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Moro Laura

Laura Moro's picture

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Email: laura.moro@pharm.unipmn.it

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Interdisciplinary or interuniversity centers

Lab members

Main research interests

There are two major research directions in our laboratory.

  • The first is to understand the way that cell adhesion to structural molecules of the extracellular matrix (ECM) regulates cell behavior. The ECM is a dynamic structure that regulates cell shape and migration, and also has a key role in determining the intracellular responses of extracellular signaling ligands for survival and proliferation, as well as cellular fate and differentiation. Adhesion also contributes to most common human diseases, including inflammation, thrombosis, tumor spread and infection. We are particularly interested in how the class of cell surface receptors for ECM called integrins cooperates with Receptor Tyrosine Kinases (RTKs) to promote cell survival and proliferation. Our laboratory is employing a wide variety of biochemical, molecular biological and cell biological techniques to understand the molecular details of how signals initiated by integrin-containing adhesion complexes, together with those triggered by soluble factors, are integrated to activate transcription of specific genes.
  • The second major facet of our work is to elucidate non-genomic signal trasduction pathways mediated by steroid hormones receptors. In particular we are interested in non genomic actions mediated by estrogen receptors in the control of proliferation of breast cancer cells and in the identification of new interactors of estrogen receptors and their role in drug resistance.

Key references

  • Moro L., Venturino M., Bozzo C., Beguinot L., Silengo L., Altruda F., Tarone G. and Defilippi P. Integrin mediated adhesion induces ligand-independent activation of EGF-R: role in MAPK induction and adhesion dependent cell survival. 1998 EMBO J., 17, 22: 6622-6632. IF 10.492
  • Moro L., Dolce L., Cabodi S., Bergatto E., Boeri Erba E., Smeriglio M., Turco E., Retta F.S., Giuffrida G., Venturino M., Godovac-Zimmerman J., Scaefer E., Beguinot L., Tacchetti C., Gaggini P., Silengo L., Tarone G., Defilippi P. Integrin-induced EGF receptor activation requires c-Src and p130Cas and leads to phosphorylation of specific EGF receptor tyrosines. 2002 J Biol Chem. 277, 11, 9405-9414. [News and views by K. Yamada. Nature Cell Biology. 2002 march.] IF 6.355
  • Cabodi S., Moro L., Baj G., Smeriglio M. , Di Stefano P., Surico N., Silengo L. , Turco E., Tarone G. and Defilippi P. p130Cas interacts with estrogen receptor alpha and modulates non-genomic estrogen signaling in breast cancer cells. 2004 J Cell Sci, Mar 15;117(Pt 8):1603-11. IF 6.910
  • S. Cabodi, L. Moro, E. Bergatto, E. Boeri Erba, P. Di Stefano, E. Turco, G. Tarone and P. Defilippi Integrin-dependent regulation of EGF receptor and of EGF-dependent responses. 2004 Biochem. Soc. Trans., Jun;32(Pt3):438-42. IF 2.267
  • Moro L., Reineri S, Piranda D, Pietrapiana D, Lova P, Bertoni A, Graziani A, Defilippi P, Canobbio I, Torti M, Sinigaglia F. Non-genomic effects of 17{beta}-estradiol in human platelets: potentiation of thrombin-induced aggregation through estrogen receptor {beta} and Src kinase. Blood. 2005 Jan 1;105(1):115-21. IF 9.782

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