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Biomedical subjects

W Roszkowska-Jakimiec

Publications and source records attributed to W Roszkowska-Jakimiec.

At least 19 recordsLinked to original sources
PubMed2005

Effect of fluoride preparations on the activity of human salivary cathepsin C.

Preparations containing organic and inorganic fluorine compounds are used for oral hygiene. Fluoride ions contained in these preparations display high bioactivity and can alter the environment of the mouth. The aim of the study was to determine the effect of preparations containing aminofluorides, commonly used in oral hygiene, on the activity of salivary cathepsin C (EC 3.4.14.1). The research material included mixed saliva, collected at rest before and after the application of the following preparations: Elmex gelee, Elmex red fluid, Elmex green fluid, Fluormex rinse. The salivary pH, concentration of fluoride ions and activity of cathepsin C were determined. Fluoride preparations inhibit the activity of cathepsin C and cause changes in human salivary pH. Saliva can serve as a diagnostic material in the examination of the environmental exposure to fluorides.

Adult↗
PubMed2004

Immunohistochemical evaluation of mast cells and mark activity tryptase and chymase in experimental fibrosarcoma.

The aim of the study was an evaluation of the activity of mast cells and mark activity tryptase and chymase and of protein levels in experimental fibrosarcoma, induced in rat skin. The experiments were carried out on 50 male Wistar rats. The cancer was induced in rats by one subcutaneous injection of 0.2 mg 3-methylcholanthrene in 0.25 ml of olive oil. Tissue material was fixed in Bouin's fluid. Immunohistochemical tryptase detecting reactions were performed--using specific antibodies and the ABC complex. The activities of tryptase and chymase and protein levels were determined in supernatant of 10% homogenate. We found a very significant growth of mast cell quantity in the connective tissue of tumours. We observed slight differences in the activity of examined enzymes in tumours of different mass.

Animals↗
PubMed2004

Effects of cathepsin D inhibitor from Vicia sativa L. seed hulls on human skin fibroblasts and breast cancer cells (in vitro studies).

Cathepsin D is a lysosomal protease which plays an important role in cancer invasion and metastasis. There are known inhibitors of that enzyme, such as pepstatin and potato inhibitor. In this study, we examined effects of the cathepsin D inhibitor from Vicia sativa L. seed hulls on cell cultures of human skin fibroblasts and breast cancer cells. There is no effect of the D-cathepsin inhibitor from Vicia sativa L. seed hulls on the proliferative activity of either human skin fibroblasts or breast cancer cells, measured by the [3H] thymidine incorporation assay.

Breast Neoplasms↗
PubMed2003

Synthesis of benzylamides of dipeptides as potential inhibitors of plasmin.

Four benzylamides of dipeptides with the general formula: X-L-Lys-NH-CH2-C6H5, where X = L-or D-Leu and L-or D-Phe were prepared as potential inhibitors of plasmin. All of them influenced on the fibrynolytic activity of plasmin, but only D-Leu-L-Lys-NH-CH2-C6H5 inhibited the amidolytic activity of this enzyme. None of the tested compounds was an inhibitor of thrombin in an amidolytic test.

Benzyl Compounds↗
PubMed2001

[Activity of cathepsin B and cystatins in the placenta during EPH-gestosis].

Activity of cathepsin B using Bz-DL-Arg-pNA contents of SH-group by means of Ellman method, activity of cystatins against papain using casein as a substrate and contents of deoxyribonuclein acids by Burton method were determined in 64 placentas of pregnancies with EPH-gestosis and in 36 placentas of physiological pregnancies. The placentas from pregnancies with EPH-gestosis showed markedly higher activity of cathepsin B, no difference in the contents of SH-group, slightly higher activity of cystatins and they contain less deoxyribonucleic acids than the placentas from physiological pregnancies. The obtained results show that proteolytic--anti-proteolytic balance in placentas from pregnacies with EPH-gestosis is changed to the advantage of cathepsin B. This protease may in formation of structural and functional changes observed in placentas during EPH-gestosis.

Cathepsin B↗
PubMed2000

Hemorrhagic shock activates mast cells in the rat stomach wall.

The activation of mast cells (MC) and liberation of their mediators can play an essential role in initiating and controlling inflammatory processes in the wall of the gastrointestinal tract (GIT) due to ischemia. The role of MC in changes induced by hemorrhagic shock (HS) remains unknown. Heparin provided by MC seems to inhibit local inflammation and prevent DIC. The aim of this study was to evaluate the morphometric changes and biochemical activity of MC in the stomach wall after 75 minutes of hemorrhagic shock. The MC in mucosal, submucosal, muscular and serosal compartments of the various stomach wall regions were examined in shocked rats and in the control group. Additionally, the contents of glycosaminoglycans (GAG), measured as uronic acids concentration, as well as anticoagulative activity in the stomach wall were assessed. HS resulted in an evident increase in the number of mast cells detected in the stomach mucosa and serosa, in slight alterations in number of MC in the submucosal and muscular layers, a significant increase in size and changes of the shape of the MC. The elevation of the width, area, and circular shape of MC in all layers were noted. No clear and significant differences between various stomach regions in MC numbers and MC sizes could be shown. No reaction of other inflammatory cells at this stage of shock was observed. Highly significant increases in GAG concentration, and anticoagulative activity in the stomach wall due to shock were noted. The morphometric and biochemical data may indicate MC activation, especially in mucosa and serosa. The shock-induced migration of MC settled in the stomach wall seems to be possible. The results suggest an essential role of MC reaction in the stomach wall in the early phase of hemorrhagic shock.

