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Biomedical subjects

M Gacko

Publications and source records attributed to M Gacko.

At least 19 recordsLinked to original sources
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↗
PubMed2001

[Proteolytic activity of placenta with EPH-gestosis determined by casein and azocasein].

Total proteolytic activity, activity of cathepsin B, activity of cysteine cathepsins and contents of protein degradation products were determined in placentas of pregnancies complicated with mild, moderate and severe EPH-gestosis and in placentas from normal pregnancies. The highest activity of all the determined proteases was observed in placentas of pregnancies complicated with severe EPH-gestosis. The placentas of pregnancies complicated with severe EPH-gestosis also include the highest amounts of aminoacids and low-molecular peptides.

Caseins↗
PubMed2000

[Experimental aortic aneurysm].

Experimental aortic aneurysm may be evoked in animals by application of chemical compounds disturbing biosynthesis, posttranslating modifications and degradation of elastin and collagen, local damage of the aortic wall by chemical, thermal and mechanical factors and by increased blood pressure. Administration of protease inhibitors, anti-inflammatory drugs, agents enhancing synthesis and formation of elastic and collagen fibers and hypotensive drugs prevent formation enlargement and rupture of aneurysm.

Aneurysm, Ruptured↗
PubMed1999

Distribution, activity and concentration of cathepsin B and cystatin C in the wall of aortic aneurysm.

Intensity of immunohistochemical reaction to cathepsin B is stronger and to cystatin C weaker in the wall of aortic aneurysm than in normal aorta. Localization of cathepsin B and cystatin C in the aneurysm wall is different from that in the control aorta, but activity and concentration of cystatin C in the aneurysmal wall is lower than in normal aorta. The parietal thrombus of aneurysm also shows high activity of cathepsin B. The obtained results point to participation of cathepsin B in degradation of aneurysmal structural proteins and in enlargement of the aneurysmal size.

Adult↗
PubMed1999

Coagulative and fibrinolytic activity in parietal thrombus of aortic aneurysm.

Lumen of aortic aneurysm is usually filled with parietal thrombus. Behaviour of the parietal thrombus is determined by the ratio of coagulation factors to factors of fibrinolytic system. Activity of some factors of coagulation and fibrinolysis in the parietal thrombus of aortic aneurysm was determined using coagulative, fibrinolytic and caseinolytic tests. Retracted, blood clot was a comparative material. Tissue factor activity in the parietal thrombus of the aneurysm was above threefold higher and antiheparin activity was nearly twice higher in comparison to the blood clot. Activity of plasminogen activators in the parietal thrombus was higher than in the blood clot. The parietal thrombus contained fourfold more of the plasminogen. Antiplasmin activity in the thrombus was above twofold lower than in the blood clot. High activity of the tissue factor and substances neutralizing heparin may intensify the thrombus growth. Yet the thrombotic tendency may be balanced by a high activity of plasminogen activators and plasminogen.

Aortic Aneurysm↗
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

Activities of proteases in parietal thrombus of aortic aneurysm.

Deterioration of the aortic wall resulting in formation of aneurysm may be evoked by increased activity of elastases, collagenases and lysosomal proteases. These enzymes come from macrophages and neutrophil granulocytes which are elements of the inflammatory reaction accompanying aneurysm. These cells may also come from parietal thrombus in the aneurysm lumen. The aim of this work was to determine activity of elastase, cathepsin G, collagenase-like Pz-peptidase and cathepsins A, B, C, D and E in the parietal thrombus of aortic aneurysm. The thrombus was obtained from the lumen of the aortic aneurysm of six patients during operation. Protease activities were determined using specific substrates at optimum pH. Retracted blood clot was a comparative material. The thrombus of aortic aneurysm showed two-five fold higher activity of elastases, collagenase-like Pz-peptidase and cathepsins A, D and G in comparison to the blood clot (P < 0.001). However, activity of cathepsins B, C and E in the thrombus was only slightly higher (P < 0.05). Prolonged effect of proteases coming from parietal thrombus on the aneurysm wall could evoke marked degradation of fibrillar proteins resulting in increase of aneurysm.

Aortic Aneurysm↗
PubMed1998

Cathepsin D and cathepsin L activities in aortic aneurysm wall and parietal thrombus.

Deterioration of the aortic wall resulting in formation of aneurysms may be caused by increased activity of metalloproteases and lysosomal proteases. The aim of this work was the evaluation of cathepsin D and cathepsin L activities, and activities of inhibitors of cysteine cathepsins in the wall of aortic aneurysms and in parietal thrombus. Aortic aneurysms were obtained during operation. Aortas taken from organ donors and blood clots were used as control material. Activities of cathepsin D and cathepsin L in the aortic aneurysm wall and parietal thrombus were higher than in the control groups. The aneurysm wall showed lower activity of inhibitors of cysteine proteases than the normal aorta. Parietal thrombus had a higher level of cysteine protease inhibitor activity than blood clot. Cathepsin D and cathepsin L present in the aneurysm wall and in the parietal thrombus filling the aneurysm may act on proteins determining elasticity and mechanical resistance of arteries.

