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Biomedical subjects

E Bańkowski

Publications and source records attributed to E Bańkowski.

At least 37 records · Page 2Linked to original sources
PubMed1998

Collagenous constituents of amniotic fluid.

The amniotic fluid (AF) was fractionated by dialysis, gel filtration and SDS/PAGE, and submitted to the assay of collagenous constituents. The collagenous character of peptides and proteins of amniotic fluid was confirmed by hydroxyproline (Hyp) assay and treatment with bacterial collagenase followed by electrophoresis and gel filtration of the digestion products. It was found that AF contains collagen degradation products but the classical method of Hyp determination described by Woessner (Arch. Biochem. Biophys., 1961, 93, 440-447) gives overestimated values due to the interference with other AF components. Fractionation of AF on Sephadex G-100 column allowed to remove the interfering material and to estimate the actual Hyp content which equals to approx. 6.2 microg/ml. About 70% of Hyp was found in low molecular dialyzable products and the rest (about 30%) appears to be a constituent of nondialyzable collagenous polypeptides of the molecular mass of about 7.9-26.3 kDa. It is suggested that such collagenous polypeptides may be the products of proteolytic conversion of collagen precursor (procollagen) into the monomeric form of this protein. No high molecular forms of collagen, corresponding to alpha-subunits, were found.

Amniocentesis↗
PubMed1998

[Alterations in the content of collagenous constituents of amniotic fluid in the course of EPH-gestosis].

OBJECTIVES: EPH-gestosis may cause placental insufficiency and affect the metabolism of placenta and fetus. Various metabolites of amniotic fluid may reflect the fetal metabolism. DESIGN: It was decided to compare the content and some biochemical features of hydroxyproline-containing collagenous constituents in the amniotic fluid derived from normal gestations and gestations affected by EPH-gestosis. MATERIALS AND METHODS: Amniotic fluid was taken during labour (full-term gestations) by amniocentesis from 10 healthy women (control group) and 10 women with EPH-gestosis. UV-absorption spectra, protein and hydroxyproline were measured in non-dialyzed and dialyzed amniotic fluid. Hydroxyproline-containing collagenous constituents of amniotic fluid were chromatographed on Sephadex G-200. RESULTS: Statistical differences in concentrations of total and non-dialyzable hydroxyproline between normal and gestotic amniotic fluid were not found. In contrast to that, gestotic amniotic fluid contains more dialyzable hydroxyproline (6.2 mg/ml) than normal fluid (4.5 mg/ml; p < 0.05). Molecular sieving on Sephadex G-200 shows that this difference is due to higher content of low molecular collagen degradation products. CONCLUSION: Amniotic fluid, derived from pregnancies complicated by EPH-gestosis, contains higher amount of low molecular collagen degradation products than normal amniotic fluid. It is probably the result of more intensive degradation of fetal and placental collagen.

Amniotic Fluid↗
PubMed1998

Electrophoretic and chromatographic patterns of glycosaminoglycans of the umbilical cord vessels and their alteration in EPH-gestosis.

It was found that hyaluronic acid is the most abundant glycosaminoglycan (GAG) both in the umbilical cord arteries and in the umbilical cord veins. Chromatographic and as well as electrophoretic studies demonstrated that EPH-gestosis (Edema-Proteinuria-Hypertension), the most common pathological syndrome occurring in pregnancy, is accompanied by premature replacement of hyaluronic acid by sulphated GAGs in the investigated arteries but not in the veins. Such a replacement is a characteristic feature of the ageing process. One may conclude that EPH-gestosis is associated with a "premature ageing" of the umbilical cord arterial walls. The mechanism and possible role of this phenomenon in pathology are discussed.

Chromatography, Gel↗
PubMed1997

Glycosaminoglycan-biosynthesis in the wall of the umbilical cord artery and its alteration in EPH-gestosis.

The mechanism of edema, proteinuria, hypertension (EPH)-gestosis-associated premature replacement of hyaluronic acid by sulphated glycosaminoglycans (GAGs) in the umbilical cord arteries is not known. It may result from altered biosynthesis, a different degradation rate or a combination of both phenomena. In order to solve this problem, it was decided to evaluate the biosynthesis and degradation of newly synthesized GAGs in the umbilical cord arteries of control newborns and those delivered by mothers with EPH-gestosis. Incorporation of radioactive precursors ([14C]glucosamine and [35S]sulphate) into GAGs and degradation of newly synthesized GAGs using the pulse-chase experiment were evaluated. We found that the investigated tissue slices incorporated distinctly less [14C]glucosamine into hyaluronic acid in comparison to controls. In contrast to that, the biosynthesis of sulphated GAGs did not change significantly. However, the degradation of newly synthesized sulphated GAGs was distinctly slower than in control tissues. It may be concluded that an EPH-gestosis associated decrease in hyaluronic acid content in the umbilical cord artery is a result of decreased biosynthesis of this substance, whereas an increase in sulphated GAGs-content is rather a result of slower degradation of newly synthesized GAGs.

