Lessons Learnt from the Fukushima Accident-A Swedish Medical Preparedness Perspective.

The triple disaster in March 2011 tragically and severely affected the Japanese society, in spite of its well-developed infrastructure and good access to resources. A multitude of Japanese and international reports have since described the chain of events and actions taken in connection with the earthquake, the tsunami and the power plant failure in Fukushima. In order to further evaluate Japanese experiences of the disaster, and to bring home 'lessons-learnt' of relevance for continued emergency preparedness planning, a group from the National Board of Health and Welfare and other Swedish agencies performed an observer visit to Japan in 2012. A report from the group was recently published. Its main conclusions, and implications focusing on a strengthened national medical preparedness for radionuclear events in Sweden (and possibly elsewhere), are presented here.

Personal decontamination after exposure to stimulated liquid phase contaminants: functional assessment of a new unit.

OBJECTIVE: To evaluate the efficacy of a decontamination station following exposure of volunteers to liquids with physical characteristics comparable to sarin and mustard gas. DESIGN: Twenty-four volunteers participated in the experiment which was performed with all staff wearing personal protective equipment including respiratory protection. The clothes, skin, and hair of the volunteers were contaminated with the simulated liquid phase contaminants, ethyl lactate and methyl salicylate. Sulphur hexafluoride gas was used to confirm the ventilation efficacy. Decontamination followed guidelines using a two-stage procedure. In the first chamber, all volunteers received a 3-minute shower with water at 30 degrees C, and their clothes but not their respiratory masks were removed. In the second, they were twice washed thoroughly with soap and water. After decontamination, the volunteers entered a third chamber for first aid measures. RESULTS: The air concentration of sulphur hexafluoride was reduced by 1:10,000 between the first and the third chambers. Ethyl lactate and methyl salicylate were measured in low concentrations in the third chamber. The capacity was 16 volunteers per hour with two-thirds on stretchers. After self-decontamination of the staff, the concentration of ethyl lactate increased significantly in the third chamber, consistent with residual ethyl lactate adsorbed by their underwear. This observation revealed a deficiency in the guidelines for self-decontamination. CONCLUSION: The capacity of the decontamination unit was found to be 16 volunteers per hour. The ventilation system and guidelines of the decontamination unit were demonstrated to be effective under the conditions examined. The self-decontamination of the staff was not optimal.

Myocardial lactate dehydrogenase and its isoenzyme activities in transplanted human hearts.

Lactate dehydrogenase and its heart (H) and muscle (M) subunit activities were studied in right ventricular endomyocardial biopsies from eight transplanted human hearts and compared with five chronically failing hearts and six normal human hearts from brain-dead liver/kidney donors. Of the 17 transplant biopsies (taken 5-95 weeks postoperatively), only two showed histologic signs of chronic rejection: They were excluded from the group analysis. A higher proportion of the M subunit of lactate dehydrogenase (M%) was found in the transplanted and the chronically failing hearts than in the normal hearts, presumably reflecting increased myocardial anaerobic glycolytic stress. In the early post-transplantation period, M% was higher in the transplanted than in the chronically failing hearts. Thereafter M% gradually fell, but had not reached normal levels 1-2 years after transplantation. During that time it was similar to the values in the chronic-failure hearts. In the two biopsies with chronic rejection, M% was nearly twice as high as in contemporaneous biopsies showing mild or no rejection. Monitoring of enzymatic adaptation from endomyocardial biopsies may be of clinical interest.

Fibrillin immunoreactive fibers constitute a unique network in the human dermis: immunohistochemical comparison of the distributions of fibrillin, vitronectin, amyloid P component, and orcein stainable structures in normal skin and elastosis.

Fibrillin, a 350-kD glycoprotein, was recently localized to elastin-associated 10 nm microfibrils. Here, the distribution of fibrillin immunoreactivity was determined in normal skin in individuals of different ages and in lesions of solar elastosis or anetoderma. It was compared with the distribution of orcein-stainable fibers and with the immunoreactivities of vitronectin and amyloid P component. These glycoproteins are known to occur in conjunction with the orcein-stainable elastic fibers in adults, but not in the young. Fibrillin immunoreactivity was associated with orcein-stainable fibers in normal skin of both adults and the young. In addition, the fibrillin immunoreactive fiber network comprised fine fibers that were unstainable by orcein, anti-vitronectin, or anti-amyloid P component. Such fine fibers were especially abundant close to the dermal-epidermal junction zone. Immunoreactivities of anti-vitronectin and anti-amyloid P component were not always associated with fibrillin immunoreactivity but were consistently found to co-localize with orcein-stainable fibers in adults. This suggests vitronectin and amyloid P component to be associated with the amorphous elastin rather than with the microfibrils, although alternative interpretations are possible. In elastotic lesions, fibrillin immunoreactivity was generally fainter than that obtained using anti-vitronectin or anti-amyloid P component. In contrast, an extensive network of dermal fibers stained by anti-fibrillin, but not by anti-amyloid P component, anti-vitronectin, or orcein, was seen in an anetoderma lesion. In conclusion, fibrillin immunoreactivity is associated with a unique dermal network, which ultrastructurally is composed of microfibrils. These fibers are proposed to have an important structural and functional role in anchoring the dermal elastic fibers in the extracellular matrix and to the lamina densa.

The prevalence of renal amyloidosis of the AA-type in a series of 1,158 consecutive autopsies.

To determine the prevalence of renal amyloidosis of the AA-type in a defined population, formalin-fixed specimens from the kidneys of all the cases autopsied in 1983 at The General Hospital of Malmö, Sweden, were investigated using immunohistochemical techniques. Amyloid deposits of protein AA were found in 10 of 1,158 investigated cases and the calculated prevalence was 0.86 per cent. The mean age at death of the individuals with the AA-type of amyloidosis was 79 years. Six of the cases with amyloidosis had rheumatoid arthritis. The avidin-biotin-peroxidase complex technique was found to be superior to the immunofluorescence method and a high sensitivity and specificity was achieved when sequence-specific antibodies against a synthetized nonapeptide corresponding to a hydrophilic segment of the polypeptide chain of protein AA were used in the assay. Nine cases with other types of amyloid deposits in the kidneys were also detected. None of these cases showed any AA immunoreactivity but all of them demonstrated Congophilic deposits which were immunohistochemically stained by antibodies against the amyloid P-component. The prevalence of renal amyloidosis comprising all types of amyloid protein deposits was 1.64 per cent.

Fractionation of some bovine whey proteins by recycling gel filtration on a large scale.

Fractionation of bovine whey concentrate was performed by gel filtration on Sephadex G-75 both on a laboratory scale and on a large scale. By a recycling procedure and improved separation was obtained and the whey proteins were resolved into four fractions in the weight ratio 3:12:1:4. The fractions were analysed by polyacrylamide gel (PAG) electrophoresis and the apparent molecular weights were determined by thin layer gel chromatography (TLG) and by sodium dodecylsulfate (SDS) gel electrophoresis.