PubMed Health⌕ Search

Biomedical subjects

L V Kravchenko

Publications and source records attributed to L V Kravchenko.

At least 55 records · Page 3Linked to original sources
PubMed1976

Effect of long-term starvation on the rat liver lysosomes.

The effect of 120- and 240-h starvation on rats hepatocytes ultrastructure and particularly the changes of the lysosomes were studied. Eelectronmicroscopically and cytochemically there have been observed diminution of the number of mitochondria and degranulation and vacuolzation of the ER. At the same time Golgi complex was hypertrophied and the number of lysosomes was much increased, mainly those of the autophagic type. Biochemically was shown, that the activity of some acid hydrolases (beta-glucosidase, alpha- and beta-galactosidases, beta-N-acetylglucosaminidase, beta-glucuronidase and arylsulphatases A and B) in the liver of starved rats was markedly expressed. The sedimentation properties of the lysosomes and the lysosomal membrane stability was damaged as well. The data received have been discussed in the light of the reconstructive role of lysosomes.

Acetylglucosaminidase↗
PubMed1975

Action of the mycotoxin of Fusarium sporotrichiella v. sporotrichioides on lysosomal membranes.

The effect of the mycotoxin of Fusarium sporotrichiella v. sporotrichioides (sporofusarin) was studied in vitro on the total and nonsedimenting activity of eight lysosomal enzymes: acid ribonuclease, aryl sulfatases A and B, beta-glucuronidase, alpha- and beta-galactosidases, beta-glucosidase, beta-acetylglucosaminidase, and alpha-mannosidase. Incubation of a suspension of rat liver lysosomes with an aqueous solution of sporofusarin led to inhibition of the total activity of the membrane-bound lysosomal enzyme beta-glucosidase. In a dose of only 1.6 x 10-5 M sporofusarin caused a significant increase in the nonsedimenting activity of nearly all the enzymes; in a concentration of 1.6 x 10-3 M most of the enzymes of the lysosomal matrix (beta-glucuronidase, beta-galactosidase, aryl sulfatases A and B) were liberated almost completely into the supernatant, and nearly all the beta-glucosidase also was liberated. It is postulated that damage to the subcellular membranes is an important component of the toxic action of sporofusarin.

Animals↗
PubMed1975

[The effect of sporofusarin on the cell membranes of isolated perfused liver].

A study was made of the effect of sporofusarin (mycotoxin produced by Fusarium Sporotrichiella v. Sporotrichoides) on the functional activity and permeability of cell membranes of the isolated perfused rat liver. Sporofusarin (in the end concentration of 5.9 . 10(-5) M) produced a marked depressive effect on the rate of bile, formation, urea synthesis and oxygen consumption, and also caused an early and marked disturbance of permeability of the lysosomal and plasma membranes of hepatocytes (an increase in the activity of the enzymes--beta-acetylglucosaminidase, beta-glucuronidase, arylsulfatases A and B, beta-galactosidase in the supernatant fluid of liver homogenate and in the perfusata). It is supposed that depression of the functional activity of the liver under the effect of sporofusarin resulted from damage of the membrane structures of the cell, and, primarily, of lysosomes.

Acetylglucosaminidase↗
PubMed1975

[Morphologic and biochemical heterogeneity of lysosomes].

By means of isopycnic centrifugation in the continuous density gradient of sucrose two subfractions of lysosomes were isolated from rat liver homogenates: a "light" one (with the floating density p=1.13) and a "heavy" one (p=1.24). Electron microscopic, enzymatic and electron microscope enzymatic analysis of the isolated subfractions showed that the "light" subfraction consisted mainly of newly-formed primary lysosomes, while the "heavy" one was presented by secondary lysosomes. Parallel biochemical investigations demonstrated a considerable enzymatic heterogeneity of the two lysosomal subfractions: the "light" subfraction was characterized by a high specific activity of acid DNase, acid RNase and beta-galactosidase, and by almost total absence of beta-glucosidase activity, while the "heavy" one was characterized by a high specific activity of beta-glucosidase, beta-glucuronidase and beta-N-acetylglucosaminidase. Possible causes of enzyme heterogeneity of rat liver lysosomes are discussed.

Acetylglucosaminidase↗
PubMedDate not supplied

Dietary selenium protects against acute toxicity of T-2 toxin in rats.

The efficacy of dietary selenium (Se) supplementation on acute toxicity of T-2 toxin was investigated. Wistar male rats were divided into six groups with 15 rats in each and fed for 6 weeks ad libitum a semi-synthetic diet containing either 0.03 (groups 1 and 2), 0.5 (groups 3 and 4) or 2.5 mg Se/kg (groups 5 and 6). By the end of the experiment the rats in groups 2, 4 and 6 were administered once per os 3.8 mg/kg body weight T-2 toxin, while the animals in groups 1, 3 and 5 received equal doses of the solvent. Twenty-four hours after administration of the toxin the surviving rats were sacrificed and the liver microsomes isolated and determined for activities of enzymes relating to xenobiotics metabolism and Se. The results showed that feeding the rats 2.5 mg Se/kg diet increased the deethylation rate of 7-ethoxycoumarin by 42% and slightly decreased (20%) glutathione-S-transferase activity. Twenty-four hours after the administration of T-2 toxin the lethality percentages in groups 2, 4 and 6 were 47%, 27% and 20%, respectively. Furthermore, administration of T-2 toxin to group 6 rats resulted in a significant decrease in the level of cytochrome P-450 and 7-ethoxycoumarin deethylase activity (to 78% and 51%, respectively) compared to the control group. At the same time a 72% increase in the UDP-glucuronosyltransferase activity and of 61% in epoxide hydrolase activity compared to the control group was found. Similarly, although somewhat smaller, changes were seen in the group 4 rats receiving 0.5 mg Se/kg diet.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