Cristina Fasolato
Cristina Fasolato
affiliation: Università di Padova
research area(s): Neuroscience, Cell Biology
Course: Biosciences and Biotechnologies
University/Istitution: Università di Padova
Curriculum Vitae of Dr. Cristina Fasolato

Name: Cristina
Surname: Fasolato
Date and place of birth: 12-06-1959, Adria (Rovigo) Italy
Marital Status: married with 2 kids

1983, graduated with full marks in Biological Sciences at the University of Padua.
1984-1986, research associate at the Institute of Biological Chemistry, University of Padua, Prof. L. Galzigna.
1987-1991, Doctorate in "Molecular and cellular biology and pathology" of the University of Padua, III cycle, supervisor Prof. T. Pozzan.
1994-1998. research associate at the Department of Biomedical Sciences, University of Padova.
1998-date Academic Researcher (Faculty of Pharmacy) at the Department of Biomedical Sciences, University of Padua.

1992-1993 EMBO fellowship recipient at the Max Planck Institut für Biophysikalische Chemie, Göttingen, Germany, supervisor Dr. R. Penner.
1996-1997 Fellowship recipient at the Catholic University of Leuven, Belgium, Department of Molecular and Cellular Biology, Faculty of Medicine, Leuven, supervisor Prof. B. Nilius.

Editorial Activity
Dr. Fasolato has been referee for various scientific journals: J. Cell Biol., Eur. J. Neurosci., Cell Calcium, Eur. J. Pharmacol., Eur. J. Biochem, J. Physiol. London, J. Neurochem., J. Biol. Chem., Cell Calcium and for the Alzheimer’s Association.
Dr. Fasolato edited with Dr. R. Rizzuto the book "Imaging living cells", published by Springer-Verlag, Heidelberg, 1998.

Teaching Activity
Dr. Fasolato is member of the teaching staff of the School of Doctorate in Biosciences and Biotechnologies– Neurobiology section – of the University of Padua
Since 1998 to date, Dr. Fasolato has been teaching “Physiology” and “Biophysics” in different courses of the Faculty of Pharmacy and the Faculty of Medicine at the University of Padua.

Scientific Society Affiliations
Dr. Fasolato is member of the “Associazione Italiana di Biologia Cellulare e del Differenziamento”, “Societa’ Italiana di Fisiologia” and “Societa’ Italiana di Neuroscienze”.
Research interests

During the doctorate, the research focused on Ca2+ homeostasis and transmembrane signaling, by using fluorescent probes specific for Ca2+ and membrane potential, as well as on inositol-phosphates turnover by HPLC analysis.
In the period spent in the group of Dr. R. Penner, Dr. Fasolato was involved in the characterization, by means of the electrophysiological technique combined with microfluorimetry, of the Ca2+ -release activated Ca2+ current, ICRAC.
Current projects focus on different aspects of Ca2+ homeostasis:
i) the dynamic properties of Ca2+ stores as well as CCE/ICRAC in excitable and non-excitable cells; ii) the role of external Ca2+ changes in neurons; iii) the linkage between Ca2+ homeostasis and Alzheimer’s Disease, with particularly attention to the role played by presenilins and beta-amyloid peptides.
M.J. KIPANYULA, L. CONTRERAS, E. ZAMPESE, C. LAZZARI, A.K.C. WONG, P. PIZZO, C. FASOLATO AND T. POZZAN (2012) Ca2+ dysregulation in neurons from transgenic mice expressing mutant presenilin 2. Aging Cell 11, 885–893 ISSN: 1474-9718, doi: 10.1111/j.1474-9726.2012.00858.x.

R. FILADI, E. ZAMPESE, T. POZZAN, P. PIZZO AND C. FASOLATO. (2012) “Endoplasmic Reticulum-mitochondria connections, calcium cross-talk and cell fate: a closer inspection” in “Endoplasmic Reticulum Stress in Health and Disease” Agostinis, P.; Samali, A. Springer Edition , Part 1, 75-106, DOI: 10.1007/978-94-007-4351-9_4

E. ZAMPESE, C. FASOLATO, J.M. KIPANYULA, M. BORTOLOZZI, T. POZZAN, AND P. PIZZO. Presenilin 2 modulates endoplasmic reticulum (ER)–mitochondria interactions and Ca2+ cross–talk. (2011). Proc Natl Acad Sci U S A., 108: 2777-82. ISSN: 0027-8424, IF 9.432

E. ZAMPESE, C. FASOLATO, T. POZZAN AND P. PIZZO (2011) Presenilin-2 modulation of ER-mitochondria interactions. FAD mutations, mechanisms and pathological consequences. Communicative & Integrative Biology 4:3, 1-4.

