CV Science

Patrice X. PETIT Doctor es Sciences, phD, Research Director CNRS.

Course and current status

Patrice X. Petit completed his studies at  University Pierre et Maris Curie in France, with a Doctorat es Sciences and earned a Ph.D. in Biology from the University Denis Diderot in Paris. Early in his career, Patrice X. Petit worked for the French National Research Center (CNRS, since 1979). He is a Cell Biology Research Director at CNRS.

Journal reviewer for: Antioxidant, Apoptosis, Autophagy, BBA, Cancer Research, Cellular and Molecular Biology, Cell Death and Diseases, Cell death and Differentiation, Cells, Blood, FASEB Journal,  Frontiers in Bioscience-Landmark, International Journal of Molecular Sciences, Journal of Biological Chemistry, Journal of Cell Biology, Journal of Cell Science, Journal of Immunology, JoVE Research, Molecular and Cellular Biology, Molecules, Oncogene, PLoS One, Proceedings of the National Academy of Sciences USA (PNAS), Toxicology Letters.

Grant reviewer for: Academy of Sciences of Austria; Agence Nationale de Recherche, France; Agencia Nacional de Sciencia; Association pour la Recherche sur le Cancer, France; EMBO (European Molecular Biology Organization) Fellowship Program; EMBO Young Investigator Program; European Science Foundation; Fondation pour la Recherche Médicale, France; Institut National de la Santé et de la Recherche Médicale (INSERM), France; Swiss National Science Foundation.

Teaching and abroad experiment Academia of Sciences, Beijing (Pékin), China, Autonomous University of Madrid, Spain, Beatson Cancer Research Center, Glasgow, Scotland, Faculty of Sciences; Ecole Supérieure de Physique et de Chimie Industrielle de la Ville de Paris, France; University of Odense, Denmark; University of Innsbruck, Austria, Faculty of Medicine, Austria; University of Lund, Sweden; University of Lyon, Faculty of Medicine, France; University of Lyon, Scientific University, France; Medical School Manchester, Manchester, England; Max-Planc institut Martinried, München, Germany; Odense university, Odense, Denmark; University of Nice Sophia Antipolis, France; University of Paris VI, Pierre et Maris Curie, Faculty of Sciences, France; University of Paris VII Denis Diderot, Faculty of Medicine, France; University of Paris René Descartes-Necker Hospital, France; University of Paris Sud, Faculty of Sciences, France; University of Stockholm, Arrhenius Laboratoriet, Sweden; University of Strasbourg, France,; University of Umea, Sweden; University autonomous of Madrid, Madrid, Spain; University of Valencia, Faculty of Medecine, Spain; University of Vancuver, Vancouver, Canada; Caltech and san Diego University USA; ; University of Versailles-Saint Quentin, Faculty of Sciences, France; University of Whenzhou, Whenzou China; Academy of Sciences, Beinjng, China; University of Würzburg, Plant physiology department, Germany; UT SouthWestern, Dallas, Texas, USA. University of Seattle, Seattle, USA.

Licenced in History, University Paris Diderot 1979

DIU Maladies rares, University of Strasbourg 2017

Elected member of the Scientific Council of the Institut of Biological Sciences (INSB) of CNRS, 2016 - 2020

ORCID number 0000 - 0002 - 5038 - 9101

Publications : 134 occurences, 12500 citations and h index 42 (mixed sources, Web of Sciences, PubMed, ResearcgGate, Google Scolar including the plant research field).

lien: https://www.researchgate.net/profile/Patrice-Petit

Scientific summary

After an early career devoted to the physiology of lichen symbiosis (partner relationship and lectins), Patrice X. Petit specialises in the bionergetics of mitochondria in photosynthetic tissues. He keep in mind all along its work that mitochondria are issued from an early endosymbiotic context. In the 1990’s Patrice X. Petit shifted from plant physiology to mammalian cell biology studies with a special dedication to mitochondrial bionergetic.

He specialize early in flow cytometry techniques and developed a fine analysis of isolated mitochondria in flow together with a special dedication to bioenergetic (and also of other organelles like chloroplast, nuclei and also lipidic vesicles (GUVs).

Patrice X. Petit was leading the discovery of involvement of mitochondria in apoptosis (mainly centered around a drop in mitochondrial membrane potential and the fact that mitochondrial membrane permeabilization is a concrete step in the process of programmed cell death). At first, he published with B. Mignotte and J.L. Vayssière (1994) in PNAS, the pioneering work highlighting the essential role of mitochondrial potential in the early stages of apoptosis and on is proper name in 1995 in Journal of Cell Biology. He pursued this work afterwards as senior scientist in the Guido’s Kroemer team (Journal of Exp.Med. a and b in 1995). Clearly the change of theme and the meeting with apoptosis specialists (J.L. Vayssière and Bernard Mignotte), allowed me, as a specialist in mitochondrial bioenergetics, to point out the missing link between pro-apototic signalling from the plasma membrane to the executing caspases, i.e. the destabilisation of the mitochondrial compartment in terms of membrane potential, structure and permeability of the outer membrane (PNAS 1994 Vol. 91, pp. 11752-11756, and J. Cell Bio. 1995, 130, 1, 157-167). This work formed the basis for the subsequent discovery of cytochrome c release and its adaptation to APAF-1/caspase-9 as a major pathway for the induction of apoptosis (Li P and X. Wang Cell. 1997 Nov 14;91(4):479-89

His work has had far reaching implications for the comprehension, detection and therapeutic manipulation of cellular demise

He continued his research with one of the least studied proteins of the Bcl-2 family Bid. Bid is a proapoptotic member of the Bcl-2 family of cell death regulators. Bid shares sequence homology with other members of the family within a single α-helical domain, BH3. BH3 is required for Bid to interact with Bcl2 and Bax, as well as for its function as a death agonist.

