Carlo Rodolfo
Carlo Rodolfo
affiliation: Università di Roma Tor Vergata
research area(s): Cell Biology, Cancer Biology
Course: Cell and Molecular Biology
University/Istitution: Università di Roma Tor Vergata
Born in Vigevano (PV), February 12, 1967
Researcher, Department of Biology, University of Rome Tor Vergata
Phone: +39-0672594240

2000 PhD in Cellular and Molecular Biology, University of Rome Tor Vergata
1992 Degree in Biology (LAUREA in Scienze Biologiche), University of Pavia

Doctoral and Post-Doctoral training.
1989-1996: Undergraduate and graduate fellow at the Institute of Molecular Genetics-CNR, Pavia, Italy. Working on DNA damage and repair.

Sept 1996-Dec 1996: Visiting Fellow in the group of Prof. J.M. Egly, Institut de Génétique et de Biologie Moléculaire et Cellulaire, Strasbourg, France. Supported by a fellowship of "EC Concerted Action on DNA Repair and Cancer".

1997-1998: Fellow in the group of Prof M. Piacentini, Department of Biology University of Rome Tor Vergata, Rome, Italy. Fellowship of the European Community-Biotechnology Project.

1998-2000: PhD Student in Cellular and Molecular Biology, University of Rome Tor Vergata.

2000-2002: Post-Doc in the group of Prof M. Piacentini, Department of Biology University of Rome Tor Vergata, Rome, Italy. Fellowship of the European Community-Biotechnology Project

April 2001-June 2001: Visiting Fellow in the group of Prof. G. Kroemer, Institut Goustave Roussy, Villejuif, France. Supported by a fellowship from "Protein Crosslinking" The ESF transglutaminases program"

2002-present Researcher, Department of Biology, University of Rome Tor Vergata
Field of study: Role of Transglutaminase 2 in Programmed Cell Death, Mitochondrial physiology, Cancer and Neurodegenerative Disease's onset and development.

Since 2002: Teaching Cytology and Histology for the first level degree in Biotechnology, Faculty of Science, University of Rome Tor Vergata.
Type 2 Transglutaminase in cancer and neurodegenerative diseases.

Type 2 Transglutaminase (TG2) belongs to a family of Ca2+-dependent acyl transferases that catalyze the formation of covalent bonds between the γ-carboxamide groups of peptide-bound glutamine residues and various primary amines, including the ε-amino group of lysine in certain proteins. TG2 is a ubiquitously expressed enzyme which, in addition to its cross-linking activity, might also bind and hydrolyse GTP, thus acting as a G-protein in adrenergics, thromboxane, and oxytocin receptor signalling, and reduce/oxidise disulphide bonds, thus acting as a protein disulphide isomerase (PDI). The PDI activity it's mainly exerted at mitochondrial level, where it results to be important in the correct assembly of the mitochondrial respiratory chains protein complexes. In addition, TG2 may interact with and modify some mitochondrial resident or translocated proteins such as the Adenine Nucleotide Transferase (ANT1) and the pro-apoptotic factors Bax and Bak. We demonstrated that TG2 is involved in the homeostasis of mitochondria, through the PDI activity, and in the regulation of the mitochondrial pathway of apoptosis, by acting as a BH3-only protein. In fact, lack of TG2 results in the alteration of the mitochondrial physiology, coupled with a reduced response of the organelle towards apoptotic/autophagic stimuli. The comprehension of the molecular mechanisms involving TG2 at mitochondrial level might be of relevance in those neurodegenerative diseases, like Huntington's Disease (HD), showing mitochondrial dysfunction as a central player in the onset and progression of the disease. In addition, mitochondria are the decoying system for cellular stresses, such as DNA damage and ER-stress, which are induced by treatment of cancer cells with chemotherapeutic agents and during metastases formation. The aim of our projects is to assess which could be the effects of TG2 specific inhibition/mutation in relationship with mitochondrial physiology, apoptosis, autophagy, as well as HD and metastases onset and/or progression in animal models for HD and melanoma.
Nicoll, WS, Sacci, JB, Rodolfo, C, Di Giacomo, G, Piacentini, M, Holland, ZJ, Doerig, C, Hollingdale, MR, Lanar, DE (2011) Plasmodium falciparum liver stage antigen-1 is cross-linked by tissue transglutaminase. Malar J 10:14

Rodolfo, C, Ciccosanti, F, Di Giacomo, G, Piacentini, M, Fimia, GM. (2010) Proteomic analysis of mitochondrial dysfunction in neurodegenerative diseases. Expert Rev Proteomics 7 (4):519-42

Malorni, W, Farrace, MG, Matarrese, P, Tinari, A, Ciarlo, L, Mousavi-Shafaei, P, D'Eletto, M, Di Giacomo, G, Melino, G, Palmieri, L, Rodolfo, C, Piacentini, M (2009) The adenine nucleotide translocator 1 acts as a type 2 transglutaminase substrate: implications for mitochondrial-dependent apoptosis. Cell Death Differ. 16(11):1480-92

Di Giacomo, G, Lentini, A, Beninati, S, Piacentini, M, Rodolfo, C (2008) In vivo evaluation of type 2 transglutaminase contribution to the metastasis formation in melanoma. Amino Acids 36(4):717-724

Rodolfo, C, Falasca, L, Di Giacomo, G, Mastroberardino, PG, Piacentini, M (2008) More than two sides of a coin? How to detect the multiple activities of type 2 transglutaminase. Meth Enzymol 442:201-12

Malorni, W, Farrace, MG, Rodolfo, C, Piacentini, M. (2008) Type 2 transglutaminase in neurodegenerative diseases: the mitochondrial connection. Curr Pharm Des 14(3):278-88

Mastroberardino, PG, Farrace, MG, Viti, I, Pavone, F, Fimia, GM, Melino, G, Rodolfo, C, Piacentini, M. (2006) "Tissue" transglutaminase contributes to the formation of disulphide bridges in proteins of mitochondrial respiratory complexes. Biochim. Biophys. Acta 1757(9-10):1357-65

Rodolfo, C, Mormone, E, Matarrese, P, Ciccosanti, F, Farrace, MG, Garofano, E, Piredda, L, Fimia, GM, Malorni, W, Piacentini, M. (2004) Tissue transglutaminase is a multifunctional BH3-only protein. J. Biol. Chem. 279(52):54783-92
No projects are available to students for the current accademic year.