Preparing for Euro 2012: developing a hazard risk assessment.

INTRODUCTION: Risk assessment is a vital step in the disaster-preparedness continuum as it is the foundation of subsequent phases, including mitigation, response, and recovery. HYPOTHESIS/PROBLEM: To develop a risk assessment tool geared specifically towards the Union of European Football Associations (UEFA) Euro 2012. METHODS: In partnership with the Donetsk National Medical University, Donetsk Research and Development Institute of Traumatology and Orthopedics, Donetsk Regional Public Health Administration, and the Ministry of Emergency of Ukraine, a table-based tool was created, which, based on historical evidence, identifies relevant potential threats, evaluates their impacts and likelihoods on graded scales based on previous available data, identifies potential mitigating shortcomings, and recommends further mitigation measures. RESULTS: This risk assessment tool has been applied in the vulnerability-assessment-phase of the UEFA Euro 2012. Twenty-three sub-types of potential hazards were identified and analyzed. Ten specific hazards were recognized as likely to very likely to occur, including natural disasters, bombing and blast events, road traffic collisions, and disorderly conduct. Preventative measures, such as increased stadium security and zero tolerance for impaired driving, were recommended. Mitigating factors were suggested, including clear, incident-specific preparedness plans and enhanced inter-agency communication. CONCLUSION: This hazard risk assessment tool is a simple aid in vulnerability assessment, essential for disaster preparedness and response, and may be applied broadly to future international events.

Regulation of the Ste20-like kinase, SLK: involvement of activation segment phosphorylation.

Expression and activation of the Ste20-like kinase, SLK, is increased during kidney development and recovery from ischemic acute kidney injury. SLK promotes apoptosis, and it may regulate cell survival during injury or repair. This study addresses the role of phosphorylation in the regulation of kinase activity. We mutated serine and threonine residues in the putative activation segment of the SLK catalytic domain and expressed wild type (WT) and mutant proteins in COS-1 or glomerular epithelial cells. Compared with SLK WT, the T183A, S189A, and T183A/S189A mutants showed reduced in vitro kinase activity. SLK WT, but not mutants, increased activation-specific phosphorylation of c-Jun N-terminal kinase (JNK) and p38 kinase. Similarly, SLK WT stimulated activator protein-1 reporter activity, but activation of activator protein-1 by the three SLK mutants was ineffective. To test if homodimerization of SLK affects phosphorylation, the cDNA encoding SLK amino acids 1-373 (which include the catalytic domain) was fused with a cDNA for a modified FK506-binding protein, Fv (Fv-SLK 1-373). After transfection, the addition of AP20187 (an FK506 analog) induced regulated dimerization of Fv-SLK 1-373. AP20187-stimulated dimerization enhanced the kinase activity of Fv-SLK 1-373 WT. In contrast, kinase activity of Fv-SLK 1-373 T183A/S189A was weak and was not enhanced after dimerization. Finally, apoptosis was increased after expression of Fv-SLK 1-373 WT but not T183A/S189A. Thus, phosphorylation of Thr-183 and Ser-189 plays a key role in the activation and signaling of SLK and could represent a target for novel therapeutic approaches to renal injury.