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Luisa Franco

Chief Technician

Facility

Neurofacility

Contacts

Via Moerego 30
+39 010 2896 432
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About

Luisa Franco graduates in Biological Science at the University of Genoa discussing the thesis "Heterogeneity of erythrocytic human G proteins" with the grade of "110/110 cum laude" (1990). She achieve her PhD in "Cellular Biotechnology applied to Pharmacology and Molecular Biotechnology applied to Biomedicine" at the University of Milan, discussing the thesis "Correlation between extracellular production of Cyclic ADP-ribose and its intracellular functions" (1995). As a post doc fellow at the University of Minnesota in the Physiology Department she focused her research on calcium homeostasis following the project:"Functional characterization of ADP-ribosyl cyclase and of its product cADPR in the calcium homeostasis" (1996-97). She continued her studies on calcium signalling as post-doc at the University of Genoa, Department of experimental medicine, Section of Biochemistry, pursuing the following research projects: i) NAD+ and cADPR transport through cellular plasmamembrane; ii) role of cADPR in the calcium homeostasis and contraction of bovine tracheal smooth muscle (1997-99). At the University Federico II of Naples, Centre of Biocrystallography, Chemistry Department, she focused her studies on the purification of the protein connexin 43 and characterization of its role in NAD+ transport through the plasmamembrane (1999-2001). As senior researcher at the scientific direction of the G.Gaslini Institute, Genoa (2001-2004) she deepened the role of Cyclic ADP-ribose as intracellular calcium mobilizing messenger in different cell types from fibroblasts to glia cells. In 2005 she attends to the Master in Scientific Communication of the University of Milan, department of Pharmacology,and starts her collaborations with the journal "Tempo Medico" as free lance journalist through the Agency for science communication Zadig in Milan; she also collaborates with press office of the "Festival della scienza" in Genova (2005-06). Since 2006 shecollaborates with the Fondazione Istituto Italiano di Tecnologia in Genoa to planning, construction and preparation of the laboratories of the Department of Neuroscience and Brain Technologies (2000 m), acquisition of all the instruments through European tenders, coordination of the scientific activity, grant applications, collaborations with other research institutes and supervision of administrative activities. Since 2011, she is at IIT as manager of the Neuro-facilty Unit of the Neuroscience and Brain Technologies Department.

 

