Torino 2006. XX Olympic and IX Paralympic Winter Games: the ENT experience.

A total of 27 competition days, more than 3000 athletes, over 10,000 components of the Olympic family, 3,500 workers, 2,500 volunteers, an overall business of more than 2 billion Euros. These, in a nutshell, are just a few of the data concerning the XX Olympic and the IX Paralympic Winter Games, Torino, Italy, 2006. Such a huge event, obviously required a meticulously organized medical service to cope with the healthcare of the athletes, official workers and the Olympic family, distributed over a geographic area of approximately 80 km in diameter. An ENT service was organized within the medical service, which was divided between 3 Polyclinics, in which 12 ENT Specialists were on duty. The present report gives an account of the final data concerning the service involved, together with a description of the approach used in the actual organization, with a view to providing useful information for colleagues who will be called upon, for a similar service, in future Olympic Winter Games. The ENT healthcare offered was confirmed to be proportional to the requirements, both from a qualitative and quantitative point of view. All the ENT specialists involved, reported having gained an immense store of human experience from having lived the Olympic atmosphere as a volunteer exerting one's own profession. The facilities available in the Polyclinics, which were at a considerable distance from the Hospital, were found to be more than adequate with respect to the pathological conditions and service requested, particularly in 17% of the cases which would otherwise have been sent to a Hospital Outpatient Unit at least 80 km away.

Antennapedia/HS1 chimeric phosphotyrosyl peptide: conformational properties, binding capability to c-Fgr SH2 domain and cell permeability.

With the aim of interfering with the signaling pathways mediated by the SH2 domains of Src-like tyrosine kinases, we synthesized a tyrosyl-phospho decapeptide, corresponding to the sequence 392-401 of HS1 protein, which inhibits the secondary phosphorylation of HS1 protein catalyzed by the Src-like kinases c-Fgr or Lyn. This phospho-peptide was modified to enter cells by coupling to the third helix of Antennapedia homeodomain, which is able to translocate across cell membranes. Here we present CD and fluorescence studies on the conformational behavior in membrane-mimicking environments and on lipid interactions of Antennapedia fragment and its chimeric phosphorylated and unphosphorylated derivatives. These studies evidenced that electrostatic rather than amphiphilic interactions determine the peptide adsorption on lipids. Experiments performed with recombinant protein containing the SH2 domain of c-Fgr fused with GST and with isolated erythrocyte membranes demonstrated that the presence of the N-terminal Antennapedia fragment only slightly affects the binding of the phospho-HS1 peptide to the SH2 domain. In fact, it has been shown that in isolated erythrocyte membranes, both phospho-HS1 peptide and its chimeric derivative greatly affect either the SH2-mediated recruitment of the c-Fgr to the transmembrane protein band 3 and the following phosphorylation of the protein catalyzed by the Src-like kinase c-Fgr. The ability of the chimeric phospho-peptide to enter cells has been demonstrated by confocal microscopy analysis.