In this context he discovered that tBid requires cardiolipin-activated caspase-8 to assume its role of destabilizing mitochondrial homeostasis to allow the action of Bax or Bak.  He introduced for the first time the notion of a "mitochondrial activating platform", composed of Cardiolipin-Caspase-8 and tBid.

Intrigued by the cardiolipin (CL) component of the mitochondria membranes , he continued his work with a model of human pathology (a rare disease), called Barth syndrome,  where the CL are less abundant and monolysocardiolipin accumulated. Indeed the amount and quality of the CL decipher for the defect of mitochondria detected within this pathology, as the mitochondrial membrane potential reduction with an abnormal ROS production. CL abnormality is directlely associated to a reduction of the membrane potential that directly affects the mitochondrial homeostasis and impacts both apoptosis and autophagy

Reducing equivalents are essential not only for energy conversion, but also for maintaining a redox buffer, which is required to detoxify reactive oxygen species (ROS). Defects in CL may also affect Ca²⁺ uptake into mitochondria and thereby hamper energy supply and demand matching, but also detoxification of ROS. So, Patrice X. Petit started to work with some neutraceuticals that are susceptible of reduce ROS level and eventually to chelate metal ions, with a special attention to curcumin. He discovered the impact of curcumin not only in reducing ROS level but its ability to inhibit cell death and to regulate autophagy.

• Tafazzin Mutation Affecting Cardiolipin Leads to Increased Mitochondrial Superoxide Anions
and Mitophagy Inhibition in Barth Syndrome. Petit P.X., Ardilla-Osorio H.,Penalvia L. and Rainey Nathan N.E., Cells 2020, 9, 2333; doi:10.3390/cells9102333

• Highlighting Curcumin-Induced Crosstalk between Autophagy and Apoptosis as Supported by Its Specific Subcellular Localization. de Oyanguren F.J.S., Rainey N.E., Moustapha A., Saric A., Sureau F., O’Connor J.E. and Petit P.X. Cells 2020, 9, 361.

• Barth syndrome: Cellular compensation of mitochondrial dysfunction and apoptosis inhibition due to changes in cardiolipin remodeling linked to tafazzin (TAZ) gene mutation
Gonzalvez F.,D'Aurelio M., Boutant M., Moustapha A., Puech J.P., Landes T., Arnauné Pelloquin L., Vial G.,Taleux N., Slomianny C., Wanders R.J., Houtkooper R.H., Pascale Bellenguer P., Møller I.M., Gottlieb E., Vaz F.M., Manfredi G. and Petit P.X.. Biochimica et Biophysica Acta 1832 (2013) 1194–1206.

• Analysis of the membrane potential of rat‐and mouse‐liver mitochondria by flow cytometry and possible applications PX Petit, JE O’Connor, D Grunwald, SC Brown - European journal of biochemistry, 1990 Cited by 265 (premises)

• Alterations in mitochondrial structure and function are early events of dexamethasone-induced thymocyte apoptosis. PX Petit, H Lecoeur, E Zorn, C Dauguet, B Mignotte… - The Journal of cell biology, 1995 Cited by 748

• Sequential reduction of mitochondrial transmembrane potential and generation of reactive oxygen species in early programmed cell death. N Zamzami, P Marchetti, M Castedo, D Decaudin…Petit PX… - The Journal of experimental medicine (a), 1995 Cited by 1861

• Reduction in mitochondrial potential constitutes an early irreversible step of programmed lymphocyte death in vivo. N Zamzami, P Marchetti, M Castedo, C Zanin…Petit PX… - The Journal of experimental medicine (b), 1995 Cited by 1478

• The biochemistry of programmed cell death G Kroemer, PX Petit, N Zamzami, JL Vayssière… - The FASEB Journal, 1995 Cited by 1291

• Mitochondria and programmed cell death: back to the future PX Petit, SA Susin, N Zamzami, B Mignotte, G Kroemer - FEBS letters, 1996 Cited by 597

• Commitment to apoptosis is associated with changes in mitochondrial biogenesis and activity in cell lines conditionally immortalized with simian virus 40. JL Vayssiere, PX Petit, Y Risler, B Mignotte - Proceedings of the National Academy of Sciences, 1994 Cited by 388

• Disruption of the outer mitochondrial membrane as a result of large amplitude swelling: the impact of irreversible permeability transition PX Petit, M Goubern, P Diolez, SA Susin, N Zamzami, G Kroemer FEBS letters 426 (1), 111-116 cited by 348