Selected Publications

  1. Abscisic acid activates the murine microglial cell line N9 through the second messenger cyclic ADP-ribose.Bodrato N, Franco L, Fresia C, Guida L, Usai C, Salis A, Moreschi I, Ferraris C, Verderio C, Basile G, Bruzzone S, Scarfì S, De Flora A, Zocchi E.  J Biol Chem.284; 14777-87, 20092 
  2. Cyclic ADP-ribose is a second messenger in the lipopolysaccharide-stimulated activation of murine N9 microglial cell line. Luisa Franco, Nicoletta Bodrato,  Iliana Moreschi,  Cesare Usai, Santina Bruzzone, Sonia Scarfì, Elena Zocchi and Antonio De Flora. Journal Of Neurochemistry,99,165-76, 2006.
  3. 3. ADP-ribosyl cyclases generate two unusual adenite homodinucleotides with cytotoxic activity on mammalian cells. Basile, G., Taglialatela-Scafati, O., Da monte, G., Amirotti,A., Buzzone, S., Guida, L., Franco, L.,  Usai, C., Fattorusso, E., De Flora, A. and Zocchi, E..Proc. Natl. Acad. Sci. U.S.A. 102, 14509-14514, 2005.
  4. Concentrative uptake of cyclic ADP-ribose generated by BST-1+ stroma stimulates proliferation of human hematopoietic progenitors. Podestà, M., Benvenuto, F., Pitto, A., Figari, O., Bacigalupo, A., Bruzzone, S., Guida, L., Franco, L., Paleari, L., Bodrato, N., Usai, C., De Flora, A. and  Zocchi E. J. Biol. Chem. 280, 5343-9, 2005
  5. Autocrine and Paracrine Calcium signaling by the CD38/NAD+ /cyclic ADP-ribose system. DeFlora, A., Zocchi,E., Guida, L., Franco,L. and Bruzzone, S. Ann.N.Y. Acad. Sci.1028, 1-16, 2004.
  6. Concentrative influx of functionally active cyclic ADP-ribose in Dimethylsulfoxide-differentiated HL-60 cells. Guida,L., Franco,L., Bruzzone, S., Sturla,L., Zocchi,E., Basile,G., Usai, C. and De Flora A. J Biol Chem. 279,22066-75, 2004.
  7. Cyclic ADP-ribose generation by CD38 improves human hemopoietic stem cell engraftment into NOD/SCID mice Marina Podestà, Anna Pitto, Osvaldo Figari, Andrea Bacigalupo, Santina Bruzzone, Lucrezia Guida, Luisa Franco, Antonio De Flora and Elena Zocchi. FASEB J., 17, 310-312, 2002.
  8. Equilibrative and concentrative nucleoside transporters mediate influx of extracellular cyclic ADP-ribose into 3T3 murine fibroblasts. Guida, L., Bruzzone, S., Sturla, S., Franco, L., Zocchi, E. and De Flora, A. J. Biol. Chem. 277, 47097-47105, 2002. 
  9. The temperature-signaling cascade in sponges involves a heat gated cation channel, abscisic acid, and cyclic ADP-ribose. Zocchi,E., Carapaneto, A., Cerrano, C., Bavestrello , G., Giovine, M., Bruzzone, S., Guida, L., Franco, L., and Usai, C. Proc. Natl, Acad. Sci. USA, 98, 14859-14864, 2001
  10. A self-restricted CD38-connexin 43 cross-talk affects NAD+ and Cyclic ADP-ribose metabolism and regulates intracellular calcium in 3T3 fibroblasts . Bruzzone, S., Franco, L., Guida, L., Zocchi, E., Contini, P., Bisso, A., Usai, C. and De Flora, A. J.Biol. Chem., 276, 48300-48308, 2001.
  11. Extracellular NAD+ induces calcium signaling and apoptosis in human osteoblastic cells. Romanello, M., Padoan, M., Franco, L., Veronesi., V., Moro, L. and D’andrea, P. Biochem. Biophys. Res. Commun.285, 1226-1231, 2001.
  12. Paracrine roles of NAD+ and Cyclic ADP-ribose in increasing intracellular calcium and enhancing cell proliferation of 3T3 fibroblasts. Franco, L., Zocchi, E., Usai, C., Guida, L., Bruzzone, S., Costa, A. and De Flora, A. J.Biol.Chem. 24, 21642-8, 2001. 
  13. Paracrinally stimulated expansion of early human hemopoietic progenitors by stroma-generated cyclic ADP-ribose. Zocchi, E., Podestà, M., Pitto, A., Usai, C., Bruzzone, S., Franco, L., Guida, L., Bacigalupo, A. and De Flora, A. FASEB J. 15, 1610-12, 2001.
