A new role for PGRP-S (Tag7) in immune defense: lymphocyte migration is induced by a chemoattractant complex of Tag7 with Mts1

PGRP-S (Tag7) is an innate immunity protein involved in the antimicrobial defense systems, both in insects and in mammals. We have previously shown that Tag7 specifically interacts with several proteins, including Hsp70 and the calcium binding protein S100A4 (Mts1), providing a number of novel cellular functions. Here we show that Tag7–Mts1 complex causes chemotactic migration of lymphocytes, with NK cells being a preferred target. Cells of either innate immunity (neutrophils and monocytes) or acquired immunity (CD4⁺ and CD8⁺ lymphocytes) can produce this complex, which confirms the close connection between components of the 2 branches of immune response.     

Interaction of chondroitin sulfate with enzymes

Chondroitin sulphate forms noncovalent electrostatic biocatalyst-glycosaminoglycan complexes in the solutions of enzymes. Chondroitin sulphate also interacts with enzymes developing complexes after carbodiimide activation of its carboxylic groups. Relatively low-molecular weight of biocatalysts (chymotrypsin, superoxide dismutase) forms stable noncovalent conjugates with the additional interaction as compared with electrostatic complexes. High-molecular weight of enzymes (acid phosphatase) develops covalent conjugates. Chondroitin sulphate is proposed for covalent binding of large proteins and multi-enzymatic complexes to obtain their stabilized derivatives for medical application.     

Nonenzymatic reduction of Met-Hb under the action of NAD radicals generated in the presence of HAD.H and Fe(II) salts. Antioxidant properties of Met-Hb]

It has been found that superoxide radicals formed at autooxidation of Fe(II) ions or of their complexes with EDTA in the presence of NAD.H cause reduction of met-Hb into deoxy or oxy-form. Under the effect of hydroxyl radicals generated in the ultrasonic field in the presence of NADH reduction of met-Hb into the ferro-form (carboxy-Hb) was observed in Co atmosphere and not in O2 atmosphere. It was induced by a high oxidation rate of oxy-Hb by hydroxyl radicals into met-Hb as compared to carboxy-Hb. Reduction of met-Hb was shown to be accompanied with the formation of NAD+. The role of NAD. radicals in the reduction of met-Hb which acts as an antioxidant in respect to organic free radicals was discussed.     

Age-dependent characteristics of the regulation of cytoplasmic NADP+-dehydrogenases in the liver of rats on different diets

It is established that the activity of malate dehydrogenase and glucose-6-phosphate dehydrogenase in rats aged 1,3 and 12 months lowers under fasting and on high-fatty diet and in old animals (24 months) on a high-fatty diet only the glucose-6-phosphate dehydrogenase activity decreases. When rats after fasting are put on high-carbohydrate diet the activity value of the mentioned enzymes has already returned to the initial level after 12 hours in rats aged 1 and 12 months and in rats aged 3 months it exceeds that activity in intact rats. The rise in the activity of the determined enzymes is completely blocked by the preliminary administration of actinomycin D. The isocitrate dehydrogenase activity remains unchanged under conditions of maintaining animals on different diets.     

Efficiency of Transient Expression in Protoplasts of Various Potato Cultivars

Applied Biochemistry and Microbiology - The production of mesophilic protoplasts of potato (Solanum tuberosum L.) for transient gene expression is a required technological stage in the testing of...     

Post-fire dynamics of humid subtaiga in low mountain part of East Sayan

The results of studying the postfire successional change of light-coniferous and small-leaved forests of the prienisey part of the East Sayan Region are presented based on the landscape ecology approach. A general diagram of the direction and rate of succession changes has been made and analyzed considering the pyrogenous factor.     

Ecdysterone Modulates Antitumor Activity of Cytostatics and Biosynthesis of Macromolecules in Tumor-Bearing Mice

The influence of therapeutic and half doses of cisplatin and adriamycin combination with the anabolic drug ecdysterone (20-hydroecdison) on development of subcutaneously and intraperitoneally transplanted P388 and L1210 leukemia and metastasizing B16 melanoma was studied. Ecdysterone significantly stimulated the chemotherapeutic effect of low doses of the cytostatics: inhibition of tumor growth, mice survival rate, their lifespan, and the antimetastatic activity index were comparable or better than after therapy with high doses of the antitumor drugs. The influence of high and low doses of cisplatin and its low dose in combination with ecdysterone on the dynamics of protein and DNA biosynthesis in the liver, pancreas, thymus, spleen, and adrenals of tumor-bearing mice were also studied. Although the therapeutic effect of 4 mg/kg cisplatin by activated protein biosynthesis and DNA repair is comparable or better than that of its low dose (2 mg/kg) in combination with ecdysterone, in terms of chemotherapy the combination looks preferable since the therapeutic dose of cisplatin is toxic for the intact tissues.     

Human recombinant laminin-binding protein: isolation, purification, and crystallization

The mRNA of the precursor of laminin-binding protein (LBP) was isolated from a human embryo kidney cell line and cloned. The determined sequence of the LBP gene showed complete identity with the LBP genes isolated from human lung and large intestine cells. The human LBP was expressed by E. coli cells, and it was purified using Ni-NTA-Sepharose chromatography. The mobility of the homogeneous recombinant human laminin-binding protein on SDS-PAGE was 43 kD. A mixture of eight murine monoclonal antibodies, the MPLR Pool against LBP, reacted with the recombinant LBP in Western blot. The interaction of the antiidiotypical antibodies 10H10 and E6B provided evidence that the epitope binding to protein E of the tick-borne encephalitis (TBE) virus is also preserved on the human recombinant LBP. Enzyme immunoassay confirmed the ability of the recombinant LBP to interact with protein E of TBE virus. The biological activity of the recombinant LBP allowed us to perform X-ray analysis of the spatial arrangement of the LBP molecule using the recombinant protein. For this purpose, crystals of the human LBP were obtained by the standing drop version of the pore diffusion technique. The crystals appropriate for X-ray structural analysis were 0.3 x 0.1 x 0.05 mm in size. The X-ray diffraction field of the crystal extended to 2.5 A.