Estrogen-dependent activity of kidney lysosomal proteolytic enzymes. 2001

E Radzikowska, and K Janicki, and R Maciejewski, and B Madej
Human Anatomy Department, Medical University of Lublin.

Drug-induced kidney injury is a potential complication of a number of medicaments. The wide-spread use of estrogens in the form of oral contraceptives and in the form of hormonal replacement therapy, has necessitated extensive studies on the biochemical alterations. The following effects of estrogens on kidney are discussed in greater detail with special regard to enzyme induction. The aim of the study was to evaluate the influence of long-term activity estrogens on kidney lysosomal enzymes like cathepsin B, D and L. Female rats were divided randomly into eight experimental groups. Oestradiolum benzoicum was used for the purpose of this study. Estrogens were given i.m. one time per week for 8 weeks in different doses, respectively: E1--0.00075 g/kg b.w., one time per week; E1.1--0.00075 g/kg b.w. every three days; E2--0.0015 g/kg b.w.. one time per week. E2.1--0.0015 g/kg b.w.. every three days; E3--0.03 g/kg b.w.. one time per week; E3.1--0.003 g/kg b.w.. every three days; KO--untreated animals; K1--treated control, rats received oleum pro injection at the dose of 1.2 ml/100 g b.w. The activity of free and bound fractions of lysosomal enzymes, such as cathepsin B, D and L were assayed in kidney homogenates using spectrophotometric methods. Differences between various experimental groups were tested with ANOVA test. The activity of cathepsin B, D and L fractions showed significant changes compared to control groups. The observed changes were not characteristic in all the studied groups. The most important changes referred to the activity of cathepsin B and D. Differences were noted between the enzymes activity in animals treated with the smallest dose of estrogen and that in control groups. It was smaller in group E1 than in groups K0 and K1. The activity of cathepsin B was higher in group E1 than in control groups. There was no correlation between the dose of injected estrogens and the observed lysosomal activity changes. The changes in lysosomal activity were uncharacteristic.

UI MeSH Term Description Entries
D007668 Kidney Body organ that filters blood for the secretion of URINE and that regulates ion concentrations. Kidneys
D008247 Lysosomes A class of morphologically heterogeneous cytoplasmic particles in animal and plant tissues characterized by their content of hydrolytic enzymes and the structure-linked latency of these enzymes. The intracellular functions of lysosomes depend on their lytic potential. The single unit membrane of the lysosome acts as a barrier between the enzymes enclosed in the lysosome and the external substrate. The activity of the enzymes contained in lysosomes is limited or nil unless the vesicle in which they are enclosed is ruptured or undergoes MEMBRANE FUSION. (From Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed). Autolysosome,Autolysosomes,Lysosome
D010447 Peptide Hydrolases Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES. Peptidase,Peptidases,Peptide Hydrolase,Protease,Proteases,Proteinase,Proteinases,Proteolytic Enzyme,Proteolytic Enzymes,Esteroproteases,Enzyme, Proteolytic,Hydrolase, Peptide
D002401 Cathepsin B A lysosomal cysteine proteinase with a specificity similar to that of PAPAIN. The enzyme is present in a variety of tissues and is important in many physiological and pathological processes. In pathology, cathepsin B has been found to be involved in DEMYELINATION; EMPHYSEMA; RHEUMATOID ARTHRITIS, and NEOPLASM INVASIVENESS. Cathepsin B-Like Proteinase,Cathepsin B1,Cathepsin B Like Proteinase,Proteinase, Cathepsin B-Like
D002403 Cathepsins A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES. Cathepsin
D003546 Cysteine Endopeptidases ENDOPEPTIDASES which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by CYSTEINE PROTEINASE INHIBITORS such as CYSTATINS and SULFHYDRYL REAGENTS.
D004790 Enzyme Induction An increase in the rate of synthesis of an enzyme due to the presence of an inducer which acts to derepress the gene responsible for enzyme synthesis. Induction, Enzyme
D004967 Estrogens Compounds that interact with ESTROGEN RECEPTORS in target tissues to bring about the effects similar to those of ESTRADIOL. Estrogens stimulate the female reproductive organs, and the development of secondary female SEX CHARACTERISTICS. Estrogenic chemicals include natural, synthetic, steroidal, or non-steroidal compounds. Estrogen,Estrogen Effect,Estrogen Effects,Estrogen Receptor Agonists,Estrogenic Agents,Estrogenic Compounds,Estrogenic Effect,Estrogenic Effects,Agents, Estrogenic,Agonists, Estrogen Receptor,Compounds, Estrogenic,Effects, Estrogen,Effects, Estrogenic,Receptor Agonists, Estrogen
D005260 Female Females
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia

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