BackgroundBreast cancer is the most frequent localization of malignant process in American women and women of European countries. To date it is not possible to control the morbidity growth due to lack of effective ways of primary prevention. Comparing the incidence of breast cancer in developed countries with the countries of Asia and Africa, there is the fact of population predominance lesion in more urbanized countries. This suggests that the environment along with other factors, occupies a significant place in the initiation and progression of breast neoplasia. The impressive rates of industrial development led to the pollution of soil, surface water and, as a consequence, food by heavy metal salts.The purposes of this paper are as follows: the chemical composition determination of neoplastic breast tissue, evaluation of the DNA methylation level, study of prognostic-important receptors expression in the breast cancer cells, establishing linkages between all the derived indicators.MethodsIn our study we used the following methods: studying of the chemical composition of breast cancer tissue by atomic absorption spectrophotometry and energy-dispersion spectrometer; іmmunohistochemical study of ER, PR, HER2/neu, p53, Ki-67, E-cadherin and MGMT receptors; DNA extraction and investigation by oscillating infrared spectroscopy method.ResultsThe total amount of heavy metals in breast cancer tissue ranged from 51.21 × 10−3 to 84.86 × 10−3 μg/kg. We have got the following results: the growth of heavy metals in neoplastic tissue is accompanied with the increase of HER2/neu, p53, Ki-67, MGMT expression and decrease of ER and PR expression. The increment of pathological DNA methylation is accompanied with the increasing amount of heavy metals in tumor tissue.ConclusionsHeavy metals through different pathogenetic links stimulate the progression of breast cancer and reduce its sensitivity to treatment. DNA of tumor tissue has a different level of methylation which changes with the amount of heavy metals in cancer cells. This is displayed on the synthesis of prognostically important receptors in neoplastic tissue.

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PurposeThe purpose of this paper is to describe the research results of the morphological structure of white laboratory rats’ tongue at the macro-, micro-, and ultrastructural levels by scanning, light, and transmission electron microscopy.ResultsOur results show that the tongue of these rats has a number of unique morphological features that are different from the tongue of other rodents consequently to allow identifying their species-specific features.ConclusionsOur findings have shown the features of the tongue structure of white laboratory rats at micro-, macro-, and ultrascopic levels. The data analysis revealed that mucous membrane of the tongue contains a large number of papillae, such as fungiform, filiform, foliate, vallate, and multifilamentary papillae. Each has a different shape, size, and location. The tongue’s morphological feature consists of three types of filiform papillae, well-developed foliate and multifilamentary papillae, as well as one large and similar smaller circumvallate papillae. The muscle of the tongue contains a large number of mitochondria of different shapes and sizes. However, we have received data for a complete picture of structure of this organ that will be useful in further experimental and morphological studies of the white laboratory rats.

Streptococcus agalactiae, also known as group B Streptococcus (GBS), is the major cause of neonatal sepsis in humans. A critical step to infection is adhesion of bacteria to epithelial surfaces. GBS adhesins have been identified to bind extracellular matrix components and cellular receptors. However, several putative adhesins have no host binding partner characterised. We report here that surfaceexpressed b protein of GBS binds to human CEACAM1 and CEACAM5 receptors. A crystal structure of the complex showed that an IgSF domain in b represents a novel Ig-fold subtype called IgI3, in which unique features allow binding to CEACAM1. Bioinformatic assessment revealed that this newly identified IgI3 fold is not exclusively present in GBS but is predicted to be present in adhesins from other clinically important human pathogens. In agreement with this prediction, we found that CEACAM1 binds to an IgI3 domain found in an adhesin from a different streptococcal species. Overall, our results indicate that the IgI3 fold could provide a broadly applied mechanism for bacteria to target CEACAMs.