Animals↗
PubMed2000

Interaction of L-gamma-glutamyl-alpha,beta-dehydroamino acids with gamma-glutamyl transpeptidase.

Three gamma-glutamyl alpha,beta-dehydroamino acids: L-gamma-glutamyl-dehydroalanine, L-gamma-glutamyl-(Z)-dehydrobutyrine and L-gamma-glutamyl-(E)-dehydrobutyrine have been prepared as potential ligands (inhibitors or substrates) for gamma-glutamyl transpeptidase (GGT). Both isomers of gamma-glutamyl-dehydrobutyrines proved to be inhibitors of GGT, slightly better than the saturated analogue, L-gamma-glutamyl-L-butyrine. However, their solvolysis catalysed by the enzyme is slower than that of the latter. L-gamma-Glutamyl-(E)-dehydrobutyrine seems to be a more active compound in both enzymatic tests. L-gamma-Glutamyl-dehydroalanine elicited only low inhibitory activity and, moreover, was unstable under conditions of the solvolysis test.

Enzyme Inhibitors↗
PubMed1999

Anticoagulative effect of pepsin.

Anticoagulative effect of pepsin is observed in vitro when its concentration is 36 microM and higher. This effect is due to inhibition of fibrin monomer polymerization. Protamine abolishes anticoagulative effect of pepsin. Pepsin does not influence platelet aggregation induced by ADP and collagen.

Anticoagulants↗
PubMed1998

Cathepsin D inhibitor from Vicia sativa L.

Specific inhibitor of cathepsin D has been shown in the extract of Vicia sativa L. seeds. This inhibitor does not inhibit the activity of other aspartic proteases. Also it does not inhibit the activity of cysteine proteases and serine proteases.

Cathepsin D↗
PubMed1998

Inhibitors of pepsin, trypsin and chymotrypsin in seeds of plants consumed by humans and animals. I. Evaluation of pepsin, trypsin, and chymotrypsin inhibitors activity in seeds of 26 plant species.

Antipepsin, antitrypsin and antichymotrypsin activity was determined in seed extracts of 26 plants consumed by humans and animals (small bean, broad bean, pumpkin, kidney bean, charlock, pea, buckwheat, barley, maize, flax, lupine, poppy, almond, peanut, hazel, walnut, oat, millet, wheat, rice, rape, sunflower, lentils soya bean, vetch, rye). Antipepsin activity is found in the seeds of small bean, pumpkin, flax, peanut, walnut, oat, wheat, sunflower, lentils and soya bean. Antitrypsin and antichymotrypsin activities are of different intensity in seed extracts of all examined plants.

Animals↗
PubMed1997

Tripeptide methylketones: synthesis and antiplasmin activity.

A series of tripeptide methylketones with C-terminal lysine was obtained via Dakin-West method and tested for their antiplasmin activity with the use of antifibrinolytic and antiamidolytic tests. The tripeptide methylketones has been found to inhibit plasmin, however with much lower potency than respective aldehydes.

Chemical Phenomena↗
PubMed1996

Influence of dipeptide derivatives of S-substituted cysteines on the time of fibrinolysis.

Amino acids containing sulphur, dipeptide derivatives of methionine and S-substituted derivatives of cysteine are potent antifibrinolytic agents. The structural moiety of the substances responsible for the effect on the clot formation is not known. Present study was undertaken in order to evaluate the effect of some analogues of dipeptides containing S-substituted derivatives of cysteine with the formula A-Cys(S-X)-Y (where A-amino acid, X-benzyl, butyl, hexyl, nonyl and Y-OH or OMe) on clot dissolution under the antifibrinolytic test conditions. It has been found that dipeptide derivatives of S-substituted cysteine (except benzyl derivative) at low concentration evoke antifibrynolytic activity, while at high concentration they prevent clot formation. The results suggest that antifibrinolytic activity of tested compounds at low concentration may be due to the formation of antifibrinolitycally active conformation, while high concentration overcome the effect.

Antifibrinolytic Agents↗
PubMed1994

Synthesis and activity of dipeptides containing epsilon-aminocaproic acid.

Five new dipeptides containing epsilon-aminocaproic acid were synthesized. All dipeptides markedly inhibit fibrinolytic activity of plasmin but only in low concentration (0.0002M). In higher concentration fibrinolytic activity was observed. Activity of dipeptides containing epsilon-aminocaproic acid, which antifibrinolytic activity is known, was tested on plasmin, thrombin, urokinase and euglobulin fraction using synthetic substrates.

Amides↗
PubMed1992

[Interaction of acetaldehyde and proteins].

A review of literature dealing with acetaldehyde-proteins reactions in vitro and in vivo was done. The changes in proteins structure and functions resulting from acetaldehyde binding were discussed.

Acetaldehyde↗
PubMed1992

[Proteolytic enzymes of the digestive tract in ethanol poisoning].

The present paper reviews the literature on changes of proteolytic enzymes activity, disorders of protein digestion and absorption of protein degradation products from digestive tract in ethanol intoxication. Magnitude of the change depends on concentration, dose and time of ethanol consumption. Acute ethanol intoxication causes increase in gastric and pancreatic proteolytic enzymes secretion and reduces amino acids and peptides absorption. Chronic ethanol consumption results in reduced synthesis and secretion of gastric and pancreatic proteinases.

Alcohol Dehydrogenase↗