Dr Carlo Vascotto

After the BS in Biology, obtained in 2001 at the University of Trieste, Trieste (Italy), Carlo Vascotto started the PhD course in Biomedical and Biotechnological Sciences at the University of Udine under the supervision of Prof. Gianluca Tell. During the PhD, he worked as a visiting student in the laboratory of Prof. Veronica Van Heyningen in Edinburgh (UK), at the MRC, Human Genetic Unit (2004) and later in the laboratory of Prof. Sankar Mitra in Galveston, TX (USA), at the University of Texas Medical Branch (2006). In 2010, he received a Fulbright Research fellowship and joined the laboratory of Prof. Mark Kelley at the Department of Pediatrics, Indiana University, Indianapolis, IN (USA). Since 2011, he has been Assistant Professor of Molecular Biology at the University of Udine.

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As a PhD student and later as a post-doc, his research interests focused on the role of reactive oxygen species (ROS) in modulating cellular activity. ROS are considered highly toxic by-products of oxygen metabolism with deleterious biological effects. However, recent evidence shows that ROS act as signal transducing molecules that play a significant role in the activation of transcription factors leading to gene expression under both physiological and pathological conditions. In this context, Dr. Vascotto used proteomic approaches to characterize molecular signaling pathways involved in the response to oxidative stress in human cells, particularly in hepatocytes.

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During the last seven years, his research interests have focused on the study of DNA damage, the mechanisms of repair in mammalian cells and, in particular, the role of the major human Apurinc/apirimidinic endonuclease (APE1) under physiological and pathological conditions. APE1 localizes in the nucleus, accumulates into nucleoli, but is also present within the mitochondrial matrix where mtDNA resides. Dr. Vascotto's laboratory demonstrated the interaction of APE1 with the Mitochondrial intermembrane space import and assembly protein 40 (Mia40) and showed the correlation between the expression of Mia40 and APE1 with the stability of mtDNA during tumorigenic processes in hepatocellular carcinoma. He also identified the inner membrane translocase responsible for the IMS/matrix translocation of APE1 and how oxidative stress determines rapid matrix internalization of APE1 to maintain mtDNA stability. The final insight into the characterization of the mitochondrial APE1 form is its involvement in the degradation of damaged, nonfunctional mitochondrial mRNAs.