E. ZAMPESE, L. BRUNELLO, C. FASOLATO AND P. PIZZO. Ca2+ dysregulation mediated by presenilins in Familial Alzheimer’s Disease: causing or modulating factor? Invited review (2009). Current Trends in Neurology Vol. 3, 1-14 - issn: 0972-8252

L. BRUNELLO, E. ZAMPESE, C. FLOREAN, T. POZZAN, P. PIZZO AND C. FASOLATO. Presenilin-2 dampens intracellular Ca2+ stores by increasing Ca2+ leakage and reducing Ca2+ uptake. (2009). Journal of Cellular and Molecular Medicine Vol 13, No 9B, pp. 3358-3369

E. ZAMPESE, L. BRUNELLO, C. FASOLATO AND P. PIZZO. Ca2+ dysregulation mediated by presenilins in Familial Alzheimer’s Disease: causing or modulating factor? Invited review (2009). Current Trends in Neurology Vol. 3, 1-14 - issn: 0972-8252

G. ZATTI, A. BURGO, M. GIACOMELLO, L. BARBIERO, R. GHIDONII, G. SINIGAGLIA, C. FLOREAN, S. BAGNOLI, G. BINETTI, S. SORBI, P. PIZZO AND C. FASOLATO. Presenilin mutations linked to Familial Alzheimer’s Disease reduce endoplasmic reticulum and Golgi apparatus calcium levels (2006). Cell Calcium 39, 539-550.

F. FACCHINETTI, C. FASOLATO, E. DEL GIUDICE, A. BURGO, S. FUREGATO, M. FUSCO, E. BASSO, R. SERAGLIA, A. D’ARRIGO AND A. LEON. Nimodipine selectively stimulates -amyloid 1-42 secretion by a mechanism independent of calcium influx blockage (2006) Neurobiology of Aging 27, 218-227.

M. GIACOMELLO, L. BARBIERO, G. ZATTI, R. SQUITTI, G. BINETTI, T. POZZAN, C. FASOLATO, R. GHIDONI AND P. PIZZO. Reduction of Ca2+ storse and capacitative Ca2+ entry is associated with the familial Alzheimer’s disease presenilin-2 T122R mutation and anticipates the onset of dementia (2005) Neurobiology of Disease 18, 638-648.

G. ZATTI, R. GHIDONI; L. BARBIERO, G. BINETTI, T. POZZAN, C. FASOLATO AND P. PIZZO. The presenilin-2 M239I mutation associated with Familial Alzheimer's Disease reduces Ca2+ release from intracellular stores (2004) Neurobiology of Disease 15, 269-278.

A. BURGO, G. CARMIGNOTO, P. PIZZO, T. POZZAN AND C. FASOLATO. Paradoxical Ca2+ Rises Induced by Low External Ca2+ in Hippocampal Neurones. (2003) J. Physiol. 549.2, 537-552.

Project Title:
Processing of the amyloid precursor protein and dysregulation of organelle calcium levels by presenilins: how do they correlate? A study in cell lines
Alzheimer’s disease (AD) is a common and devastating cerebral neurodegeneration accounting for the majority of all cases of dementia. Clues to the molecular basis of AD have been obtained from knowledge of the mutant genes and the structure and function of the proteins they encode. The cause of familial AD (FAD) is a missense mutation in one of three genes coding for amyloid precursor protein (APP), presenilin-1 (PS1) and presenilin-2 (PS2). The sequential processing of the type 1 transmembrane protein APP by beta and gamma -secretases cause the formation of a peptide, known as amyloid-beta (Abeta), the main component of senile plaques, a hallmark of AD brains. A non-amyloidogenic APP processing occurs at the plasma membrane (PM) level by alfa-secretase and competes with Abeta production, which mainly occurs at the intracellular level. The two most abundant forms of Abeta are Ab40 and Ab42, this latter being considered the most toxic form, especially as a soluble oligomer. Notably all the autosomal FAD-linked mutations in APP as well as in PS (the catalytic core of the gamma-secretase) cause an increase in the Ab42/Ab40 ratio.
It has been suggested that the FAD-linked PS mutants also cause a complex dysregulation of intracellular Ca2+ homeostasis by acting at multiple levels and mainly in a way independent of gamma-secretase activity. We have recently demonstrated that both endogenous and mutant forms of PS2, but not of PS1, exert a primary role in controlling the Ca2+ dynamics of the major Ca2+ stores, i.e. the endoplasmic reticulum (ER) and the Golgi apparatus. Furthermore, upon ER Ca2+ release PS2 increases the Ca2+ response of mitochondria as well as their physical coupling with the ER at the level of the Mitochondria-Associated Membranes (MAMs). All these sites are directly implicated in APP maturation and trafficking as well as in APP sorting to the PM and, consequently on Abeta processing.
This project aims at approaching a novel issue: the control of APP maturation and processing by PS2 as a modulator of organelle Ca2+ level. FAD cases linked to mutations in PS2 are characterized by a milder phenotype and a later age of onset compared to those linked to PS1 mutations, thus being closer to sporadic AD. Moreover, dysregulation of organelle Ca2+ and ER/mitochondria connectivity is now considered to play a primary role in ageing and sporadic AD. On the base of the major role played by PS2 on Ca2+ homeostasis, we believe that this type of investigation will help to better define the still mysterious mechanisms that control APP maturation and processing in cell lines as well in brain cells from transgenic AD mouse models.