Methodology for evaluating the safety level of current accepted design solutions for limiting fire spread between buildings

External fire spread between buildings is internationally considered as a major concern for buildings in dense urban environments. While design guidelines differ between countries, the fundamental methods currently used for limiting the risk of fire spread between buildings are generally limited to specifying the minimum required separation distance for a given unprotected façade area, or conversely, limiting the maximum allowable unprotected façade area for a given separation distance. The safety level associated with the current design guidelines is however unknown, making the implementation of innovative, safer and more cost-effective design solutions difficult. In order to assess the safety target implicitly incorporated in currently accepted design solutions, a methodology is developed for evaluating the annual probability of reaching unacceptable radiation intensities at the opposite façade. As a case study, the methodology is applied to a design which is in agreement with the current UK requirements specified in BR 187. This case study exposes inconsistencies in the current design guidelines, indicating the need for developing explicit safety targets

Hakkeen kuivaus Bioenergiakeskuksen monikäyttökuivurissa auringon energiaa lisälämmönlähteenä hyödyntäen

Hakkeen kuivaus auringon energiaa lisälämmönlähteenä hyödyntämällä osoittautui tehdyn kokeen valossa toimivaksi ratkaisuksi. Kuivaus tehostuu merkittävästi lämmittämällä kuivausilmaa, jo yhden asteen lämpötilan nousu pudottaa ilman suhteellista kosteutta 5 prosenttiyksikköä ja ilman kuivauskyky kasvaa

Protein Phosphatase 2A in the Regulatory Network Underlying Biotic Stress Resistance in Plants

Biotic stress factors pose a major threat to plant health and can significantly deteriorate plant productivity by impairing the physiological functions of the plant. To combat the wide range of pathogens and insect herbivores, plants deploy converging signaling pathways, where counteracting activities of protein kinases and phosphatases form a basic mechanism for determining appropriate defensive measures. Recent studies have identified Protein Phosphatase 2A (PP2A) as a crucial component that controls pathogenesis responses in various plant species. Genetic, proteomic and metabolomic approaches have underscored the versatile nature of PP2A, which contributes to the regulation of receptor signaling, organellar signaling, gene expression, metabolic pathways, and cell death, all of which essentially impact plant immunity. Associated with this, various PP2A subunits mediate post-translational regulation of metabolic enzymes and signaling components. Here we provide an overview of protein kinase/phosphatase functions in plant immunity signaling, and position the multifaceted functions of PP2A in the tightly inter-connected regulatory network that controls the perception, signaling and responding to biotic stress agents in plants.Peer reviewe

PP2A-B’γ modulates foliar trans-methylation capacity and the formation of 4-methoxy-indol-3-yl-methyl glucosinolate in Arabidopsis leaves

Glucosinolates (GSL) of cruciferous plants comprise a major group of structurally diverse secondary compounds which act as deterrents against aphids and microbial pathogens and have large commercial and ecological impacts. While the transcriptional regulation governing the biosynthesis and modification of GSL is now relatively well understood, post-translational regulatory components that specifically determine the structural variation of indole glucosinolates have not been reported. We show that the cytoplasmic protein phosphatase 2A regulatory subunit B'gamma (PP2A-B'gamma) physically interacts with indole glucosinolate methyltransferases and controls the methoxylation of indole glucosinolates and the formation of 4-meth-oxy-indol-3-yl-methyl glucosinolate in Arabidopsis leaves. By taking advantage of proteomic approaches and metabolic analysis we further demonstrate that PP2A-B'gamma is required to control the abundance of oligomeric protein complexes functionally linked with the activated methyl cycle and the trans-methylation capacity of leaf cells. These findings highlight the key regulatory role of PP2A-B'gamma in methionine metabolism and provide a previously unrecognized perspective for metabolic engineering of glucosinolate metabolism in cruciferous plants.Peer reviewe

Effect of site of lactate infusion on regional lactate exchange in pigs

Background The rate of extra-hepatic lactate production and the route of influx of lactate to the liver may influence both hepatic and extra-hepatic lactate exchange. We assessed the dose-response of hepatic and extra-hepatic lactate exchange during portal and central venous lactate infusion. Methods Eighteen pigs randomly received either portal (n=5) or central venous (n=7) lactate infusion or saline (n=6). Sodium lactate was infused at 33, 66, 99, and 133 µmol kg−1 min−1 for 20 min each. Systemic and regional abdominal blood flows and plasma lactate were measured at 20 min intervals until 1 h post-infusion, and regional lactate exchange was calculated (area under lactate uptake-time curve). Results Total hepatic lactate uptake [median (95% confidence interval)] during the experimental protocol (140 min) was higher during portal [8198 (5487-12 798) µmol kg−1] than during central venous lactate infusion [4530 (3903-5514) µmol kg−1, P<0.05]. At a similar hepatic lactate delivery (∼400 µmol kg−1 min−1), hepatic lactate uptake [mean and standard deviation (sd)] was higher during portal [118 (sd 55) µmol kg−1 min−1] than during central venous lactate infusion [44 (12) µmol kg−1 min−1, P<0.05]. Time courses of arterial lactate concentrations and lactate uptake at other measured regions were similar in both groups. Conclusions Higher hepatic lactate uptake during portal compared with central venous lactate infusion at a similar total hepatic lactate influx underlines the role of portal vein lactate concentration in total hepatic lactate uptake capacity. Arterial lactate concentration does not depend on the site of lactate infusion. At higher arterial lactate concentrations, all regions participated in lactate uptak