Mauro Torti
e-mail: mauro.torti AT unipv.it
affiliation: Università di Pavia
research area(s): Cell Biology, Chemical Biology
Course:
Biomolecular Sciences and Biotechnology
University/Istitution: Istituto Universitario di Studi Superiori, Pavia
University/Istitution: Istituto Universitario di Studi Superiori, Pavia
ACADEMIC POSITION
Full Professor of Biochemistry, University of Pavia
EDUCATION
1986: Degree in Biology, University of Pavia, Italy
1990: Ph.D in Biochemistry, University of Pavia, Italy
1991-1992: Post-doctoral fellow. Division Cell Biology , Burroughs Wellcome
Co., Research Triangle Park, NC, USA.
1996: Visiting scientist, Case Western Reserve University, Cleveland OH,
USA
1997: Specialisation in Clinical Biochemistry, University of Pavia, Italy
Full Professor of Biochemistry, University of Pavia
EDUCATION
1986: Degree in Biology, University of Pavia, Italy
1990: Ph.D in Biochemistry, University of Pavia, Italy
1991-1992: Post-doctoral fellow. Division Cell Biology , Burroughs Wellcome
Co., Research Triangle Park, NC, USA.
1996: Visiting scientist, Case Western Reserve University, Cleveland OH,
USA
1997: Specialisation in Clinical Biochemistry, University of Pavia, Italy
Research activity encompasses fundamental aspects of transmembrane signaling in human platelets, including small GTP-binding proteins, tyrosine kinases and adhesion receptors.
Specific area of interest include:
- Mechanisms of blood platelets aggregation
- Signal transduction through platelet integrins alpha2beta1 and alphaIIbbeta3
- Role of the purinergic receptor P2Y12 in regulation of platelet function
- Mechanisms regulating inositol phospholipids metabolizing enzymes
phospholipase C and phosphatidylinositol 3-kinase
- Protein-tyrosine kinases and cellular function
- Function and regulation of the ras-related small GTPases Rap1 and Rap2
- Analysis of the biochemical abnormalities of platelets in familiar
macrothrombocytopenic syndromes
- metabolism and funcion of amyloid precursor protein: blood platelets as a
cellaulr model for neurodegenerative disorders
Specific area of interest include:
- Mechanisms of blood platelets aggregation
- Signal transduction through platelet integrins alpha2beta1 and alphaIIbbeta3
- Role of the purinergic receptor P2Y12 in regulation of platelet function
- Mechanisms regulating inositol phospholipids metabolizing enzymes
phospholipase C and phosphatidylinositol 3-kinase
- Protein-tyrosine kinases and cellular function
- Function and regulation of the ras-related small GTPases Rap1 and Rap2
- Analysis of the biochemical abnormalities of platelets in familiar
macrothrombocytopenic syndromes
- metabolism and funcion of amyloid precursor protein: blood platelets as a
cellaulr model for neurodegenerative disorders
Lova P, Guidetti GF, Canobbio I, Catricalà S, Balduini C, Torti M.
Epinephrine-mediated protein kinase C and RAP1b activation requires the co-stimulation of Gz-, Gq-, and Gi-coupled receptors.
Thromb Haemost. 2011; 105: 479-86.
Canobbio I, Catricalà S, Balduini C, Torti M.
Calmodulin regulates the non-amyloidogenic metabolism of amyloid precursor protein in platelets.
Biochim Biophys Acta. 2011; 1813: 500-6.
Lova P, Canobbio I, Guidetti GF, Balduini C, Torti M.
Thrombin induces platelet activation in the absence of functional protease activated receptors 1 and 4 and glycoprotein Ib-IX-V.
Cell Signal. 2010; 22: 1681-7.
Canobbio I, Stefanini L, Cipolla L, Ciraolo E, Gruppi C, Balduini C, Hirsch E, Torti M.
Genetic evidence for a predominant role of PI3Kbeta catalytic activity in ITAM- and integrin-mediated signaling in platelets.
Blood. 2009; 114:2193-6.
Guidetti GF, Bernardi B, Consonni A, Rizzo P, Gruppi C, Balduini C, Torti M.
Integrin alpha2beta1 induces phosphorylation-dependent and phosphorylation-independent activation of phospholipase C2 in platelets: role of Src kinase and Rac GTPase.
J Thromb Haemost. 2009; 7: 1200-6
Epinephrine-mediated protein kinase C and RAP1b activation requires the co-stimulation of Gz-, Gq-, and Gi-coupled receptors.
Thromb Haemost. 2011; 105: 479-86.
Canobbio I, Catricalà S, Balduini C, Torti M.
Calmodulin regulates the non-amyloidogenic metabolism of amyloid precursor protein in platelets.
Biochim Biophys Acta. 2011; 1813: 500-6.
Lova P, Canobbio I, Guidetti GF, Balduini C, Torti M.
Thrombin induces platelet activation in the absence of functional protease activated receptors 1 and 4 and glycoprotein Ib-IX-V.
Cell Signal. 2010; 22: 1681-7.
Canobbio I, Stefanini L, Cipolla L, Ciraolo E, Gruppi C, Balduini C, Hirsch E, Torti M.
Genetic evidence for a predominant role of PI3Kbeta catalytic activity in ITAM- and integrin-mediated signaling in platelets.
Blood. 2009; 114:2193-6.
Guidetti GF, Bernardi B, Consonni A, Rizzo P, Gruppi C, Balduini C, Torti M.
Integrin alpha2beta1 induces phosphorylation-dependent and phosphorylation-independent activation of phospholipase C2 in platelets: role of Src kinase and Rac GTPase.
J Thromb Haemost. 2009; 7: 1200-6
Project Title:
The research project is aimed to define the role the focal adhesion kinase Pyk2 in platelet function and thrombus formation, in order to verify whether this protein might represent a potential target for anti-platelet treatmentsin cardiovascular diseases. We will take advantage from the analysis of a recently generated transgenic mice strain lacking Pyk2. The project proposes an extensive ex vivo functional analysis on isolated platelets from Pyk2 KO mice, in order to clarify the role of this kinase in integrin-mediated platelet adhesion, as well as in agonist-induced platelet secretion and aggregation, and a comprehensive investigation of the activated intracellular signaling pathways to unravel the molecular dynamics of Pyk2 involvement in platelet functionality.
Role of the tyrosine kinase Pyk2 in platelet activation
The research project is aimed to define the role the focal adhesion kinase Pyk2 in platelet function and thrombus formation, in order to verify whether this protein might represent a potential target for anti-platelet treatmentsin cardiovascular diseases. We will take advantage from the analysis of a recently generated transgenic mice strain lacking Pyk2. The project proposes an extensive ex vivo functional analysis on isolated platelets from Pyk2 KO mice, in order to clarify the role of this kinase in integrin-mediated platelet adhesion, as well as in agonist-induced platelet secretion and aggregation, and a comprehensive investigation of the activated intracellular signaling pathways to unravel the molecular dynamics of Pyk2 involvement in platelet functionality.