Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 7 de 7
Filter
Add more filters











Database
Language
Publication year range
1.
Ukr Biokhim Zh (1999) ; 73(2): 97-101, 2001.
Article in Russian | MEDLINE | ID: mdl-11642052

ABSTRACT

The effect of the total single and chronic roentgen irradiation in the dose of 0.25 Gy on the rats to alteration dynamics in lysosomal cysteine cathepsin L [CE 3.4.22.15] level in different brain regions (cortex, cerebellum, middle brain, varolian, hippocampus, striatum) was studied as a result of 1, 12, 24, 120 and 168 hours of exposure. The data obtained displayed the opposite consequences of chronic effect of 0.01 Gy during 25 days if compare with the single irradiation by 0.25 Gy that led to the cathepsin L changes different in directivity and activity level in dependence on brain region and post-irradiation period.


Subject(s)
Brain/radiation effects , Cathepsins/metabolism , Animals , Brain/enzymology , Cathepsin L , Cysteine Endopeptidases , Dose-Response Relationship, Radiation , Rats , X-Rays
2.
Ukr Biokhim Zh (1978) ; 70(5): 97-103, 1998.
Article in Russian | MEDLINE | ID: mdl-10445268

ABSTRACT

Cysteine cathepsin L was isolated and purified 1242-fold from human brain. Cathepsin L pH-optimum, Vmax, K(m), lysosomal origin and thiol nature were determined. The distribution of cathepsin L activity in human brain tumours of different histological structure, histogenesis and degree of malignization was studied. The activity of cathepsin L in most the tumours was found to be higher compared to the normal brain tissue.


Subject(s)
Brain Neoplasms/enzymology , Cathepsins/isolation & purification , Cysteine Endopeptidases/isolation & purification , Endopeptidases , Brain Neoplasms/pathology , Case-Control Studies , Cathepsin L , Humans , Hydrogen-Ion Concentration , Lysosomes/enzymology , Neoplasm Staging
3.
Ukr Biokhim Zh (1978) ; 68(5): 116-9, 1996.
Article in Russian | MEDLINE | ID: mdl-9229846

ABSTRACT

The development of neurochemical investigations at the Institute of Biochemistry of the National Academy of Sciences of Ukraine initiated by Academician A. V. Palladin, has impelled specialists in some regions of the country to start research in this trend. The Department of Biophysics and Biochemistry of Dniepropetrovsk State University founded and headed by Professor O. D. Reva became one of such centres in the Dnieper area. The chief developments of scientific-research inventions were devoted to radiational neurochemistry, O. D. Reva should be accounted as a pioneer of the study of chemical composition and metabolism in functional and morphologically logically different sites of cats spinal cord lumbar enlargement. Thus, the significant statement, proposed by A. V. Palladin, was confirmed about the presence of biochemical differentiation in cerebrum besides the morphological and functional ones. While analysing the test data concerning the biochemical and biophysical indices of roentgen irradiation of cats in different terms and conditions an original scheme of radiation-biophysical and radiation-biochemical injury of spinal cord was proposed. Some tissue proteinases, as well as some neurospecific proteins in the norm and under the gamma-irradiation were selected and assayed. An immunoelectrophoretic technique for estimating glyolic fibrilar acid protein and cellular adhesion (N-CAM) in blood and surrounding fluid, as well as in human brain tumour was developed and a method of early prenatal diagnosis of embryo developmental disorders was proposed in order to prevent the birth of the underdeveloped infants.


Subject(s)
Neurochemistry/history , History, 20th Century , Ukraine
4.
Radiobiologiia ; 31(1): 38-42, 1991.
Article in Russian | MEDLINE | ID: mdl-2008521

ABSTRACT

The influence of X-radiation on activity of lysosomal enzymes (D, L, H cathepsins) in rat spleen tissue and in inoculated rat sarcoma 45 has been investigated. Intact rats and rats with tumors were subjected to whole-body and sarcoma 45 to local irradiation with doses of 0.155 C/kg and 0.31 C/kg in conditions of breathing gas hypoxic mixture containing 90% of nitrogen and 10% of oxygen (GHM-10). The combined exposure to radiation and GHM-10 was shown to produce a certain protective action (e.g. normalized cathepsin activity) in the spleen. In the tumor tissue the protective effect of GHM-10 was absent.


