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[...]it was not easy to find time for science. The Head of the Department Dr Osmo Jarvi had earlier observed intestinal-type epithelium in tumours of nasal and gastric mucosas and postulated that intestinal metaplasia may play a role in the histogenesis of gastric carcinoma. [...]we collected epidemiological data and observed, for instance, that, among the people living on the slopes of Mount Kilimanjaro, gastric carcinoma was markedly more prevalent than in people in the surrounding areas, and that the intestinal type was especially common in the former group. 4 We speculated that an environmental factor might be the volcanic soil there.

Abstract Phospholipase A2 (PLA2 ) is a key enzyme in the generation of prostanoids that are important mediators of inflammation. Review of recent literature on the involvement of PLA2 in acute pancreatitis (AP). Pancreatic group IB PLA2 mediates local pancreatic cell injury but not distant organ damage. Nonpancreatic group (G) IIA PLA2 is an acute-phase protein that functions in defense against infection and removal of injured cells but is quite harmless to uninjured cells. The concentration of GIIA PLA2 in serum correlates with the severity of AP. PLA2 inhibitors are effective in the therapy of experimental AP but have not penetrated to clinical use as drugs to treat the human disease. Specific immunoassays have been developed for the measurement of both GIB PLA2 and GIIA PLA2 in serum. The former assay is a method suitable for detecting pancreatic injury and the latter to assess the severity of AP.

Group IIA phospholipase A2 (PLA2-IIA) is a newly recognized antibacterial acute phase protein. The concentration of PLA2-IIA increases up to 500-fold in the blood plasma of patients with severe acute diseases, compared with healthy persons. Despite numerous studies, the exact roles of this enzyme in human diseases are unknown. This study investigated the antibacterial properties of PLA2-IIA in human acute phase serum. PLA2-IIA in serum samples of patients with bacterial infections was capable of killing 90% of Staphylococcus aureus and 99% of Listeria monocytogenes in vitro after incubation for 2 h. At concentrations found in normal human serum, PLA2-IIA killed 90% of L. monocytogenes but did not kill S. aureus or Escherichia coli. The bactericidal effects of acute phase and normal human serum were abolished after depletion of PLA2-IIA by immunoadsorption.

COST (European Cooperation in the field of Scientific and Technical Research) is an intergovernmental initiative in science and research intended to promote the coordination of nationally funded research in Europe. Four working groups discuss the housing of animals, their environmental needs, refinement of procedures, genetically modified animals, and cost-benefit analysis. Based on the activities of these working groups, this book provides the European best practices for individuals and institutions working with laboratory animals. The text also discusses the ethical evaluation of experiments and procedures involving animals.

To determine the concentration of group IIA phospholipase A2 (GIIAPLA(2)) in tears of patients with keratoconjunctivitis sicca (KCS) and to compare it with the GIIAPLA(2) content of tears in age-matched healthy controls. The GIIAPLA(2)content of tears was measured with time-resolved fluoroimmunoassay in 20 patients with KCS (mean age 70.7+/-8.7 years) and in 20 normal subjects (mean age 70.2+/-9.9 years). The GIIAPLA(2)content of tears in patients with KCS was 75.8+/-54.2 microg/ml and in normal subjects it was 34.2+/-21.4 microg/ml. The difference was statistically significant. In patients with KCS the GIIAPLA(2) concentration slightly increased with decreasing Schirmer test values (Spearman's correlation =-0.20) The results of this study indicate that in patients with KCS the relative concentration of GIIAPLA(2) of tears was increased due to decreased aqueous production in the lacrimal glands and better preservation of the acinar cells in the central parts of the lobules of the lacrimal glands producing GIIAPLA(2).