  14. CD38 Expression and functional activities are upregulated by IFN-g on human monocytes and monocytic cell lines. Musso, T., Deaglio S., Franco, L., Calosso, L., Badolato, R., Garbarino, G., Dianzani, U. and Malavasi, F. Journal of Leukocyte Biology, 69,2001
  15. Extracellular Cyclic ADP-ribose potentaites Ach-induced contraction in bovine tracheal smooth muscle. Franco, L., Bruzzone, S., Song, P., Guida, L., Zocchi, E., Walseth, T.F., Crimi, E., Usai, C., De Flora, A. and Brusasco, V. Am. J. Physiol. Lung Cell. Mol. Physiol., 280,L98-L106, 2001.
  16. 16.  Connexin 43 hemichannels mediate Ca2+ -regulated transmembrane NAD+ fluxes in intact cells. Bruzzone, S., Guida, L., Zocchi, E., Franco, L. and De Flora, A. FASEB J, 15,10-12, 2001.
  17. 17.  Extracellular cyclic ADP-ribose increases intracellualr free calcium concentration and stimulates prolifersarion of human hemopoietic progenitors. Podesta’ M., Zocchi, E., Pitto, A., Usai, C., Franco, L., Bruzzone, S., Guida, L., Bacigalupo, A., Scadden, D.T., Walseth, T.F., De Flora, A. and Daga, A. FASEB J. 14, 680-690, 2000
  18. Topology of CD 38. De Flora, A., Franco, L., Guida, L., Bruzzone, S., Usai, C. and Zocchi, E. Chem. Immunol., 75, 79-98, 1999.
  19. Ligand-induced internalization of CD38 results in intracellular Ca2+ mobilization. Role of NAD+ transport across cell membranes. Zocchi, E., Usai, C., Guida, L., Franco, L., Bruzzone, S., Passalacqua, M. and De Flora, A. FASEB J.,13, 273-283, 1999.
  20. 20.  Dimeric and tetrameric forms of catalytically active transmembrane CD38 in transfected HeLa cells. Bruzzone, S., Guida, L., Franco, L., Zocchi, E., Corte, G. and De Flora, A. Febs Lett., 433, 275-278,1998.
  21. 21.  The transmembrane glycoprotein CD38 is a catalytically active transporter responsible for generation and influx of the second messenger Cyclic ADP-ribose across membranes. Franco, L., Guida, L., Bruzzone, S., Zocchi, E., Usai, C. and De Flora, A. Faseb J., 12, 1507-1520, 1998.
  22. 22.  Expression of CD38 increases intracellular calcium concentration and reduces doubling time in HeLa and 3T3 cells. Zocchi, E., Daga, A., Usai, C., Franco, L., Guida, L., Bruzzone, S., Costa, A., Marchetti, C., De Flora, A. J. Biol. Chem. 273, 8017-8024, 1998.
  23. 23.  Ectocellular CD38-catalyzed synthesis and intracellular Ca2+-mobilizing activity of Cyclic ADP-ribose. De Flora, A., Franco, L., Guida, L., Bruzzone, S., Zocchi, E. Cell Biochem. Biophys. 28, 45-62, 1998.
  24. 24.  Cyclic GMP Dependent and Independent Effects on the Synthesis of the Calcium Messengers Cyclic ADP-ribose and NAADP. Graeff R.M., Franco, L., De Flora, A., Lee, H.C. J. Biol. Chem., 273, 118-125, 1998.
  25. 25.  The CD38/Cyclic ADP-ribose system: A topological paradox. De Flora, A., Guida, L., Franco, L., Zocchi, E. Int. J. Biochem. Cell Biol. 29, 1149-1166, 1997.
  26. 26.  CD38 and ADP-ribosyl cyclase catalyze the synthesis of a dimeric ADP-ribose that potentiates the Calcium-mobilizing activity of Cyclic ADP-ribose. De Flora, A., Guida, L., Franco, L., Zocchi, E., Bruzzone, S., Benatti, U., Damonte, G.,  Lee, H.C. J. Biol. Chem. 272, 12945-12951, 1997.
  27. NAD+-dependent internalization  of the transmembrane glycoprotein CD38 in  human Namalwa B cells.  Zocchi,E., Franco, L.,  Guida, L.,  Piccini, D., Tacchetti, C.,  De Flora, A. FEBS Lett. 396, 327-332, 1996.
  28. Ectocellular in vitro and in vivo metabolism of cyclic ADP-ribose in cerebellum. De Flora, A., Guida, L., Franco, L., Zocchi, E., Pestarino, M., Usai, C., Marchetti, C., Fedele, E., Fontana, G. and Raiteri, M. Biochem. J. 320, 665-672,  1996.
