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The recent data about characteristics and of different are presented and discussed.
EN
Mast cells (MC) are found widely distributed in tissues and contribute to regulation of inflammatory responses and ongoing modulation of the tissues. Although MC are important in a variety of processes including innate immunity, their role in allergic disease has received increasing attention in the past decade. MC are located throughout the human body and upon allergen exposure they are stimulated via the IgE receptor (FceRI) to release several proinflammatory mediators such as tumor necrosis factor (TNF), reactive oxygen species such as nitric oxide (NO), proteases, and lipid-derived mediators. However, we now recognize that MC can be activated by a variety of mechanisms and that mediator release is a consequence of several intra- and extracellular signals. Some of these mechanisms, such as Fc receptor aggregation and proteinase activated receptor (PAR)-mediated activation facilitate and augment local inflammatory responses. Other mechanisms, such as interferon gamma (IFN-gamma) induction of nitric oxide (NO) may inhibit MC function and downregulate inflammatory responses. Increased understanding of these complex pathways has encouraged the development of therapies for allergic inflammation that target specific MC functions and mediators. Some novel strategies include oligonucleotides that induce or inhibit the production of specific mediators. Such approaches may yield useful therapies for allergic individuals in the near future.
EN
Burgeoning scientific literature proves that enzymes can catalyze chemical reactions in non-conventional media, are active against liquid, solid or gaseous substrates, retain their catalytic function in organic solvents, biphasic systems composed of organic solvent and water and supercritical fluids. Non-aqueous media appeared to be a promising alternative as an environment for the reactions catalyzed by enzymes. The possibility of carrying out enzymatic processes in such unusual milieus enlarged the range of applications of biocatalysis, and solved many problems witnessed by pharmaceutical, food and chemical industries. The paper describes both advantages and disadvantages of non-conventional media, and presents the examples of practical uses of selected enzymes (lipases, proteases, oxidoreductases, glycosidases) in these systems. The details on medium composition and the form of the biocatalyst are included.
EN
Sjogren syndrome (SS) is an autoimmune disease characterized by diffuse lymphoid cell infiltrates in the salivary and lacrimal glands, resulting in symptoms of dry mouth and dry eye due to insufficient secretion. Although it has been assumed that a combination of immunologic, genetic and environmental factors may play a key role on the development of autoimmune lesion in the salivary and lacrimal gland, little is known about the disease pathogenesis. We have identified the 120 KD -fodrin as an important autoantigen on the development of SS in both animal model and SS patients, but the mechanism of -fodrin cleavage leading to tissue destruction in SS remains unclear. Tissue-infiltrating CD4+ T cells purified from the salivary glands bear a large proportion of Fas ligand and the salivary gland duct cells possess apoptotic receptor Fas. Anti-Fas antibody-induced apoptotic salivary gland cells results in specific -fodrin cleavage to the 120 KD fragment in vitro. Preincubation with a combination of calpain and caspase inhibitor peptides could be responsible for inhibition of the 120 KD -fodrin cleavage. Thus, an increase in apoptotic protease activities may be involved in tha progression of -fodrin proteolysis and tissue destruction in the development of SS.
EN
The antibacterial activity of immune haemolymph Galleria mellonella directed against Escherichia coli D31 was destroyed by Pseudomonas aeruginosa crude proteolytic fraction. This was demonstrated by diffusion well assay and acid gel electrophoresis and subsequent bioautography. On the contrary, lysozyme activity appeared to be insensitive to extracellular proteases of P. aeruginosa when activity was determined using the bioautography method. In addition, no change in lysozyme protein level was observed by immunoblotting with specific antibodies directed against G. mellonella lysozyme, which confirmed that lysozyme was not degraded by the crude proteolytic fraction of P. aeruginosa. However, a significant decrease of lysozyme activity in naive and immune haemolymph exposed to the action of P. aeruginosa proteins determined by using diffusion well assay was observed. Mechanisms of the observed inhibition require further studies.
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