Angela Bachi
e-mail: a.bachi AT hsr.it
affiliation: San Raffaele Scientific Institute
research area(s): Cell Biology, Chemical Biology
Course:
Cell and Molecular Biology
University/Istitution: Università Vita-Salute San Raffaele
University/Istitution: Università Vita-Salute San Raffaele
EDUCATION
1996 PhD in Biochemistry, Mario Negri Institute for Pharmacological Research, Milan, Italy.
1991 Degree in Pharmacy, University of Genova, Italy.
1990 Degree in Pharmaceutical Chemistry & Technology, University of Genova, Italy.
RESEARCH AND PROFESSIONAL EXPERIENCE
1991-1992: Undergraduate student at the Pharmaceutical Analysis & Technology Department of the University of Genoa, Italy.
1994-1996: Graduate student supported by the "Fondazione Lombardia per l'Ambiente". Laboratory of Environmental Pharmacology and Toxicology, Analytical Biochemistry Unit, Mario Negri Institute for Pharmacological Research, Milan, Italy.
1997-1998: Postdoctoral fellow in Matthias Mann group, at the EMBL, Heidelberg, Germany.
1998-1999: Postdoctoral fellow in Matthias Wilm group, at the EMBL Heidelberg, Germany.
2000-2002: Group Leader, Biological Mass Spectrometry Unit, Department of Molecular Biology and Functional Genomics, San Raffaele Scientific Institute, Milan, Italy.
2003- now: Head of Unit, Biomolecular Mass Spectrometry Unit, Division of Genetics & Cell Biology, San Raffaele Scientific Institute, Milan, Italy.
TEACHING EXPERIENCE
- On-tenure Professor in Proteomics, Medical school, Vita-Salute University, HSR.Years: 2002-2004
-On-tenure Professor in Bioinformatics in Genomics and Proteomics, Biotechnology school, Vita-Salute University, HSR. Years: 2004-2008.
- On-tenure professor in Proteomics and Structural Biology, Biotechnology school, Vita-Salute University, HSR. Years: 2009-2011.
Professor at the Proteomics and Mass Spectrometry Course, Vitorchiano, Italy. Years: 2009-2010-2011.
- Professor at the 3rd European summer school "Quantification and Post-translational Modifications of Proteins", august 2009, Brixen, Italy.
1996 PhD in Biochemistry, Mario Negri Institute for Pharmacological Research, Milan, Italy.
1991 Degree in Pharmacy, University of Genova, Italy.
1990 Degree in Pharmaceutical Chemistry & Technology, University of Genova, Italy.
RESEARCH AND PROFESSIONAL EXPERIENCE
1991-1992: Undergraduate student at the Pharmaceutical Analysis & Technology Department of the University of Genoa, Italy.
1994-1996: Graduate student supported by the "Fondazione Lombardia per l'Ambiente". Laboratory of Environmental Pharmacology and Toxicology, Analytical Biochemistry Unit, Mario Negri Institute for Pharmacological Research, Milan, Italy.
1997-1998: Postdoctoral fellow in Matthias Mann group, at the EMBL, Heidelberg, Germany.
1998-1999: Postdoctoral fellow in Matthias Wilm group, at the EMBL Heidelberg, Germany.
2000-2002: Group Leader, Biological Mass Spectrometry Unit, Department of Molecular Biology and Functional Genomics, San Raffaele Scientific Institute, Milan, Italy.
2003- now: Head of Unit, Biomolecular Mass Spectrometry Unit, Division of Genetics & Cell Biology, San Raffaele Scientific Institute, Milan, Italy.
TEACHING EXPERIENCE
- On-tenure Professor in Proteomics, Medical school, Vita-Salute University, HSR.Years: 2002-2004
-On-tenure Professor in Bioinformatics in Genomics and Proteomics, Biotechnology school, Vita-Salute University, HSR. Years: 2004-2008.
- On-tenure professor in Proteomics and Structural Biology, Biotechnology school, Vita-Salute University, HSR. Years: 2009-2011.
Professor at the Proteomics and Mass Spectrometry Course, Vitorchiano, Italy. Years: 2009-2010-2011.
- Professor at the 3rd European summer school "Quantification and Post-translational Modifications of Proteins", august 2009, Brixen, Italy.
Recent technological innovations have driven research in proteomics from single protein characterization to global approaches, aiming at achieving a comprehensive qualitative and quantitative description of complex molecular mechanisms. To achieve this task we are interested in developing and applying new technologies in the fields of mass spectrometry and proteomics. We choose mass spectrometry as the principal analytical tool as this technique is, up to now, the most sensitive and specific tool for protein microanalysis. Our group is mainly interested in the development and application of sensitive and specific methods for protein identification and microcharacterization. In particular, we are developing novel approaches that can be applied to proteome analysis of cells under physiological and pathological states.
Our laboratory has state of the art equipment for protein microanalysis and identification, including a MALDI-TOF, a Nano electrospray Q-TOF and a new LTQ-Orbitrap mass spectrometer. Other analytical tools that we use are chromatography and 2D electrophoresis.