Aorta↗
PubMed1998

[The role of proteolytic enzymes in apoptosis].

The literature review dealing with participation of proteolytic enzymes in initiation and execution of apoptosis was done. Cysteine proteases with Asp-X cleavage specificity, called caspases, play the main role in this process. The other proteases such calpains and proteasomes take also part in apoptosis. The proteases degrade proteins of cytoskeleton and structural proteins of nucleus, they also activate proendonucleases.

Animals↗
PubMed1998

Cellular serine carboxypeptidases.

The literature on serine carboxypeptidases of cells is reviewed. These proteases occur in the vacuoles of fungi and higher plants and in the lysosomes of animals and man cells. Physico-chemical properties, chemical structure, catalytic mechanism and substrate specificity of these enzymes are presented.

Animals↗
PubMed1997

Extralysosomal degradation of proteins.

Extralysosomal degradation of proteins is carried out by proteases complex (proteasomes), calcium dependent calpains, proteases of the rough endoplasmatic reticulum and proteases of the cellular membrane. It depends on a limited proteolysis and includes the main enzymatic proteins, hormones, growth factors and cytoskeletal proteins. Thus it plays an important regulatory role in the metabolism and formation of cellular structures.

Animals↗
PubMed1997

Proteolytic enzymes in proliferation and neoplastic metastases formation.

Metalloproteases, plasminogen urokinase activator, plasmin and cathepsins enable the expansion of neoplastic tumors, leading to metastases formation. They cause neoplastic cells to detach from tumor, facilitate cell movement, implantation and participate in tumor vascularization. The regulation of these processes is accomplished during the synthesis and activation of proenzymes. Enzyme activity control is realized by their bonds with cellular membranes, and inhibitor action.

Animals↗
PubMed1997

Lysosomal cysteine proteinases and their significance in pathology.

The lysosomal cysteine proteinases are synthesized in a form of pre-proenzymes. They are submitted to posttranslational glycosylation and phosphorylation. These modifications make possible transport the modified proteins into Golgi apparatus and into lysosomes. Some disturbances of transport which occur mainly in tumour cells result in an increase of these enzymes activities in cytosol and in intercellular compartment. The activity of cysteine proteinases is regulated by specific inhibitors (cystatin, kininogen) which exist in some tissues and body fluids. The evaluation of activity and concentration of proteinases and inhibitors is important in clinical diagnostics.

Amino Acid Sequence↗
PubMed1997

Plasminogen activators and plasmin in lung cancer.

Urokinase plasminogen activator and plasmin contribute to detach neoplastic cells from solid tumor and facilitate the movement of these cells through interstitium and capillary walls as well as infiltration of the surrounding structures. Plasminogen activators inhibitors fulfill a regulatory function in these processes. Determining activity and concentration, finding subcellular, cellular and zonal localization of every component of plasminogen activation system has diagnostic and prognostic importance in different lung cancer types.

Fibrinolysin↗
PubMed1997

Biological and diagnostic role of cathepsin D.

Biosynthesis, posttranslating modifications, intracellular transport and activation of procathepsin D are discussed. Active cathepsin D evokes degradation of cellular and extracellular proteins and it also activates proenzymes, prohormones and growth factors and inactivates their active forms. Impairment of lysosomes in hypoxia or necrosis evokes transition of cathepsin D to cytosol and body fluids. Increase of cathepsin D content in cytosol also evokes enhancement of the synthesis rate observed among others, in neoplastic tissues and regenerating organs. Increase of cathepsin D content and activity in cytosol and blood serum is of essential diagnostic and prognostic importance in some pathologic conditions.

Animals↗
PubMed1997

Cancer procoagulant--CP.

A review of literature concerning cancer procoagulant (CP) has been carried out. This procoagulant directly activates coagulation factor X to factor Xa. Possibilities of utilising determinations of this activator in diagnostics and prognostics of the cancerous disease are discussed.

Animals↗
PubMed1997

Tissue factor pathway inhibitor (TFPI).

Tissue factor pathway inhibitor (TFPI) is a plasma proteinase inhibitor. It is a 42 kD glycoprotein that consists of 276 amino acid residues which sequence is known. TFPI is synthesized by vascular endothelial cells and part of it is associated with glycosaminoglycans of these cells. In blood TFPI is found in a free-form (active) and in an associated with lipoprotein form (nonactive). TFPI directly inhibits activated factor Xa and then factor VIIa/TF complex. Decreasing TFPI activity facilitates an activation of blood coagulation and fibrin forming, increasing TFPI activity inhibits these processes.

Blood Coagulation Disorders↗