Water status and LPO in rat tissues during massive blood loss and irradiation with He-Ne laser.

We revealed a relationship between water balance and LPO in the myocardium, liver, and blood plasma during massive blood loss and irradiation with He-Ne laser. Low-intensity laser irradiation of the plasma inhibits LPO and normalizes water balance in rat tissues during massive blood loss.

[Various forms of water in the rat myocardium and liver during blood loss and the early postresuscitation period]. / Zakonomernosti izmeneniia razlichnykh form vody v miokarde i pecheni krys pri krovopotere i v rannem postreanimatsionnom periode.

Different forms of water content were studied in myocardium and liver of male rats at 2-h hypotension and during the early postreanimation period. The phenomenon of redistribution of free and bound water was found. Comparison of water balance during the postreanimation period in the myocardium and liver revealed that normalization of different forms of water occured in myocardium. In hepatocytes oedema remained over the whole period studied.

Some biochemical characteristics and water exchange in human articular cartilage in osteoarthrosis.

Rearrangement of intra- and intermolecular bonds in collagen molecule, disaggregation of proteoglycans and their elimination from cartilage involved in osteoarthrosis are responsible for water accumulation and its increased mobility in cartilage.

Biochemical characteristics and water exchange in the surface layer of human joint cartilage.

We compared the contents of collagen, glycosaminoglycans, and various forms of water in the surface layer and whole tissue of joint cartilages of different localization. It was found that the surface layer is characterized by reduced content of glycosaminoglycans compared to the whole tissue and higher water-holding capacity due high content of bound water.

[Changes in biochemical characteristics of collagen and the cartilage water in osteoarthritis]. / Izmenenie biokhimicheskikh kharakteristik kollagena i sostoianiia vody khriashcha pri osteoartrite.

The stability of collagen molecules and moisture capacity of human normal and osteoarthrotic (OA) cartilage were studied before and after extraction of glycosaminoglycans (GAG) by 4M guanidinum chloride. The content and nature of water were determined by Fisher titration, DSC and analysis of sorbtion-desorbtion processes of water vapour in cartilage. The stability of collagen molecules was determined by the degree of enzymatic hydrolysis: collagenase, pronase and pepsin. It was found that weakening of bonds between main compounds of the cartilage matrix and decrease of GAG quantities in the OA cartilage were accompanied by structural disorganization of the collagen network, which is manifested by breakdowns of intramolecular bonds in telopeptides and intermolecular bonds in the spiral part of collagen molecules, these changes may contribute to increase of total water in OA cartilage. The correlation of free and bound water fractions in cartilage was increased from 5 to 44 in OA cartilage. These results can be used as a criterion of pathological condition of human articular cartilage.

[Water-exchange processes in hyaline cartilage and its basic components in a normal state and in osteoarthritis]. / Vlagoobmennye protsessy v gialinovom khriashche i ego osnovnykh komponentakh v norme i osteoartroze.

The content of different forms of tissue water was studied in the normal articular cartilage and osteoarthrosis cartilage and its structural components: collagen, potassium hyaluronate, sodium chondroitinsulphate and its complexes. In the components of cartilage matrix a few of fractions of bound water different in the strength of binding are present. At the maximal humidity, all water in collagen binds with the active groups of biopolymers and in the glycosaminoglycans, in addition to bound water, are present, two crystal forms of freezing water (free water) at least. The quantity of free water in the collagen-chondroitin sulphat membrane, is increased with the increase of chondroitin sulphate. In the collagen-hyaluronate complex, fraction of free water is found only at the low concentration of hyaluronate kalium. It was shown that in the hyalin cartilage, in different from the other connective tissue (skin, achilles tendon), the most part of water is free water and its quantity is increased in the osteoarthrosis. It is supposed that the rearrangement of binding and free-water fractions in the osteoarthrosis is the result of deficiency of hyaluronic acid and therefore this may be regarded in the improvement of methods of treatment. This scientific and methodical approach allow to receive information on the forms and binding energy of water in the biological tissues, which is absorbed from fluids and steam phase and determine characters of the pathological changes.

