scholarly journals Evaluation of Cysteine Metabolism in the Rat Liver and Kidney Following Intravenous Cocaine Administration and Abstinence

Antioxidants ◽  
2021 ◽  
Vol 10 (1) ◽  
pp. 74
Author(s):  
Danuta Kowalczyk-Pachel ◽  
Małgorzata Iciek ◽  
Anna Bilska-Wilkosz ◽  
Magdalena Górny ◽  
Joanna Jastrzębska ◽  
...  
Keyword(s):  
Rat Liver ◽  
Biological Action ◽  
Glutathione Metabolism ◽  
Self Administration ◽  
Cocaine Administration ◽  
Cysteine Metabolism ◽  
Liver And Kidney ◽  
Activity Of Enzymes ◽  
Drug Abstinence ◽  
The Impact

Many toxic effects of cocaine are attributed to reactive oxygen species (ROS) generated during its metabolism. Recently, it has been suggested that the biological action of ROS is often confused with endogenously generated reactive sulfur species (RSS). The aim of this study was to evaluate the impact of cocaine on thiols and RSS in the rat liver and kidney in the drug self-administration (SA) paradigm and the cocaine yoked delivery model (YC) followed by drug abstinence with extinction training. The level of thiols as well as RSS formed during anaerobic metabolism of cysteine and sulfate were assayed. In addition, the activity of enzymes involved in RSS formation and glutathione metabolism were determined. In the liver, following direct cocaine administration (SA and YC), the RSS levels decreased, while in the kidneys, cocaine increased the RSS contents in both groups. These changes were maintained in these tissues during drug abstinence. The level of sulfates was changed by cocaine only in the liver. In the kidney, cocaine shifted cysteine metabolism towards an anaerobic pathway. Our study demonstrates for the first time the changes in cysteine metabolism and thiol levels in the liver and kidney of rats after cocaine self-administration and abstinence.

scholarly journals Cysteine Metabolism and Oxidative Processes in the Rat Liver and Kidney after Acute and Repeated Cocaine Treatment

PLoS ONE ◽  
2016 ◽  
Vol 11 (1) ◽  
pp. e0147238 ◽  
Author(s):  
Danuta Kowalczyk-Pachel ◽  
Małgorzata Iciek ◽  
Karolina Wydra ◽  
Ewa Nowak ◽  
Magdalena Górny ◽  
...  
Keyword(s):  
Rat Liver ◽  
Cysteine Metabolism ◽  
Liver And Kidney ◽  
Oxidative Processes

ASSESSMENT OF GRAY FOREST SOIL ENZYMATIC ACTIVITY IN AGRICULTURAL SYSTEMS

2019 ◽  
Keyword(s):  
Enzymatic Activity ◽  
Environmental Sustainability ◽  
Hydrolytic Enzymes ◽  
Invertase Activity ◽  
Phosphorus Cycle ◽  
Soil Enzymatic Activity ◽  
Urease Enzyme ◽  
Natural Analogues ◽  
Activity Of Enzymes ◽  
The Impact

On the grey forest medium-loamy soil of Vladimir Opolye region we have studied the impact of various methods of basic cultivation and fertilizer systems on the activity of redox and hydrolytic enzymes: ure-ase (nitrogen cycle), invertase (carbon cycle), phosphatase (phosphorus cycle), and catalase, involved in the cycle of carbon in the soil. The second humus horizon with capacity of 19-24cm was found at the depth of 20 - 21 cm on the experimental field. We have studied three modes of basic soil cultivation: an-nual shallow flat plowing (6-8 cm), annual deep flat plowing (20-22 cm), and annual moldboard plowing (20-22 cm) with normal and intensive application of fertilizers. The most enzymatically active layer is 0-20 cm. No relevant difference has been found in the level of enzymes activity between variants of basic soil treatment. Activity of enzymes increases with application of fertilizers on the intensive background. In agrogenic soils, soil enzymatic activity is lower on average by 16-22% compared to the soil of the res-ervoir. The biggest negative transformation of activity has been observed at the urease enzyme (up to 50%). With annual moldboard plowing on the intensive backgroung, enzyme activity has been close to the natural level – 98.4%. Catalise and invertase activity in this case were found to be higher (105 and 116% respectively) than that of natural analogues. Activity of enzymes increases with intensive application of fertilizers as compared with normal background. This is particularly evident with 6-8cm deep beardless plowing and 20-22cm deep moldboard plowing. In general, the obtained biochemical indicators charac-terize the highest environmental sustainability of this variation within our research.

scholarly journals Arylamidases of Rat Liver and Kidney

1967 ◽  
Vol 242 (10) ◽  
pp. 2369-2374
Author(s):  
S. Mahadevan ◽  
A.L. Tappel
Keyword(s):  
Rat Liver ◽  
Liver And Kidney

scholarly journals Sialidase of Rat Liver and Kidney

1967 ◽  
Vol 242 (19) ◽  
pp. 4409-4413
Author(s):  
S. Mahadevan ◽  
J.C. Nduaguba ◽  
A.L. Tappel
Keyword(s):  
Rat Liver ◽  
Liver And Kidney

Adaptation of rat liver and kidney antioxidant defenses after d-Amphetamine repeated administration

1998 ◽  
Vol 95 ◽  
pp. 55 ◽  
Author(s):  
Félix Carvalho ◽  
Eduarda Fernandes ◽  
Fernando Remiño ◽  
Paulo Sousa ◽  
Maria de Lourdes Bastos
Keyword(s):  
Rat Liver ◽  
Repeated Administration ◽  
Antioxidant Defenses ◽  
Liver And Kidney

scholarly journals Properties of subunits of the multicatalytic proteinase complex revealed by the use of subunit-specific antibodies

1991 ◽  
Vol 278 (1) ◽  
pp. 171-177 ◽  
Author(s):  
A J Rivett ◽  
S T Sweeney
Keyword(s):  
Molecular Mass ◽  
Rat Liver ◽  
Gel Filtration ◽  
Immunoblot Analysis ◽  
Rat Tissues ◽  
Specific Antibodies ◽  
Multicatalytic Proteinase ◽  
Cell Extracts ◽  
Liver And Kidney ◽  
Lysosomal Proteinase

The multicatalytic proteinase (MCP) is a high-molecular-mass non-lysosomal proteinase that gives rise to a characteristic pattern of bands of molecular mass 22-34 kDa on SDS/PAGE gels. Isoelectric-focusing gels of the enzyme purified from rat liver show 16 bands with isoelectric points in the range of pH 5-8.5. Two-dimensional PAGE gels reveal that there are more than the previously reported 13 polypeptides associated with the MCP from rat liver and show a pattern of 15-20 major spots and several minor ones, similar to that of MCP isolated from some other sources. Possible relationships between the different polypeptides were investigated by immunoblot analysis of electrophoretically purified proteinase subunits with affinity-purified subunit-specific antibodies as well as antibodies raised against individual denatured subunits of the complex. The results demonstrate that many of the major polypeptide components of the MCP complex are antigenically distinct. Moreover comparison of immunoreactive material in crude cell extracts with that in purified MCP preparations has shown that the polypeptides are not derived from a smaller number of higher-molecular-mass subunits. Also, individual subunits have the same apparent molecular mass in a variety of rat tissues, suggesting close similarity between MCPs of different tissues. The highest concentrations of MCP subunits occur in liver and kidney. Gel-filtration analysis of crude extracts has demonstrated that MCP polypeptides are also associated with a higher-molecular-mass complex, which may be the 26 S proteinase that has been implicated in the degradation of ubiquitin-protein conjugates.

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