  29. Identification and characterization of an active soluble form of human CD38 in normal and pathological fluids. Funaro, A., Horenstein, A.L., Calosso, L., Morra, M., Tarocco, R.P., Franco, L., De Flora, A., Malavasi, F. Int Immunol. 8, 1643-1650, 1996.
  30. ADP-ribose, ADP-ribulose, cyclic ADP-ribose: new and old metabolites in human red blood cells. De Flora, A., Zocchi, E., Guida, L., Franco, L., Benatti, U., Bargellesi, A. and Malavasi, F. In: "The Oxygen Paradox" (Davies, K.J.A. and Ursini F. Eds.) CLEUP University Press, Padova pp.181-192, 1995.
  31. Structural role of disulfide bridges in the cyclic ADP-ribose related bifunctional ectoenzyme CD38. Guida, L., Franco, L., Zocchi, E., De Flora, A. FEBS Lett.,  368, 481-484, 1995.
  32. Self-aggregation of purified and membrane-bound erythrocyte CD38 induces extensive decrease of its ADP-ribosyl cyclase activity. Zocchi, E., Franco, L., Guida, L., Calder, L., De Flora, A. FEBS Lett., 359, 35-40, 1995.
  33. Metabolic conversions of NAD+ and cyclic ADP-ribose at the outer surface of human red blood cells. Zocchi, E., Guida, L., Franco, L., Benatti, U., Malavasi, F., De Flora, A. In: "Biochemistry of cell membranes. A compendium of selected topics" (Papa, S. and Tager, J.M. Eds.) Birkhauser Verlag  Basel,   pp. 221-229, 1995.
  34. Human CD38: a transmembrane glycoprotein with pleiotropic ectoenzyme functions. Funaro, A., Roggero, S., Horenstein, A., Calosso, L., Dianzani, U., De Monte, L.B., Zocchi, E., Franco, L., Guida, L., Ausiello, C.M., Drach, J., Mehta, K., Bargellesi, A., Malavasi, F. In: Leukocyte Typing V: White Cell Differentiation Antigens. (Schlossman, S., Boumsell, L:, Gilks, W., Harlan, J., Kishimoto, T., Morimoto, C., Ritz, J., Shaw, S., Silverstein, R., Springer, T., Tedder, T., Todd, R Eds.) Oxford University Press, pp. 381-383, 1995.
  35. Self-aggregation of the transmembrane glycoprotein CD38 purified from human erythrocytes. Franco, L., Zocchi, E., Calder, L., Guida, L., Benatti, U., De Flora, A. Biochem. Biophys. Res. Commun. 202, 1710-1718, 1994.
  36. A single protein immunologically identified as CD38 displays NAD+ glycohydrolase, ADP-ribosyl cyclase and cyclic ADP-ribose hydrolase activities at the outer surface of human erythrocytes. Zocchi, E., Franco, L., Guida, L., Benatti, U., Bargellesi, A., Malavasi, F.  Lee, H.C., De Flora, A. Biochem. Biophys. Res. Commun., 196, 1459-1465, 1993.
  37. Free Adenosine diphosphate ribose in human erythrocytes: pathways of intraerythrocytic conversion and non-enzymic binding to membrane proteins. Zocchi,E., Guida, L., Franco, L., Silvestro, L., Guerrini, M., Benatti, U. and De Flora, A. Biochem. J. 295, 121-130, 1993.
  38. Production and hydrolysis of cyclic ADP-ribose at the outer surface of human erythrocytes.Lee, H.C., Zocchi, E., Guida, L., Franco, L., Benatti, U. and De Flora, A.Biochem. Biophys. Res. Commun. 191, 639-645 1993.
  39. Adenosine diphosphate ribulose in human erythrocytes: a new metabolite with membrane binding properties. Franco, L., Guida, L., Zocchi, E., Silvestro, L., Benatti, U. and  De Flora, A. Biochem. Biophys. Res. Commun. 190, 1143-1148 1993.
  40. Presence and turnover of Adenosine Diphosphate Ribose in human erythrocytes. Guida, L., Zocchi, E., Franco, L., Benatti, U. and De Flora, A. Biochem. Biophys. Res. Commun. 188, 402-408, 1992.
  41. Heterogeneity of guanine nucleotide binding proteins in human red blood cell membranes. De Flora, A., Damonte, G., Sdraffa, A., Franco, L., Benatti, U. In: "Red Blood Cell Aging" (Magnani, M. and De Flora, A. Eds.), Plenum Press, New York, 161-171, 1991.