Current research projects focus on:
"" Protein quantification (SILAC and label free)
"" Characterization of post-translationally modified proteins, including phosphoproteins, acetylated and S-nitrosylated proteins
"" Investigation of macromolecular complexes
"" Identification of proteins isolated from different sources
"" Determination and sequencing of the primary structure of proteins
"" protein-protein interactions
Our laboratory has state of the art equipment for protein microanalysis and identification, including a MALDI-TOF, a Nano electrospray Q-TOF and a new LTQ-Orbitrap mass spectrometer. Other analytical tools that we use are chromatography and 2D electrophoresis.
Current research projects focus on:
"" Protein quantification (SILAC and label free)
"" Characterization of post-translationally modified proteins, including phosphoproteins, acetylated and S-nitrosylated proteins
"" Investigation of macromolecular complexes
"" Identification of proteins isolated from different sources
"" Determination and sequencing of the primary structure of proteins
"" protein-protein interactions
- Torta F., Fusi M., Casari C.S., Li Bassi A. Bachi A. Nanostructured TiO2 Thin Films for Phosphoproteomics Studies with MALDI Mass Spectrometry. Methods in Molecular Biology in press.
- La Marca R, Cerri F, Horiuchi K, Bachi A, Feltri ML, Wrabetz L, Blobel CP, Quattrini A, Salzer JL, Taveggia C. TACE (ADAM17) inhibits Schwann cell myelination. Nat Neurosci. 2011 Jun 12;14(7):857-65.
- Torta F. Elviri L. Bachi A. Direct and indirect detection methods for the analysis of S-nitrosylated peptides and proteins. Methods Enzymol. 2010;473:265-80.
- Scielzo C, Bertilaccio MT, Simonetti G, Dagklis A, ten Hacken E, Fazi C, Muzio M, Caiolfa V, Kitamura D, Restuccia U, Bachi A, Rocchi M, Ponzoni M, Ghia P, Caligaris-Cappio F. HS1 has a central role in the trafficking and homing of leukemic B cells. Blood. 2010 Nov 4;116(18):3537-46.
- Matafora V, D"Amato A, Mori S, Blasi F, Bachi A. Proteomic analysis of nucleolar SUMO-1 target proteins upon proteasome inhibition. Molecular &Cellular Proteomics. 2009;8(10):2243-55.
- Torta, F.; Fusi, M.; Casari, C. S.; Bottani, C. E.; Bachi, A., Titanium Dioxide Coated MALDI Plate for On Target Analysis of Phosphopeptides. Journal of proteome research 2009; Vol. 8, pp 1932-1942.
- Bachi A, Bonaldi T. Quantitative proteomics as a new piece of the systems biology puzzle. J. Proteomics. 2008 ;71(3):357-67
- La Marca R, Cerri F, Horiuchi K, Bachi A, Feltri ML, Wrabetz L, Blobel CP, Quattrini A, Salzer JL, Taveggia C. TACE (ADAM17) inhibits Schwann cell myelination. Nat Neurosci. 2011 Jun 12;14(7):857-65.
- Torta F. Elviri L. Bachi A. Direct and indirect detection methods for the analysis of S-nitrosylated peptides and proteins. Methods Enzymol. 2010;473:265-80.
- Scielzo C, Bertilaccio MT, Simonetti G, Dagklis A, ten Hacken E, Fazi C, Muzio M, Caiolfa V, Kitamura D, Restuccia U, Bachi A, Rocchi M, Ponzoni M, Ghia P, Caligaris-Cappio F. HS1 has a central role in the trafficking and homing of leukemic B cells. Blood. 2010 Nov 4;116(18):3537-46.
- Matafora V, D"Amato A, Mori S, Blasi F, Bachi A. Proteomic analysis of nucleolar SUMO-1 target proteins upon proteasome inhibition. Molecular &Cellular Proteomics. 2009;8(10):2243-55.
- Torta, F.; Fusi, M.; Casari, C. S.; Bottani, C. E.; Bachi, A., Titanium Dioxide Coated MALDI Plate for On Target Analysis of Phosphopeptides. Journal of proteome research 2009; Vol. 8, pp 1932-1942.
- Bachi A, Bonaldi T. Quantitative proteomics as a new piece of the systems biology puzzle. J. Proteomics. 2008 ;71(3):357-67
Project Title:
Dissecting the involment of Sp140 in leukocytes and in chronic lymphocytic leukemia (CLL)
Sp140, a leukocyte-specific protein member of the Sp100 family, localizes to promyelocytic leukemia nuclear bodies1. Sp140 is expressed in mature B cells and plasma cell lines; it plays a role in immune response to HIV-1, is an autoantigen in primary biliary cirrhosis and most importantly, polymorphisms in the gene were associated with risk of chronic lymphocytic leukemia (CLL), the most common adult leukemia in the western world2. Despite its involvement in human pathologies its physiological role and the molecular mechanism dictating its function are still unknown. Sp140 contains a tandem PHD-Bromo-domain which is known to work as epigenetic reader of histone tails recruiting transcription factors and nucleosome-associated complexes to chromatin, and as E3 ligase in intramolecular sumoylation reactions. We have recently found that Sp140 can indeed undergo sumoylation.The main goal of this project is to gain insights into the structure function-relationship of SP140 as a basis to clarify its molecular role in the pathogenesis of human malignancies and in particular of CLL. In particular, in order to understand Sp140 function, we will identify Sp140-associated proteins through a proteomic approach3 taking advantage of a large collection of CLL patient samples available at our institution, we will investigate how sumoylation may affect its function and we will characterization Sp140 as epigenetic reader in quantitative GST-Pull down.