[Lung diseases among inhabitants of cities with microbiological and petrochemical industries discharging industrial waste]. / Zabolevaniia legkikh v usloviiakh zalpovykh promyshlennykh vybrosov v atmosferu v gorodakh mikrobiologicheskoi i neftekhimicheskoi promyshlennosti.

Outbreaks of diseases caused by toxic waste discharge took place in some cities where microbiological and petrochemical plants are located. The diseases manifested clinically with pulmonary edemas, irritative and intoxication syndromes and affected only subjects with chronic nonspecific lesions of the lungs. A hypophysis on bronchial asthma outbreaks secondary to paprin discharges in the atmosphere by microbiological plants was not confirmed.

[The effect of ionizing radiation on human muscle tissue]. / Vliianie ioniziruiushchei radiatsii na myshechnuiu tkan' cheloveka.

The effect of ionizing radiation (gamma-irradiation of 60Co, doses from 10 Gy to 15 kGy) on human muscle tissue was studied using a biopsy material. Destructive alterations in muscle proteins were observed beginning from the dose of 1.0 kGy: appearance of new protein fractions with molecular mass 68-160 kDa and 18-36 kDa. Resistance of muscle proteins to the trypsin effect was unaltered, while the rate of pronase-induced hydrolysis was slightly increased, about 1.2-fold. Content of water and biomechanical properties of the tissue were unaltered, but the modulus of elasticity was decreased approximately 3-fold after treatment with maximal doses of the ionizing radiation used.

[Proton magnetic resonance spectra of bound water in muscles]. / Spektry protonnogo magnitnogo razonansa sviazannoi vody v myshtse.

The state of water in a muscle tissue was investigated using 1H-NMR. Water spectra in the muscle were found after holding it out at variable humidity and after the muscle species had been pressed with different effort. The NMR-spectra demonstrated the existence of two different water fractions with poor exchange between them. One of them was associated with structured water in the sarcoplasm connected with the contractile proteins. The second fraction was related with the myoplasm. The absorption isotherms for two fractions of water were observed.

[The structure and physicochemical properties of human hyaline cartilage in the disorganization of the carbohydrate-protein complexes of the ground substance]. / Struktura i fiziko-khimicheskie svoistva gialinovogo khriashcha cheloveka pri dezorganizatsii uglevodno-belkovykh kompleksov osnovnogo veshchestva.

In the experiments in vitro we studied the influence of the process of disorganization of the carbohydrate-protein complexes of the ground substance on the structure, water content and biomechanical properties of the human hyaline cartilage. It was shown that the disorganization process of the cartilage ground substance and the subsequent removal of the formed products resulted in the increasing porosity of the cartilaginous tissue. This is expressed in the exposure of the fibrillar frame of the cartilage and formation of cavities of various volumes between its elements. The mentioned changes of the cartilage structure are followed by the reduction of the amount of monomolecular-bound water and simultaneous increase in swelling in water and water vapor sorption at maximal relative humidity. The removal of about 25% of glycosaminoglycanes of the ground substance resulted in the reduction of the rigidity of the cartilagenous tissue, and the increase in the residual deformation. The examination of the hyaline cartilage did not reveal any interrelation between the contents of proteoglycanes and the water content of the cartilagenous tissue.

[Physico-chemical properties of head hair of people of European and Negroid races]. / Fiziko-khimicheskie svoistva volos golovy liudei evropeoidnoi i negroidnoi ras.

Comparative studies of head hair obtained from europeoid and negroid people showed no difference in water and sulfur content, resistance to temperature exposure and alkaline solution as well as in electrophoretic distribution of keratin proteins. At the same time values of rupture loads and extension as well as value of curl elasticity of negroid people's hair surpass substantially the same characteristics of europeoid people's hair.

