Pathological process often modifies the structure of the soft tissue and can lead changes of mechanical properties. The regularity of this relationship has already been used in the elastography and currently it is applied in medical diagnostic. Tissue stiffness can be identified by a quick measurement but more accurate details can be obtained only by biopsy. Studies, presented in a scientific literature, focus only on pathological stiffness or consider only changes in biochemical structure. These researches revealed two very important components of those modifications -elastin and collagen. Soft tissues are multicomponent, inhomogeneous and anisotropic structures. Their functionality depends on complicated processes on molecular level. Probably the individual components of the tissue can effect on each other. They may promote creation of processes, which can participate in modifications of elasticity. For this reason, it is very important to relate changes on the structural level with mechanical properties. This information can be very helpful in diagnosis and treatment of soft tissue disease.
Mite allergens belong to the group of inhalant allergens and represent antigenic substances which are particutlarly important in the pathogenesis of respiratory system diseases and skin diseases. The most common diseases associated with chronic exposure to these aeroallergens include: allergic rhinitis, bronchial asthma and atopic dermatitis. Mite allergens are simple proteins or glycoproteins with different molecular structures and various biochemical functions. The sensitizing capacity of these proteins is connected from their physicochemical properties. Individual allergens perform, among others, the functions of structural proteins, act as enzymes, transport lipids, bind metal ions, and are capable of glycosylation. In addition, mite allergenic proteases degrade proteins of the skin epithelium-resulting in a weakening of its natural protective barrier-and induce the immune response. The proteases also induce the release of pro-inflammatory cytokines: interleukin-4 (IL-4), interleukin 6 (IL-6), interleukin 8 (IL-8), eotaxin, and granulocyte-macrophage colony-stimulating factor-GM-CSF. The article presents the tertiary structure of major and mid-range mite allergens and their classification. Based on literature reports concerning the chemical structure of allergenic proteins, it was emphasized that the structural differences between homologous proteins with allergenic pozoproperties relate to the distribution of amino acid residues on the surface of the molecule. IgE binding affinity and the similarities and differences in the amino acid sequence of the allergens were also the basis for determining cross-reactivity of allergenic proteins. The paper shows an example of this phenomenon, describing the existence of common allergens for various mite species.
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