Subject(s)
Hypoxia/enzymology , Peptide Hydrolases/radiation effects , Sarcoma, Experimental/enzymology , Spleen/radiation effects , Animals , Lysosomes/enzymology , Lysosomes/radiation effects , Male , Neoplasm Transplantation , Nitrogen/pharmacology , Oxygen/pharmacology , Peptide Hydrolases/metabolism , Radiation-Protective Agents/pharmacology , Rats , Rats, Inbred Strains , Spleen/enzymology , Time Factors , Whole-Body Irradiation
5.
Ukr Biokhim Zh (1978) ; 61(5): 47-50, 1989.
Article in Russian | MEDLINE | ID: mdl-2588347

ABSTRACT

The human brain cathepsin H is shown to be a specific cysteine aminopeptidase with the optimum activity at pH 6.0. Human brain tumours of neuroectodermal (astrocytomas and glioblastomas) and epithelial (meningiomas) origin were used to study the cathepsin H activity in the malignant brain tissue. A significant increase in the aminopeptidase cathepsin H activity was found in malignant human brain tumours as compared to benign tumours and normal brain tissues.


Subject(s)
Brain Neoplasms/enzymology , Brain/enzymology , Cathepsins/metabolism , Cysteine Endopeptidases , Cathepsin H , Humans , Hydrogen-Ion Concentration
6.
Ukr Biokhim Zh (1978) ; 54(3): 249-53, 1982.
Article in Russian | MEDLINE | ID: mdl-7101470

ABSTRACT

Thiol-activated cathepsin was isolated from bovine cerebral hemispheres and cerebellum. The enzyme from the hemispheres was purified by the affinity sorbent chromatography method with the sepharose-4B-immobilized protein substrate, azocasein, and with subsequent separation of nonspecifically sorbed protein by column gel-chromatography on Sephadex G-100. The cathepsin pH-optimum was 6.0. The coincidence in cellular (neuron and glia enriched fractions) and subcellular distribution of cathepsin D and thiol-activated cathepsin activities shows the probable lysosomal origin of the latter. The data obtained about the influence of the various proteolytic enzyme inhibitors and activators on the thiol-activated cathepsin activity show a definite similarity of the enzyme with the thiol proteinases of the rat liver lysosomes, cathepsin B1 and L.


Subject(s)
Brain/enzymology , Cathepsins/isolation & purification , Cerebellum/enzymology , Sulfhydryl Compounds/pharmacology , Animals , Cathepsins/metabolism , Cattle , Enzyme Activation , Kinetics
7.
Ukr Biokhim Zh (1978) ; 50(4): 411-4, 1978.
Article in Russian | MEDLINE | ID: mdl-684867

ABSTRACT

The dependence of the cathepsin B1 (EC 3.4.22.1) activity on pH of a medium with substrates N alpha-benzoyl-L-arginine amide (BAA) and N alpha-benzoyl-DL-arginine-paranitroanilide (BAPNA) was studied. Several maxima of the studied enzyme activity are established depending on pH in the grey and white matter of the cat cerebral hemispheres. The activity of cathepsin BI is different in functionally and morphologically different areas of brain (grey matter of cerebral hemispheres less than than cerebellum less than white matter of cerebral hemispheres less than medulla oblongata). A six-fold freezing and defrosting of homogenates of the brain structures under study causes an increase in the cathepsin B1 activity. It is shown that the cathepsin B1 activity in the brain grey matter grows in the presence of L-cysteine and is inhibited under the effect of pChMB, monoiodoacetic acid, Mn2+ and Cu2+.


Subject(s)
Brain/enzymology , Cathepsins/metabolism , Animals , Cats , Enzyme Activation , Freezing , Kinetics , Tissue Distribution
SELECTION OF CITATIONS
SEARCH DETAIL