Factors Influencing the Prioritization of Injured Patients for Transfer to a Burn or Trauma Center Following a Mass Casualty Event.

OBJECTIVES: In New York City, a multi-disciplinary Mass Casualty Consultation team is proposed to support prioritization of patients for coordinated inter-facility transfer after a large-scale mass casualty event. This study examines factors that influence consultation team prioritization decisions. METHODS: As part of a multi-hospital functional exercise, 2 teams prioritized the same set of 69 patient profiles. Prioritization decisions were compared between teams. Agreement between teams was assessed based on patient profile demographics and injury severity. An investigator interviewed team leaders to determine reasons for discordant transfer decisions. RESULTS: The 2 teams differed significantly in the total number of transfers recommended (49 vs 36; P = 0.003). However, there was substantial agreement when recommending transfer to burn centers, with 85.5% agreement and inter-rater reliability of 0.67 (confidence interval: 0.49-0.85). There was better agreement for patients with a higher acuity of injuries. Based on interviews, the most common reason for discordance was insider knowledge of the local community hospital and its capabilities. CONCLUSIONS: A multi-disciplinary Mass Casualty Consultation team was able to rapidly prioritize patients for coordinated secondary transfer using limited clinical information. Training for consultation teams should emphasize guidelines for transfer based on existing services at sending and receiving hospitals, as knowledge of local community hospital capabilities influence physician decision-making.

Association of ambient fine particles with out-of-hospital cardiac arrests in New York City.

Cardiovascular morbidity has been associated with particulate matter (PM) air pollution, although the relation between pollutants and sudden death from cardiac arrest has not been established. This study examined associations between out-of-hospital cardiac arrests and fine PM (of aerodynamic diameter ≤2.5 µm, or PM(2.5)), ozone, nitrogen dioxide, sulfur dioxide, and carbon monoxide in New York City. The authors analyzed 8,216 out-of-hospital cardiac arrests of primary cardiac etiology during the years 2002-2006. Time-series and case-crossover analyses were conducted, controlling for season, day-of-week, same-day, and delayed/apparent temperature. An increased risk of cardiac arrest in time-series (relative risk (RR) = 1.06, 95% confidence interval (CI): 1.02, 1.10) and case-crossover (RR = 1.04, 95% CI: 0.99, 1.08) analysis for a PM(2.5) increase of 10 µg/m³ in the average of 0- and 1-day lags was found. The association was significant in the warm season (RR = 1.09, 95% CI: 1.03, 1.15) but not the cold season (RR = 1.01, 95% CI: 0.95, 1.07). Associations of cardiac arrest with other pollutants were weaker. These findings, consistent with studies implicating acute cardiovascular effects of PM, support a link between PM(2.5) and out-of-hospital cardiac arrests. Since few individuals survive an arrest, air pollution control may help prevent future cardiovascular mortality.

Novel Zn2+ coordination by the regulatory N-terminus metal binding domain of Arabidopsis thaliana Zn(2+)-ATPase HMA2.

Arabidopsis thaliana HMA2 is a Zn2+ transporting P1B-type ATPase required for maintaining plant metal homeostasis. HMA2 and all eukaryote Zn2+-ATPases have unique conserved N- and C-terminal sequences that differentiate them from other P1B-type ATPases. Homology modeling and structural comparison by circular dichroism indicate that the 75 amino acid long HMA2 N-terminus shares the betaalphabetabetaalpha folding present in most P1B-type ATPase N-terminal metal binding domains (N-MBDs). However, the characteristic metal binding sequence CysXXCys is replaced by Cys17CysXXGlu21, a sequence present in all plant Zn2+-ATPases. The isolated HMA2 N-MBD fragment binds a single Zn2+ (Kd 0.18 microM), Cd2+ (Kd 0.27 microM), or, with less affinity, Cu+ (Kd 13 microM). Mutagenesis studies indicate that Cys17, Cys18, and Glu21 participate in Zn2+ and Cd2+ coordination, while Cys17 and Glu21, but not Cys18, are required for Cu+ binding. Interestingly, the Glu21Cys mutation that generates a CysCysXXCys site is unable to bind Zn2+ or Cd2+ but it binds Cu+ with affinity (Kd 1 microM) higher than wild type N-MBD. Truncated HMA2 lacking the N-MBD showed reduced ATPase activity without significant changes in metal binding to transmembrane metal binding sites. Likewise, ATPase activity of HMA2 carrying mutations Cys17Ala, Cys18Ala, and Glu21Ala/Cys was also reduced but showed a metal dependence similar to the wild type enzyme. These observations suggest that plant Zn2+-ATPase N-MBDs have a folding and function similar to Cu+-ATPase N-MBDs. However, the unique Zn2+ coordination via two thiols and a carboxyl group provides selective binding of the activating metals to these regulatory domains. Metal binding through these side chains, although found in different sequences, appears as a common feature of both bacterial and eukaryotic Zn2+-ATPase N-MBDs.