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RESPONSABILE DELLA U. O. |
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Cognome e Nome |
Zolla Lello
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Qualifica |
Full Professor |
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Facoltà |
MM. FF. NN. Sciences |
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Dipartimento |
Environmental Sciences (DISA) |
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Settore Scientifico Disciplinare |
BIO/011 |
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E-mail |
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PERSONALE STRUTTURATO |
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Cognome e Nome |
Timperio Anna Maria |
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Qualifica |
Researcher
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Dipartimento |
Environmental Sciences (DISA) |
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Ente di appartenenza |
Tuscia University
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Cognome e Nome |
Vinciguerra Vittorio
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Qualifica |
Researcher
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Dipartimento |
Environmental Sciences (DISA) |
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Ente di appartenenza |
Tuscia University
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Cognome e Nome |
Zolla Lello
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Qualifica |
Full Professor |
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Dipartimento |
Environmental Sciences (DISA) |
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Ente di appartenenza |
Tuscia University
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PERSONALE NON STRUTTURATO |
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Cognome e Nome |
Ciambella Corrado
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Qualifica |
Post-Doc
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Dipartimento |
Environmental Sciences (DISA) |
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Ente di appartenenza |
Tuscia University
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Cognome e Nome |
D’Amici Giammaria |
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Qualifica |
PhD student |
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Dipartimento |
Environmental Sciences (DISA) |
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Ente di appartenenza |
Tuscia University
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Cognome e Nome |
Faggioni Marco |
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Qualifica |
PhD Student
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Dipartimento |
Environmental Sciences (DISA) |
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Ente di appartenenza |
Tuscia University
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Cognome e Nome |
Latini Arianna |
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Qualifica |
PhD Student |
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Dipartimento |
Environmental Sciences (DISA) |
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Ente di appartenenza |
Tuscia University
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Cognome e Nome |
Rinalducci Sara |
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Qualifica |
Post-Doc |
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Dipartimento |
Environmental Sciences (DISA) |
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Ente di appartenenza |
Tuscia University
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Cognome e Nome |
Rosetto Francesca
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Qualifica |
Fellow Ship
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Dipartimento |
Environmental Sciences (DISA) |
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Ente di appartenenza |
Tuscia University
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LINEE DI RICERCA |
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Nowadays mass spectrometry is a powerful tool used to study, by a proteomic approach, the protein content and its function in different biological systems. Our investigations concern the study of cell proteins, in both animal and plant kingdom, that could be over- or under-expressed upon stress conditions or after chemical and therapeutic treatments
1. Plant systems
1.1 Proteomic of plants, algae and cyanobacteria under environmental stress conditions Proteomic mapping of the photosynthetic apparatus from plants, algae and cyanobacteria allows us to check if any change in the environmental conditions can result as a consequence of the adaptation. Thus, comparing untreated organism with one grown in stress conditions (water stress, light stress, heavy metals stress, temperature stress) it is possible to identify which are the main proteins involved and how the organism could be genetically modified; this gives the opportunity to obtain resistant organisms, hence to improve the productivity of determined crops.
1.2 Proteomic of genetically modified organisms (GMO): Three Zea mays lines (MON-810, Bt11, Bt176) have been developed by specific genetic modifications to become resistant to European corn borer (ECB): Ostrinia nubilalis. In this case the main aim of the research is to identify which are the changes of protein expression due to new gene insertion.
2 Animal systems
2.1 Proteomic of different pancreatic tumoral cell strains after drug treatment
Pancreatic tumoral cell strains have been treated (separately or in combination) with drugs acting on the tumor epigenetic events (e.g. histone deacetylation, DNA hypermethylation). The proteomic analysis is focused on the identification of differential expressed proteins after drugs treatment. The study of activation/repression levels of the involved proteins results in an increased knowledge of growth processes and cell apoptotic response.
2.2 Proteomic of erythrocytes membranes and cell aging
These studies are focused on the characterization of proteic pattern changes following the oxidative events due to cell aging during the common blood storage.
2.3 Proteomic of mammary glands of different cows
The aim of this differential proteomic is the identification of specific proteins that could be potentially responsible of the biodiversity of cow races used for milk production. |
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TECNOLOGIE IN POSSESSO DELL'U. O. |
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1. Protein separation by 2-D electrophoresis and by high performance liquid chromatography.
