Epidemiology and cost of herpes zoster and postherpetic neuralgia among patients treated in primary care centres in the valencian community of Spain

<p>Abstract</p> <p>Background</p> <p>Data on the epidemiology and costs related to herpes zoster (HZ) and postherpetic neuralgia (PHN) in Spain are scarce; therefore, studies are needed to evaluate the epidemiological and economic impact of HZ and its most common complication, PHN. The present study aimed to estimate the clinical and economic burden of HZ and PHN in Valencia (Spain).</p> <p>Methods</p> <p>We prospectively analyzed the burden of HZ and PHN and their attributable costs in patients from 25 general practices in the Autonomous Community of Valencia serving 36,030 persons aged > 14 years. All patients with a clinical diagnosis of HZ who attended these centers between December 1^st2006 and November 30^th2007 were asked to participate. Patients included were followed for 1 year.</p> <p>Results</p> <p>Of the 130 cases of HZ followed up, continued pain was experienced by 47.6% (95% confidence interval (CI) = 35.6-56.7%) at 1 month after rash onset, by 14.5% (95% CI = 7.8-1.2%) at 3 months, by 9.0% (95% CI = 3.7-14.3%) at 6 months, and by 5.9% (95% CI = 1.5-10.3%) at 12 months. The percentage of patients with PHN increased with age, from 21.4% (95% CI = 8.3-40) in patients < 50 years to 59.2% (95% CI = 44.4-74) in patients ≥ 70 years. The estimated total cost for the 130 HZ cases during the follow-up period was €49,160 ($67,349). Mean cost per patient was €378 (range 53-2,830) ($517, range 73-3,877).</p> <p>Conclusions</p> <p>This study shows that PHN is a relatively common complication of HZ and that both conditions combined give rise to a significant clinical and economic burden for patients and providers.</p

THE RELIABILITY OF A COMMERCIAL ACCELEROMETER UNIT DURING ANAEROBIC TESTING OF COMPETITIVE ATHLETES

Molly N. Schieber, Dave Heller, Nicole Moodie; Rockhurst University, Kansas City, Missouri e-mail: [email protected] Accelerometers are a tool that can be used to objectively measure frequency, duration, and intensity of a physical activity and exercise. An easily accessible tool such as an accelerometer could be beneficial to a widespread range of athletes. PURPOSE: This aim of the present study was to test the reliability of designated G-force measures obtained by a commercial accelerometer. METHODS: Fourteen competitive athletes (10 male, 4 female) volunteered to attend one anaerobic testing session. At the beginning of the session athletes completed a required warm-up consisting of a 5 minute jog, stretching of major muscle groups, and two progressive 50 yard sprints. After the warm-up the accelerometer was placed on the athletes’ back between the shoulder blades and anchored at two points with adhesive. Athletes then completed two 40 yard dashes with a 5 minute rest interval between trials. RESULTS: Data from the accelerometer unit was analyzed using software created by the unit developer. Based on the G-forces recorded by the accelerometer unit, the software created explosion, right-left symmetry, efficiency, and propulsion scores. Paired samples t-tests determined no significant differences between trial 1-trial 2 scores for explosion [t(13)=0.186, p\u3c0.05], right-left symmetry t(13)=0.181, p\u3c0.05], efficiency [t(13)=-1.984, p\u3c0.05], and propulsion [t(13)=-1.969, p\u3c0.05]. CONCLUSION: The lack of significant difference in these measures shows the test/re-test reliability of the Impulse accelerometer

Arrest defective 1 regulates the oxidative stress response in human cells and mice by acetylating methionine sulfoxide reductase A

Methionine sulfoxide reductase A (MSRA) protects proteins from oxidation, and also helps remove reactive oxygen species (ROS) by recovering antioxidant enzymes inactivated by oxidation. Although its functions have been investigated extensively, little is known about the mechanism by which MSRA is regulated. Arrest defective 1 (ARD1) is an enzyme that catalyzes not only N-terminal acetylation as a cotranslational modification but also lysine acetylation as a posttranslational modification. ARD1, which is expressed in most cell types, is believed to participate in diverse biological processes, but its roles are poorly understood. Given that MSRA was hunted in a yeast two-hybrid screen with ARD1 as the bait, we here investigated whether ARD1 is a novel regulator of MSRA. ARD1 was shown to interact with and acetylate MSRA in both cells and test tubes. It specifically acetylated the K49 residue of MSRA, and by doing so repressed the enzymatic function of MSRA. ARD1 increased cellular levels of ROS, carbonylated proteins and DNA breaks under oxidative stress. Moreover, it promoted cell death induced by pro-oxidants, which was attenuated in MSRA-deficient cells. When mice were exposed to hyperoxic conditions for 2 days, their livers and kidneys were injured and protein carbonylation was increased. The oxidative tissue injury was more severe in ARD1 transgenic mice than in their wild-type littermates. In conclusion, ARD1 has a crucial role in the cellular response to oxidative stress as a bona fide regulator of MSRA. ARD1 is a potential target for ameliorating oxidative injury or for potentiating ROS-producing anticancer agents