c/o Complesso Biologico Interdipartimentale
Viale Giuseppe Colombo 3
Position: Senior Researcher, Italian National Research Council (CNR), Neuroscience Institute at the Department of Biomedical Sciences, University of Padova, Italy
Doctor in Chemistry, University of Padova, Italy, (June 16, 1982)
2003-present: Senior Researcher, CNR Neuroscience Institute
1986-2002: Researcher, CNR
1989-1991: NATO-CNR Senior Fellow, Department of Molecular and Cell Biology, University of California at Berkeley (USA)
1998: Visiting Scientist, Center for Biomedical Imaging Technology, University of Connecticut Health Center, Farmington, Connecticut(USA).
1983-1986: Research Assistant, CNR
Dr. Petronilli began her studies on mitochondrial physiology and bioenergetics under the guidance of Prof. Giovanni Felice Azzone, one of the founding Fathers of Bioenergetics. Successively, in collaboration with Dr. Zoratti, she discovered and characterized, by patch-clamp technique, mega ion channels in bacteria and mithochondria. At the end of 1980s she spent 2 years at the Department of Molecular and Cell Biology, University of California at Berkeley (USA) where she worked under the supervision of Prof. G.F.-L. Ames. During this period her research was addressed to the study of the functioning mechanism of bacterial histidine permease, an ABC transporter. In 1991 she came back in Padua and joined the newly established research group, directed by Prof. Bernardi, where she has studied mitochondrial channels and their role in cellular pathophysiology. In particular, she has focused on the permeability transition pore (PTP), a high conductance channel that has been increasingly recognized as a key player in cell death. During the early 1990s she collaborated in carrying out a thorough characterization of the PTP in isolated mitochondria, and in defining key points of regulation (membrane potential, matrix pH, Me2+-binding sites, specific redox-sensitive sites). From the mid-1990s she collaborated in the development of tools to reliably monitor mitochondrial function in situ, which in turn allowed to address mechanistic questions related to PTP operation in intact cells and organs. These advances made it then possible to address the question of how pharmacological modulation of mitochondrial function in situ can be exploited to force apoptosis in cancer cells and to prevent apoptosis in degenerative diseases, an area that is still under study. At present, Dr. Petronilli is still collaborating with Prof. Bernardi group towards the molecular definition of the PTP, the identification of novel mitochondrial drugs, and their rigorous testing in relevant models of disease.
- Study of coupling mechanisms of the reactions of mitochondrial proton pumps to the translocation of protons across the membrane and role of proton electrochemical gradient as energy coupling intermediate between the proton pumps.
- Electrophysiological investigation of ionic channels in bacterial and mitochondrial
- membranes by patch-clamp technique.
- Study of transport mechanisms of ABC transporters by characterization of the bacterial histidine permease and its reconstitution in proteoliposomes.
- Characterization of the mitochondrial permeability transition pore and study of its involvement in the pathways to programmed and accidental cell death.
Giorgio V, von SS, Antoniel M, Fabbro A, Fogolari F, Forte M, Glick GD, Petronilli V, Zoratti M, Szabo I, Lippe G, and Bernardi P (2013)
Dimers of mitochondrial ATP synthase form the permeability transition pore. Proc Natl Acad Sci U S A, 110, 5887-5892
Giorgio V, Petronilli V, Ghelli A, Carelli V, Rugolo M, Lenaz G, and Bernardi P (2012)
The effects of idebenone on mitochondrial bioenergetics. Biochimica et Biophysica Acta-Bioenergetics, 1817, 363-369.
Porcelli,A.M., Angelin,A., Ghelli,A., Mariani,E., Martinuzzi,A., Carelli,V., Petronilli,V., Bernardi,P., and Rugolo,M. (2009).
Respiratory Complex I Dysfunction Due to Mitochondrial DNA Mutations Shifts the Voltage Threshold for Opening of the Permeability Transition Pore toward Resting Levels. Journal of Biological Chemistry, 284, 2045-2052
Basso,E., Petronilli,V., Forte,M.A., and Bernardi,P. (2008).
Phosphate is essential for inhibition of the mitochondrial permeability transition pore by cyclosporin A and by cyclophilin D ablation. Journal of Biological Chemistry, 283, 26307-26311.
Petronilli V, Penzo D, Scorrano L, Bernardi P, Di Lisa F. (2001)
The mitochondrial permeability transition, release of cytochrome c and cell death. Correlation with the duration of pore openings in situ. J Biol Chem; 276:12030-12034
Bernardi,P., Petronilli,V., Di Lisa,F., and Forte,M. (2001).
A mitochondrial perspective on cell death. Trends in Biochemical Sciences, 26, 112-117
Petronilli V, Miotto G, Canton M, Brini M, Colonna R, Bernardi P, Di Lisa F. (1999)
Transient and long-lasting openings of the mitochondrial permeability transition pore can be monitored directly in intact cells by changes in mitochondrial calcein fluorescence. Biophys J 1999; 76:725-734
Bernardi,P., Scorrano,L., Colonna,R., Petronilli,V., and Di Lisa,F. (1999).
Mitochondria and cell death - Mechanistic aspects and methodological issues. European Journal of Biochemistry, 264, 687-701
Bernardi,P. and Petronilli,V. (1996).
The permeability transition pore as a mitochondrial calcium release channel: A critical appraisal. Journal of Bioenergetics and Biomembranes, 28, 131-138
Petronilli,V., Costantini,P., Scorrano,L., Colonna,R., Passamonti,S., and Bernardi,P. (1994).
The Voltage Sensor of the Mitochondrial Permeability Transition Pore Is Tuned by the Oxidation-Reduction State of Vicinal Thiols - Increase of the Gating Potential by Oxidants and Its Reversal by Reducing Agents. Journal of Biological Chemistry, 269, 16638-16642
Petronilli,V., Cola,C., Massari,S., Colonna,R., and Bernardi,P. (1993).
Physiological Effectors Modify Voltage Sensing by the Cyclosporine A-Sensitive Permeability Transition Pore of Mitochondria. Journal of Biological Chemistry, 268, 21939-21945
Petronilli,V., Szabo,I., and Zoratti,M. (1989).
The Inner Mitochondrial-Membrane Contains Ion-Conducting Channels Similar to Those Found in Bacteria. Febs Letters, 259, 137-143