2. Protein identification by PMF (Peptide Mass Fingerprinting), Sequence-Tag and IMM (Intact Molecular Mass).
3. DNA fragment separation and SNPs identification by mass-spectrometry.
4. Oxigen Singlet determination by EPR.
5. Membrane Proteins separation and identification.
6. Monolith capillary column for nano-HPLC separation.
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STRUMENTAZIONE |
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Denominazione
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Struttura ove la strumentazione è allocata
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Responsabile della strumentazione
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Mass Spectrometer micro-TOF-Q Bruker
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Proteomic and Genomic Lab. (DISA)
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Prof. Zolla
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Mass Spectrometer HCT plus Bruker
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Proteomic and Genomic Lab. (DISA)
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Prof. Zolla
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Mass Spectrometer Esquire 3000 plus Bruker
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Proteomic and Genomic Lab. (DISA)
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Prof. Zolla
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Mass spectrometer MALDI-TOF Biflex III Bruker
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Proteomic and Genomic Lab. (DISA)
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Prof. Zolla
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ESP 300 spectrometer Bruker
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Proteomic and Genomic Lab. (DISA)
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Prof. Zolla
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Two Ultracentrifuges (Beckman and Kontron)
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Proteomic and Genomic Lab. (DISA)
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Prof. Zolla
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Two HPLC (Beckman Gold System and Pelkin Elmer)
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Proteomic and Genomic Lab. (DISA)
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Prof. Zolla
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Two nano-HPLC Dionex
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Proteomic and Genomic Lab. (DISA)
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Prof. Zolla
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Spectrophotometer UV-Vis Cary 4 Varian
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Proteomic and Genomic Lab. (DISA)
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Prof. Zolla
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Etan Dalt Six 2D-gel system Amersham Biosciences
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Proteomic and Genomic Lab. (DISA)
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Prof. Zolla
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PUBBLICAZIONI |
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1. Rinalducci S., Campostrini N., Antonioli P., Righetti P. G., Roepstorff P., Zolla L. Formation of truncated proteins and high-molecular-mass aggregates upon soft illumination of photosynthetic proteins. J Proteome Res. 2005; 4:2327-37
2. Timperio A. M., Zolla L. Investigation of the lateral light-induced migration of photosystem II light-harvesting proteins by nano-high performance liquid chromatography electrospray ionization mass spectrometry. J Biol Chem. 2005; 280: 28858-66.
3. Gil-Augusti M.T., Campostrini N., Zolla L., Ciambella C., Invernizzi C., Righetti P.G. Two-dimensional mapping as a tool for classification of green coffee bean species. Proteomics. 2005; 5: 710-8.
4. Monacelli B., Pasqua G., Botta B., Vinciguerra V., Gacs-Baitz E., Delle Monache G. "Abietane Diterpenoids from callus cultures of taxus bacata". Planta Med. 2002; 68: 764-766.
5. Zolla L., Rinalducci S. Involvement of active oxygen species in degradation of light-harvesting proteins under light stresses. Biochemistry. 2002; 48: 14391-402
6. Huber C.G., Timperio A. M., Zolla L. Isoforms of photosystem II antenna proteins in different plant species revealed by liquid chromatography-electrospray ionization mass spectrometry. J Biol Chem. 2001; 276: 45755-61.
7. Zolla L., Rinalducci S., Timperio A. M., Huber C.G., Righetti P.G. Intact mass measurements for unequivocal identification of hydrophobic photosynthetic photosystems I and II antenna proteins. Electrophoresis. 2004; 25:1353-66.
8. Huber C.G., Walker W., Timperio A. M., Troiani S., Porceddu A, Zolla L. Multidimensional proteomic analysis of photosynthetic membrane proteins by liquid extraction-ultracentrifugation-liquid chromatography-mass spectrometry. Proteomics. 2004; 4:3909-20.
9. Walker W., Timperio A. M., Zolla L., Huber C. G. Characterization of a variant of the spinach PSII type I light-harvesting protein using kinetically controlled digestion and RP-HPLC-ESI-MS. Anal Chem. 2003; 75:6775-80.
10. Zolla L., Rinalducci S., Timperio A. M., Huber C. G. Proteomics of light-harvesting proteins in different plant species. Analysis and comparison by liquid chromatography-electrospray ionization mass spectrometry. Photosystem I. Plant Physiol. 2002;130:1938-50.
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DOTTORATI DI RICERCA |
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| Componente U.O. |
Dottorato di Ricerca |
Coordinatore |
Sede |
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Zolla Lello
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Genetics and Molecular Biology
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Prof. Prantera Giorgio Dept. Environ. Sciences
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University
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Timperio Anna Maria
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Genetics and Molecular Biology
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Prof. Prantera Giorgio Dept. Environ. Sciences
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University
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CONGRESSI C.I.B. |
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| Congressi |
Partecipazione |
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CNB4
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CNB5
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CNB6
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CNB7
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CNB8
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| CNB10 |
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