel subfamily K member 2, also known as TREK-1, is a protein that in humans is encoded by the KCNK2 gene.

<span class="mw-page-title-main">KCNK3</span> Protein-coding gene in the species Homo sapiens

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

<span class="mw-page-title-main">KCNK4</span> Protein-coding gene in the species Homo sapiens

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.

<span class="mw-page-title-main">ASIC2</span> Protein-coding gene in the species Homo sapiens

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.

<span class="mw-page-title-main">KCNB2</span> 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.

<span class="mw-page-title-main">KCNV1</span> 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.

<span class="mw-page-title-main">KCNK10</span> Protein-coding gene in the species Homo sapiens

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.

<span class="mw-page-title-main">Potassium channel blocker</span> Several medications that disrupt movement of K+ ions

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

<span class="mw-page-title-main">Channel blocker</span> Molecule able to block protein channels, frequently used as pharmaceutical

A channel blocker is the biological mechanism in which a particular molecule is used to prevent the opening of ion channels in order to produce a physiological response in a cell. Channel blocking is conducted by different types of molecules, such as cations, anions, amino acids, and other chemicals. These blockers act as ion channel antagonists, preventing the response that is normally provided by the opening of the channel.

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

Mechanosensitive channels (MSCs), mechanosensitive ion channels or stretch-gated ion channels are membrane proteins capable of responding to mechanical stress over a wide dynamic range of external mechanical stimuli. 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.

<span class="mw-page-title-main">Psalmotoxin</span>

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.

<span class="mw-page-title-main">Colin Nichols</span> English academic

Colin G. Nichols FRS is the Carl Cori Endowed Professor, and Director of the Center for Investigation of Membrane Excitability Diseases at Washington University in St. Louis, Missouri.

<span class="mw-page-title-main">Lipid-gated ion channels</span> Type of ion channel transmembrane protein

Lipid-gated ion channels are a class of ion channels whose conductance of ions through the membrane depends directly on lipids. Classically the lipids are membrane resident anionic signaling lipids that bind to the transmembrane domain on the inner leaflet of the plasma membrane with properties of a classic ligand. Other classes of lipid-gated channels include the mechanosensitive ion channels that respond to lipid tension, thickness, and hydrophobic mismatch. A lipid ligand differs from a lipid cofactor in that a ligand derives its function by dissociating from the channel while a cofactor typically derives its function by remaining bound.

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. 247 (4944). American Association for the Advancement of Science (AAAS): 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. 386 (6621). Springer Science and Business Media LLC: 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. 9 (9). Springer Science and Business Media LLC: 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. 2 (5). Springer Science and Business Media LLC: 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. 354 (6354). Springer Science and Business Media LLC: 526–528. Bibcode:1991Natur.354..526D. doi: 10.1038/354526a0 . ISSN   0028-0836. PMID   1722027. S2CID   4233457.
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