Andrea Berti

Biography

The professor. Andrea Berti graduated in Biological Sciences in 1973. After obtaining a research grant, in 1981 he became a researcher at the Department of Biochemical Sciences at the University of Florence. In 1988 he won a post of Associate Professor of Enzymology at the Faculty of Medicine. In 2001 he became Professor of Extraordinary Biochemistry at the University of Florence. Currently, as an Ordinary Professor of the Faculty of Agriculture at the University of Florence, she teaches Biochemistry, Applied Enzymology and Nutrition Physiology in the Degree courses in Food Science and Technology and in Food Quality. The scientific activity of prof. Berti focuses on studying the relationship between protein structure and function and in particular enzymes such as phosphonoidrolases. These studies were conducted with classical biochemistry techniques, such as sequence determination, and molecular biology methodologies. Purified acylphosphatases have been sequenced by various animal tissues. Some aspects of their biological role have been studied and clarified. A major effort has been made in studies on the expression of low molecular weight phosphatase phosphatase in cells transformed by various oncogenes. With the direct site mutagenesis, the role of four cysteines in the enzyme sequence was clarified. The regulation mechanism by the SRC kinase has been demonstrated and data regarding its implication in the mechanisms involved in cell motility and adhesion have recently been obtained. More recently, prof. Berti studied some aspects of cell death caused by exposure to protein amyloid aggregates. In particular, some of the motivations that point the cells towards apoptosis or necrosis have been highlighted. Prof. Bertti has visited some laboratories abroad and has been a speaker at congresses. Main research lines: Study of phosphatase phosphatase role in hematopoietic cells. Study and control the enzymatic activities involved in the production of olive oil. Studies on the toxicity of protein amyloid aggregates.

Research Interest

Biochemistry