Institute of Protein Biochemistry, CNR.

Via P. Castellino, 111 - 80131 Napoli

2013-2014 IBP Seminar Series

CNR Conference Room

Friday, November 22th, 2013 at 14:30

Dr. Emilia Caputo

Institute of Genetics and Biophysics 'A. Buzzati-Traverso', Naples

"c-Myc Modulation: a Key Mechanism in Melanoma Drug Resistance "

Host: Dr. Maria Rosaria Coscia

Tel. 081-6132556; e-mail: mr.coscia@ibp.cnr.it

Dr. Caputo`s research has always been focused on the study of cancer, starting from the identification of tumour biomarkers to their characterization and to their functional role investigation. She contributed to the understanding of the biochemical role of a breast cancer marker, known as gp17/GCDFP-15, by using approaches such as molecular biology, biochemistry, bio-computing and protein engineering. After almost twenty years of studies on GCDFP-15/gp17, Dr. Caputo demonstrated that it is a protease exhibiting structural properties relating it to the aspartyl proteinase superfamily.
Her expertise in biochemistry and enzymology allowed the characterization of Rhizobium etli auxotrophic mutant strains. She contributed to the biochemical characterization of a complex, consisting of the Aes enzyme with an E. coli 50-kDa polypeptide. She contributed to identify the 50-kDa polypeptide as a-galactosidase, suggesting a potential role of Aes in the regulation of carbohydrate metabolism in E. coli, never described previously.
Her expertise in protein analysis using ProteinChip Array technology contributed to the development of methods for the identification and characterization of different proteins. She developed various protein chemistry procedures that can be applied to the identification of proteins directly on the surface of ProteinChip arrays, such as on-chip trypsin digestion and subsequent micro-sequencing of the resulting peptides using a ProteinChip Interface coupled to the tandem MS/MS QStar instrument . She also demonstrated C-terminal enzymatic sequencing on peptides by a combination of direct on-chip carboxypeptidase Y (CPD Y) digestion with SELDI-TOF mass analysis of the resulting peptide ladders. The combination of the SELDI-TOF MS sensitivity with no sample loss upon moving from digestion to analysis allowed the C-terminal sequencing of very few picomoles of total peptide.
Recently, her approach in the study of molecular properties of cancer through a combination of computational, gene and protein analysis allowed to identify potential biomarkers and/or molecular pathways associated to melanoma that could be exploited for the better understanding of the molecular mechanisms underlining melanoma onset and progression as well as the development of diagnostic and therapeutic tools.
Her current work spans a spectrum from basic science (mechanisms of melanoma development and metastasis) to translational (melanoma pharmaco-resistance and designing of innovative therapeutic strategies) to clinical research (database construction).