[Effect of ionizing radiation on the structure of the collagen fibers of human tendons]. / Vliianie ioniziruiushchei radiatsii na strukturu kollagenovykh volokon sukhozhilii cheloveka.

In studying the effect of ionizing radiation on the properties of human Achilles tendon collagen fibres, the following parameters were analyzed: hydrothermal contraction temperature, module of elasticity, the number of cross-links, free and bound water levels, acids-soluble fraction content, and ultrastructure. With radiation doses of 2-10 Gy no changes in the collagen status were noted. An increased (from 5 to 25 Gy) radiation dose caused changes in physicochemical properties which was indicative of the formation, in the connective tissue collagen, of radiation-induced intermolecular cross-links stabilizing the biopolymer structure.

[Calorimetric study of collagen hydration]. / Kalorimetricheskoe issledovanie gidratsii kollagena.

Water in human Achilles tendon was studied by differential scanning calorimetry. It was shown that in the postmortem period there takes place a redistribution of free and bound water. The quantity of free freezing water in the tissue increases, whereas that of bound unfreezing water diminishes. The data obtained can be used for organ and tissue conservation and in forensic studies.

[Structure and properties of the collagen complex of tendons following disorganization of the connective tissue ground substance]. / Struktura i svoistva kollagenovogo kompleksa sukhozhiliia pri dezorganizatsii osnovnogo veshchestva soedinitel'noi tkani.

Scanning and transmission electron microscopy, as well as physicochemical research methods were used to study the structure and characteristics of the tendon collagen complex during enzymatic distintegration of basal substance of connective tissue. Disintegration of basal substance was shown to be accompanied by substantial derangement of the microstructure of collagen fibers and to entail changes in the modulus of elasticity and residual deformation of the collagen complex with its ability to hydration in a aqueous medium to be increased. The physiochemical and rheological characteristics of the collagen complex were found to be affected to a considerable degree by structural changes occurring in collagen fibers. These changes consist in the formation of a retiform structure containing numerous macrospores.

[Effect of autolysis on the physico-chemical properties of mammalian skin]. / Vliianie autoliza na fiziko-khimicheskie svoistva kozhnogo pokrova mlekopitaiushchikh.

Alterations in physico-chemical properties and in content of several biochemical components were found in skin during postmortal storage of the tissue at the temperature 22 degrees and 5 degrees and relative moisture 92%. Within 96-120 hrs of the postmortal storage a decrease in content of hydrate-bound water and of glycosaminoglycans occurred in the tissue. The alterations were accompanied by an increase in temperature of hydrothermic denaturation and in module of elasticity of the skin. As a result of autolysis solubility of collagen in water was increased at 65 degrees and its acid soluble fractions tended to become denatured although the content of hydroxyproline was unaltered. The processes occurring in the skin within the first period after death, might be considered as a two-step sequence: formation of additional interstructural hydrogen bonds and structure transformation of both collagen and glycosaminoglycans due to the effect of proteinases.

[Structural-mechanical properties and swelling of the protein complexes of hyaluronate and protein-chondroitin-4-sulfate]. / Strukturno-mekhanicheskie svoistva i nabukhanie belkovykh kompleksov gialuronata i protein-khondroitin-sul'fata.

It was shown that the mechano-structural strength and swelling of gels consisting of gelatine and potassium hyaluronate (PH) or potassium protein-chondroitin-4-sulphate (PPCS) depended on the correlation of the components. Low PH and PPCS concentrations showed a minimal mechano-structural strength and a maximal swelling of gels. In the zones of neutralization of the positive electrical charges of gelatine by macropolyanions a high mechano-structural strength coincided with a minimal swelling. With high PH concentrations the mechano-structural strength and swelling of gels became equal to those of pure gelatine; and with high PPCS concentrations there was noted an additional parallel increase in the strength and swelling of gels.