PHD:           1988, University of Marburg


Scientific interests

His major interest over the time between 1990 and 1996 was to elucidate the molecular and cellular function of proteins (Pax-proteins) which have been associated with mouse mutants and human syndromes (mouse mutants: undulated, splotch, small eye; Human syndromes: Waardenburg, Aniridia). His group has isolated and characterized the Fras1 gene in mouse and in collaboration with Dr. P. Scambler (UK) have shown that mutations in the human counterpart FRAS1, are responsible for the Fraser syndrome. In addition to Fras1, the family of Fras1/Frem proteins comprises three additional members, Frem1, Frem2 and Frem3 which interact with each other to form an interdependent macromolecular protein complex within the basement membrane surrounding the embryonic epithelia. The major focus of the research group is to identify the proteins which interact with Fras1/Frem, aiming to explore the composition, the assembly and the protein-protein interactions of the extracellular matrix components that underlie epithelia and confer the structural cohesiveness as well as the functional interaction between epithelia and mesenchyme in mammals.

Recent publications

  • Pavlakis, E., Chiotaki, R. and Chalepakis, G. (2011). The role of Fras1/Frem proteins in the structure and function of basement membrane. Int. J. Biochem. Cell Biol. 43, 487-495.
  • Vrontou, S., Petrou, P., Meyer, B.I., Galanopoulos, V.K., Imai, K., Yanagi, M., Chowdhury, K., Scambler, P.J. and Chalepakis, G. (2003). Fras1 deficiency results in cryptophthalmos, renal agenesis and bleb phenotype in mice. Nat. Genet. 34, 209-214.
  • McGregor, L., Makela, V., Darling, S.M., Vrontou, S., Chalepakis, G., Roberts, C., Smart, N., Rutland, P., Prescott, N., Hopkins, J., Bentley, E., Shaw, A., Roberts, E., Mueller, R., Jadeja, S., Philip, N., Nelson, J., Francannet, C., Perez-Aytes, A., Megarbane, A., Kerr, B., Wainwright, B., Woolf, A.S., Winter, R.M. and Scambler, P.J. (2003). Fraser syndrome and mouse blebbed phenotype caused by mutations in FRAS1/Fras1 encoding a putative extracellular matrix protein. Nat. Genet. 34, 203-208.
  • Chiotaki, R., Petrou, P., Giakoumaki, E., Pavlakis, E., Sitaru, C. and Chalepakis, G. (2007). Spatiotemporal distribution of Fras1/Frem proteins during mouse embryonic development. Gene Expression Patterns 7, 381-388.
  • Petrou, P., Pavlakis, E., Dalezios, Y. and Chalepakis, G. (2007). Basement membrane localization of Frem3 is independent of the Fras1/Frem1/Frem2 protein complex within the sublamina densa. Matrix Biol. 26, 652-658.