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Accetta e chiudi

I numeri di IIT

L’Istituto Italiano di Tecnologia (IIT) è una fondazione di diritto privato - cfr. determinazione Corte dei Conti 23/2015 “IIT è una fondazione da inquadrare fra gli organismi di diritto pubblico con la scelta di un modello di organizzazione di diritto privato per rispondere all’esigenza di assicurare procedure più snelle nella selezione non solo nell’ambito nazionale dei collaboratori, scienziati e ricercatori ”.

IIT è sotto la vigilanza del Ministero dell'Istruzione, dell'Università e della Ricerca e del Ministero dell'Economia e delle Finanze ed è stato istituito con la Legge 326/2003. La Fondazione ha l'obiettivo di promuovere l'eccellenza nella ricerca di base e in quella applicata e di favorire lo sviluppo del sistema economico nazionale. La costruzione dei laboratori iniziata nel 2006 si è conclusa nel 2009.

Lo staff complessivo di IIT conta circa 1440 persone. L’area scientifica è rappresentata da circa l’85% del personale. Il 45% dei ricercatori proviene dall’estero: di questi, il 29% è costituito da stranieri provenienti da oltre 50 Paesi e il 16% da italiani rientrati. Oggi il personale scientifico è composto da circa 60 principal investigators, circa 110 ricercatori e tecnologi di staff, circa 350 post doc, circa 500 studenti di dottorato e borsisti, circa 130 tecnici. Oltre 330 posti su 1400 creati su fondi esterni. Età media 34 anni. 41% donne / 59 % uomini.

Nel 2015 IIT ha ricevuto finanziamenti pubblici per circa 96 milioni di euro (80% del budget), conseguendo fondi esterni per 22 milioni di euro (20% budget) provenienti da 18 progetti europei17 finanziamenti da istituzioni nazionali e internazionali, circa 60 progetti industriali

La produzione di IIT ad oggi vanta circa 6990 pubblicazioni, oltre 130 finanziamenti Europei e 11 ERC, più di 350 domande di brevetto attive, oltre 12 start up costituite e altrettante in fase di lancio. Dal 2009 l’attività scientifica è stata ulteriormente rafforzata con la creazione di dieci centri di ricerca nel territorio nazionale (a Torino, Milano, Trento, Parma, Roma, Pisa, Napoli, Lecce, Ferrara) e internazionale (MIT ed Harvard negli USA) che, unitamente al Laboratorio Centrale di Genova, sviluppano i programmi di ricerca del piano scientifico 2015-2017.

IIT: the numbers

Istituto Italiano di Tecnologia (IIT) is a public research institute that adopts the organizational model of a private law foundation. IIT is overseen by Ministero dell'Istruzione, dell'Università e della Ricerca and Ministero dell'Economia e delle Finanze (the Italian Ministries of Education, Economy and Finance).  The Institute was set up according to Italian law 326/2003 with the objective of promoting excellence in basic and applied research andfostering Italy’s economic development. Construction of the Laboratories started in 2006 and finished in 2009.

IIT has an overall staff of about 1,440 people. The scientific staff covers about 85% of the total. Out of 45% of researchers coming from abroad 29% are foreigners coming from more than 50 countries and 16% are returned Italians. The scientific staff currently consists of approximately 60 Principal Investigators110 researchers and technologists350 post-docs and 500 PhD students and grant holders and 130 technicians. External funding has allowed the creation of more than 330 positions . The average age is 34 and the gender balance proportion  is 41% female against 59% male.

In 2015 IIT received 96 million euros in public funding (accounting for 80% of its budget) and obtained 22 million euros in external funding (accounting for 20% of its budget). External funding comes from 18 European Projects, other 17 national and international competitive projects and approximately 60 industrial projects.

So far IIT accounts for: about 6990 publications, more than 130 European grants and 11 ERC grants, more than 350 patents or patent applications12 up start-ups and as many  which are about to be launched. The Institute’s scientific activity has been further strengthened since 2009 with the establishment of 11 research nodes throughout Italy (Torino, Milano, Trento, Parma, Roma, Pisa, Napoli, Lecce, Ferrara) and abroad (MIT and Harvard University, USA), which, along with the Genoa-based Central Lab, implement the research programs included in the 2015-2017 Strategic Plan.