Ordinario di Chimica Biologica
Prof. Piero Pucci got his degree in Chemistry at the University of Napoli in 1978 was Assistant Professor of Biochemistry first, then Associate Professor of Biochemistry and is now Full Professor of Biochemistry at the Department of Chemical Sciences, University Federico II of Napoli. Prof. Pucci has been Post doctoral fellow and Visiting Associate at the Biochemical Department of the Imperial College of Science, Technology and Medicine in London, U. K.
Prof. Pucci is Member of the Board of Directors of the Italian Proteomic Foundation and Member of the Director Board and the Executive Comittee of the INBB Consortium. He was a former Member of the World Council of the Human Proteome Organization (HUPO), President of the Italian Human Proteome Organization (IHUPO), Member of the Council of the Italian Proteomic Association (ItPA) and Coordinator of the Protein Group of the Italian Society of Biochemistry and Molecular Biology (SIBBM). At present, Prof. Pucci is Coordinator of the Technological Facilities and Responsible of both the Proteomic Laboratory and the Proteomic Facility at CEINGE Biotecnologie Avanzate.
Prof. Pucci delivered lectures to national and international Meetings, published more than 260 refereed papers on international journals with a H-Factor of 46 and is Consultant and Collaborator of several public and private Enterprises in the biotechnological and pharmaceutical field
Research at the CEINGE Proteomic Laboratory focuses on two lines of interest, the definition of the molecular mechanisms underlying complex physio-pathological processes and the specific detection and quantification of protein targets within biological fluids and/or entire cellular extract.
Many processes in the cell are fulfilled through the rapid and transient association of proteins within large functional complexes. Unraveling molecular mechanisms in physiological or pathological conditions thus depends on the identification of the interacting protein partners. Proteomic approaches can provide a key contribution to the investigation of cellular mechanisms either by isolating functional complexes and identifying individual protein components or by measuring up-and down-regulated protein levels in different cellular conditions.
The development of highly specific analyses for the identification and quantification of protein targets is based on advanced tandem mass spectrometric techniques in Multiple Reaction Monitoring (MRM) mode. The entire procedure is based on the selection of specific peptides belonging to each protein of interest on the basis of their molecular ion and their most intense fragments. This information is used to set up a very specific and sensitive identification method based on monitoring the specific transitions from the molecular ion to each fragment ions during LC-MS/MS experiments. Each set of peptides, defined by their specific MRM transitions, can only be associated to a single, individual protein leading to unambiguous identification and quantitation of the desired target. Moreover, the capability of the MRM proteomic methods to monitor multiple peptide transitions specific for each protein in parallel allows us to quantitate several candidate proteins in a single analysis. These approaches will constitute an effective alternative to ELISAs or immunofluorescent assays for protein targets identification purposes.
- Investigation of cellular mechanisms involving specific protein targets
- Differential Proteomics investigation of brain phosphoproteome
- Identification of splicing variant proteins involved in oncologic mechanisms
Prof. Maria Monti, Prof. Associato diChimica Biologica
Prof. Angela Amoresano, Prof. Ordinario di Chimica Analitica
Prof. Angela Duilio, Prof. Associato di Biologia Molecolare
Dr.ssa Flora Cozzolino, Ricercatore a Tempo Determinato (RTD-A)
Dr.ssa Gabriella Pinto, Ricercatore a Tempo Determinato (RTD-A)
Dr.ssa Angela Di Somma, Dottoranda in Scienze Chimiche
Dr.ssa Vittoria Monaco, Contrattista
Dr.ssa Arianna Cirillo, Conmtrattista
Dr.ssa Carolina Canè, Contrattista
1. G. D'Angelo, T. Uemura, C.C. Chuang, E. Polishchuk, M. Santoro, H. Ohvo-Rekilä, T. Sato, G. Di Tullio, A. Varriale, S. D'Auria, T. Daniele, F. Capuani, L. Johannes, P. Mattjus, M. Monti, P. Pucci, R.L. Williams, J.E. Burke, F.M. Platt, A. Harada and M.A. De Matteis. Vesicular and non-vesicular transport feed distinct glycosylation pathways in the Golgi. Nature. 501 (2013) 116-120.
2. G. Chesi, R.N. Hegde, S. Iacobacci, M. Concilli, S. Parashuraman, B.P. Festa, E.V. Polishchuk, G. Di Tullio, A. Carissimo, S. Montefusco, D. Canetti, M. Monti, A. Amoresano, P. Pucci, B. van de Sluis, S. Lutsenko, A. Luini and R.S. Polishchuk. Identification of p38 MAPK and JNK as new targets for correction of Wilson disease-causing ATP7B mutants. Hepatology 63 (2016) 1842-1859.
3. M. Zollo, M. Ahmed, V. Ferrucci, V. Salpietro, F. Asadzadeh, M. Carotenuto, R. Maroofian, A. Al-Amri, R. Singh, I. Scognamiglio, M. Mojarrad, L. Musella, A. Duilio, A. Di Somma, E. Karaca, A. Rajab, A. Al-Khayat, T.M. Mohapatra, A. Eslahi, F. Ashrafzadeh, L.E. Rawlins, R. Prasad, R. Gupta, P. Kumari, M Srivastava, F. Cozzolino, S.K. Rai, M. Monti, G.V. Harlalka, M.A. Simpson, P. Rich, F. Al-Salmi, M.A. Patton, B.A. Chioza, S. Efthymiou, F. Granata, G. Di Rosa, S. Wiethoff, E. Borgione, C. Scuderi, K. Mankad, M.G. Hanna, P. Pucci, H. Houlden, J.R. Lupski, A.H. Crosby and E.L. Baple. PRUNE is crucial for normal brain development and mutated in microcephaly with neurodevelopmental impairment. Brain 140 (2017) 940-952.
4. A. Varone, S. Mariggiò, M. Patheja, V. Maione, A. Varriale, M. Vessichelli, D. Spano, F. Formiggini, M. Lo Monte, N. Brancati, M. Frucci, P. Del Vecchio, S. D’Auria, A. Flagiello, C. Iannuzzi, A. Luini, P. Pucci, L. Banci, C. Valente and D. Corda. A signalling cascade involving receptoractivated phospholipase A2, glycerophosphoinositol 4-phosphate, Shp1 and Src in the activation of cell motility. Cell Commun Signal 17 (2019) 20.
5. F. Zappa, C. Wilson, G. Di Tullio, M. Santoro, P. Pucci, M. Monti, D. D'Amico, S. Pisonero-Vaquero, R. De Cegli, A. Romano, M.A. Saleem, E. Polishchuk, M. Failli, L. Giaquinto, M.A. De Matteis. The TRAPP complex mediates secretion arrest induced by stress granule assembly. EMBO J. (2019) doi: 10.15252/embj.2019101704.