To study the diurnal rhythm in group IIA phospholipase A(2) (GIIAPLA(2)) content of tears and the effect of the wearing time of soft contact lenses (CL) on the content of GIIAPLA(2 )in tears. The GIIAPLA(2 )content of tears was measured by a time-resolved fluoroimmunoassay in 22 healthy controls at 8 a.m., noon, 4 p.m. and 8 p.m. and in 20 CL wearers at 4 p.m. 1-2 days before using CLs and after 4 h (at noon), 8 h (4 p.m.) and 12 h (8 p.m.) use of soft CLs. The GIIAPLA(2 )content of tears of healthy controls was 80.6+/-47.8 micro g/ml (mean+/-SD). The GIIAPLA(2 )content was lower at 8 a.m. than at noon (p=0.006) and higher at 4 p.m. than at 8 p.m. ( P=0.003). There was no statistically significant difference in the GIIAPLA(2 )content of tears between the CL wearers without CLs (69.47+/-31.2 micro g/ml) and the normal subjects (92.3+/-48.2 micro g/ml) measured at 4 p.m. Compared with healthy controls, the GIIAPLA(2) values in subjects wearing CLs were statistically significantly lower at noon ( P=0.0001) and at 4 p.m. ( P=0.0002). In normal subjects, the GIIAPLA(2) content of tears increased from 8 a.m. to noon and decreased from 4 p.m. to 8 p.m. The use of CLs for 4 h and 8 h caused a decrease in the GIIAPLA(2) content of tears. This difference was not seen at 4 p.m. the day when the CL wearers did not use CLs.

Cnidarians are the oldest extant lineage of venomous animals. Despite their simple anatomy, they are capable of subduing or repelling prey and predator species that are far more complex and recently evolved. Utilizing specialized penetrating nematocysts, cnidarians inject the nematocyst content or “venom” that initiates toxic and immunological reactions in the envenomated organism. These venoms contain enzymes, potent pore forming toxins, and neurotoxins. Enzymes include lipolytic and proteolytic proteins that catabolize prey tissues. Cnidarian pore forming toxins self-assemble to form robust membrane pores that can cause cell death via osmotic lysis. Neurotoxins exhibit rapid ion channel specific activities. In addition, certain cnidarian venoms contain or induce the release of host vasodilatory biogenic amines such as serotonin, histamine, bunodosine and caissarone accelerating the pathogenic effects of other venom enzymes and porins. The cnidarian attacking/defending mechanism is fast and efficient, and massive envenomation of humans may result in death, in some cases within a few minutes to an hour after sting. The complexity of venom components represents a unique therapeutic challenge and probably reflects the ancient evolutionary history of the cnidarian venom system. Thus, they are invaluable as a therapeutic target for sting treatment or as lead compounds for drug design.

Phospholipase A 2 (PLA 2) is a key enzyme in the generation of prostanoids that are important mediators of inflammation. Review of recent literature on the involvement of PLA 2 in acute pancreatitis (AP). Pancreatic group IB PLA 2 mediates local pancreatic cell injury but not distant organ damage. Nonpancreatic group (G) IIA PLA 2 is an acute-phase protein that functions in defense against infection and removal of injured cells but is quite harmless to uninjured cells. The concentration of GIIA PLA 2 in serum correlates with the severity of AP. PLA 2 inhibitors are effective in the therapy of experimental AP but have not penetrated to clinical use as drugs to treat the human disease. Specific immunoassays have been developed for the measurement of both GIB PLA 2 and GIIA PLA 2 in serum. The former assay is a method suitable for detecting pancreatic injury and the latter to assess the severity of AP.

Group II phospholipase A2 (PLA2-II) is an inflammatory enzyme, which has been shown to be an acute-phase protein and to correlate with the severity of sepsis. In a prospective study, the concentration of PLA2-II in the sera of 46 patients with sepsis and nonseptic bacterial and viral infections was measured by a fluoroimmunoassay. The serum concentration of PLA2-II in patients with infections (median, 164.5 µg/L; range, 5.07–1,740 µg/L) was elevated 46-fold above normal concentrations (median, 3.61 µg/L; range, 1.32–25.25 µg/L). The concentration of PLA2-II was higher in patients with sepsis (median, 284.5 µg/L; range, 12.95–1,574 µg/L) and nonseptic bacterial infections (median, 210.6 µg/L; range, 5.07–1,740 µg/L) than in those with viral infections (median, 46.78 µg/L; range, 11.46–275.9 µg/L) (P = .0042). The concentration of PLA2-II correlated well with the concentration of C-reactive protein (CRP) (r = .613, P = .0001) but not with the concentration of pancreatic PLA2 (r = .089, P = .365). Measuring the serum concentration of PLA2-II is useful as an adjunct to the determination of CRP concentrations for differentiating bacterial from viral infection.

Determines basic blood chemistry parameters in the population of the island of Mauke in the South Pacific. Measures 24 laboratory parameters in serum samples of 502 subjects representing 80.8% of the total population. Source: National Library of New Zealand Te Puna Matauranga o Aotearoa, licensed by the Department of Internal Affairs for re-use under the Creative Commons Attribution 3.0 New Zealand Licence.