Extracellular heat shock protein with molecular weight of 70 kDa is a signal molecule of the immune system. It is secreted by the peripheral blood, liver and muscle cells in response to physiological, thermal, and mental stresses. The main goal of our study was to compare the levels of expression of heat shock protein (70 kDa) matrix ribonucleic acid in leukocytes and serum concentrations of the protein before and after physiological stress. In order to solve this problem, we developed enzyme immunoassay of serum heat shock (70 kDa) protein concentration and a method for evaluating the expression of matrix ribonucleic acid of this protein in leukocytes by the real time PCR. The concentration of 70 kDa heat shock protein in the serum increased 1.7 times as a result of even a short-term highly intense physiological stress, while the expression of its matrix ribonucleic acid in leukocytes increased 1.5 times. The individual features determine the response to physiological stress. Probable sources of 70 kDa heat shock protein are discussed.

Heat shock-binding protein HspBP1 is a member of the Hsp70 co-chaperone family. The interaction between HspBP1 and the ATPase domain of the major heat shock protein Hsp70 up-regulates nucleotide exchange and reduces the affinity between Hsp70 and the peptide in its peptide-binding site. Previously we have shown that Tag7 (also known as peptidoglycan recognition protein PGRP-S), an innate immunity protein, interacts with Hsp70 to form a stable Tag7-Hsp70 complex with cytotoxic activity against some tumor cell lines. This complex can be produced in cytotoxic lymphocytes and released during interaction with tumor cells. Here the effect of HspBP1 on the cytotoxic activity of the Tag7-Hsp70 complex was examined. HspBP1 could bind not only to Hsp70, but also to Tag7. This interaction eliminated the cytotoxic activity of Tag7-Hsp70 complex and decreased the ATP concentration required to dissociate Tag7 from the peptide-binding site of Hsp70. Moreover, HspBP1 inhibited the cytotoxic activity of the Tag7-Hsp70 complex secreted by lymphocytes. HspBP1 was detected in cytotoxic CD8؉ lymphocytes. This protein was released simultaneously with Tag7-Hsp70 during interaction of these lymphocytes with tumor cells. The simultaneous secretion of the cytotoxic complex with its inhibitor could be a mechanism protecting normal cells from the cytotoxic effect of this complex.

Stabilometric parameters were compared in sportsmen of various disciplines (biathlon, boat racing, judo, and water polo). A decrease in the role of gravitational factor in sport activity was accompanied by the impairment of balance characteristics, which remained within normal limits of the mean population level.

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Molecule L1CAM is specific for nerve cells and tumors of various localizations. The expression of L1CAM is significantly higher in melanoma in comparison with benign nevi and correlates with the progress of melanoma and transition from radial to vertical growth. Monoclonal antibodies to L1CAM effectively and specifically attenuate melanoma growth, though stimulates the epithelial-mesenchymal transition. shRNA-mediated knock-down of L1CAM showed the involvement of L1CAM in regulation of activity of the canonical Wnt pathway and expression of genes of class I melanoma-associated antigens (MAGE).