[Role of cathepsin D in the appearance of micronuclei in lung cells of mice immunized with influenza vaccine]. / Rol' katepsina D v induktsii mikroiader v kletkakh legkikh myshei, immunizirovannykh vaktsinnym shtammom virusa grippa.

The positive correlation of micronuclei quantity appearance and catepsin D activation in mice cells after immunization by alive influenza vaccine was demonstrated. Activation of proteinase precedes chromosomal aberrations. Catepsin D activation is supposed to lead to proteolysis in achromatic apparatus which results in micronuclei formation.

[The mechanism of action of hydrocortisone and adrenaline on the hepatic lysosomal apparatus]. / K mekhanizmu deistviia gidrokortizona i adrenalina na lizosomal'nyi apparat pecheni.

The mechanisms of hydrocortisone and adrenalin action on the structure and function of the lysosomal-vacuolar cell apparatus were studied in experiments on liver sections of Wistar rats. The sections were incubated in Krebs-Ringer bicarbonate buffer, pH 7.4 (95% O2 and 5% CO2) at 37 degrees C for 2 h. Hydrocortisone (10(-5) M) and adrenalin (10(-4) M), added to an incubation medium, were shown to produce a labilizing effect on lysosomal membranes, increasing free activity of acid phosphatase and cathepsin D and osmotic sensitivity of lysosomes. alpha-adrenergic blocker dihydroergotamine (3.4 x 10(-5) M) blocked an increase in free activity of acid phosphatase as a result of adrenalin action but did not eliminate hydrocortisone labilizing action. beta-adrenergic blocker propranolol (3 x 10(-4) M) lowered free activity indices and osmotic sensitivity of lysosomes to control values both in the presence of adrenalin and hydrocortisone. The labilization of lysosomal membranes in liver sections was also observed after adding dibutyril-cAMP (10(-8) M) or monobutyril-cGMP (10(-13)-10(-9) M) into the incubation medium.

[Effect of the antitumor preparations prospidin and spirobromin on the function of the liver lysosomal apparatus in mice]. / Vliianie protivoopukholevykh preparatov prospidina i spirobromina na sostoianie lizosomal'nogo apparata pecheni myshei.

Antitumour drugs prospidine and spirobromine were shown to suppress the activity of the mouse liver lysosome enzymes in vivo and in experiments in vitro. The revealed effect was underlied by a decrease of lysosomal membrane permeability for the corresponding substrates and enzymes rather than a reduction of the catalytic activity of acid hydrolases.

[Effect of nutrition on lysosomal function during physical loading]. / Vliianie pitaniia na sostoianie lizosom pri fizicheskoi nagruzke.

Changes of cardiac, sceletal and hepatic lysosomes effected by three different variants of balanced isocaloric diets: 1--basic, 2--protein-lipid and 3--carbohydrate, with ratios of proteins, lipids and carbohydrates in mass 1.0:0.35:2.6; 1.0:0.48:0.67; and 1.0:1.3:10.9, respectively, were studied. Activities of enzymes participating in degradation of carbohydrates (beta-glucosidase, beta-N-acetyl-glucosaminidase) were more increased in the animals fed with the carbohydrate diet. Activation of proteolytic enzymes (cathepsin D) was observed in tissues of rats taking the protein-lipid food. As a rule physical exercise exerts lysosomal enzymes activation and their membrane labilization in rats maintained on the basic diet. Reversial reactions of lysosomes to physical exercise is observed in animals receiving the carbohydrate diet for along time that is expressed in increasing the total activity of lysosomal hydrolases and stabilizing the lysosomal membranes. On the contrary, maintaining the animals on the protein-lipid diet is followed by a more pronounced activation of the lysosomal apparatus of tissues as compared to the basic diet.

[Effect of glucocorticoids and catecholamines on the state of the tissue lysosomal apparatus in rabbits with experimental diabetes]. / Vliianie gliukokortikoidov i katekholaminov na sostoianie lizosomal'nogo apparats tkanei krolikov s éksperimental'nym diabetom.

Administration to rabbits of hydrocortisone (8 mg/kg) and adrenaline (0.3 ml of 0.1% solution) during mild dithizone diabetes simulated hormonal reconstructions of the body exposed to stress. Activation of the cellular lysosomal apparatus occurs in such hormonal situation. In the liver this in manifested by an increase in the acid phosphatase, cathepside D, and beta-glucosidase free activity and by reduction in the resistance of lysosomal membranes to the effect of osmotic shock. Increase in the total acid hydrolase activity was detected in the cardiac and skeletal muscles.

[Functional and ultrastructural lysosome changes in surviving rat liver sections as affected by blood serum lipoproteins]. / Funktsional'nye i ul'trastrukturnye izmeneniia lizosom v perezhivaiushchikh srezakh pecheni krys pod vliianiem lipoproteidov syvorotki krovi.

Using surviving rat liver slices, the influence of blood serum lipoproteins on cellular lysosomes was studied. Lipoproteins were isolated by the preparative isopicnic ultracentrifugation method. Apoproteins were separated by means of delipidation of suitable lipoprotein fractions. After preincubation of liver slices in media with high density lipoproteins (HDLP), low and very low density lipoproteins (LDDLP, VLDLP), apo-HDLP and apo-VLDLP, the rise of free acid hydrolase activities was seen. The stability of lysosomes in hypotonic solutions turned out to be low, and the tendency to lysosomal aggregation increased. Typical peribiliary localization of lysosomes in the cell remained unchanged. Following preincubation of liver slices with hydrocortisone, adrenalin and VLDLP or LDLP, the rise of free lysosomal enzyme activity, greater aggregation and lysosome polymorphism and their less osmotic resistance took place. After liver slice preincubation with hormones and HDLP, besides all of these changes, the lysosomal translocation to the nuclei was seen. When apoproteins, separately or together with hormones, were added, the same type of alteration of lysosomal membranes occurred. Our results suggest an importance of lipo (apo) proteins in the control of structure and functions of cellular lysosomal apparatus.