Adolescent↗
PubMed1997

Collagen and glycosaminoglycans of Wharton's jelly.

In this study, we report quantity, solubility and molecular polymorphism of collagen, proportional relationships between various types of collagen, ultrastructure of collagen fibres, the amounts of various glycosaminoglycans (GAGs) and proportional relationships between them in Wharton's jelly of normal umbilical cords. We compare the extracellular matrix components in Wharton's jelly with those in the umbilical cord artery. Collagen of the Wharton's jelly demonstrates some specific features. It is very insoluble in neutral salt and in a slightly acidic solution and appears to be resistant to the action of depolymerizing agent (EDTA-Na2). Only 50% of total collagen may be solubilized by pepsin digestion and fractionated by differential salt precipitation. Four collagen fractions were obtained. Three of them were identified by polyacrylamide gel electrophoresis as type I, type III, and type V collagen and proportional relationship between them was calculated. Hyaluronic acid is the most abundant component of GAGs contained in Wharton's jelly. The amounts of sulphated GAGs-keratan sulphate, heparan sulphate, chondroitin-4-sulphate, chondroitin-6-sulphate, dermatan sulphate and heparin-are distinctly lower. Each of them constitutes only a few percent of total GAGs.

Adolescent↗
PubMed1996

Decrease in the glycosaminoglycan content in the skin of diabetic rats. The role of IGF-I, IGF-binding proteins and proteolytic activity.

The results of our previous studies demonstrated that acute streptozotocin-induced diabetes in rats evoked a decrease in skin collagen content with little effect on glycosaminoglycans (GAG) content. In our present study we employed the model of chronic diabetes in order to check its effect on skin GAG content. It was found that the skin of diabetic rats showed a significant decrease in almost all the investigated GAGs by 50-70%. The decrease in heparan sulfate content was slight and statistically insignificant. We sought to determine whether the insulin-like growth factor-I (IGF-I) and IGF-binding proteins (IGF-BPs) levels are altered in animals with experimental diabetes and might contribute to the decrease in tissue GAG content. Circulating IGF-I level was found to be reduced in animals with diabetes and significant changes in serum IGF-BPs were observed. The amount of high molecular weight binding proteins (HMW-BPs) was decreased and the content of low molecular weight binding proteins (LMW-BPs), known as IGF-I inactivating substances, markedly increased. Furthermore, diabetic rats demonstrated an increase of skin proteolytic activity. We conclude that the decrease of GAG content in the skin of diabetic rats is a result of three co-existing phenomena: decreased circulating IGF-I level, increased plasma content of LMW-BPs and increased proteolytic activity of the skin.

Animals↗
PubMed1996

Collagen and glycosaminoglycans of Wharton's jelly and their alterations in EPH-gestosis.

Some prenatal pathological processes may be caused by biochemical and morphological alterations in the umbilical cord (UC). EPH-gestosis is the most common pregnancy-associated pathological process. For these reasons the role of collagen and glycos-aminoglycans (GAGs) of UC in pathobiochemistry of this syndrome seems to be important. We studied histology of extracellular matrix components, quantity, solubility and molecular polymorphism of collagen, proportional relationships between various types of collagen, the amounts of GAGs and proportional relationships between them in Wharton's jelly of control newborns delivered by healthy mothers and those delivered by mothers with EPH-gestosis. We found that Wharton's jelly is abundant in collagen and GAGs. This collagen is very insoluble and resistant to the action of depolymerizing agents (4% EDTA-Na2, pepsin). Types I, III and V collagens were isolated and quantified. Hyaluronic acid constitutes about 70%, whereas sulphated GAGs constitute about 30% of total GAGs. EPH-gestosis is accompanied by significant increase in sulphated GAGs: hyaluronic acid ratio. The EPH-gestosis-associated alterations in Wharton's jelly correspond to 'premature ageing' of this tissue.

Adult↗
PubMed1996

Alterations in glycosaminoglycan composition of methylcholanthrene-induced sarcoma at various stages of the tumour growth.

The methylcholanthrene-induced sarcoma contains several types of glycosaminoglycans, hyaluronic acid being the major component. Furthermore it contains all sulphated glycosaminoglycans present in the skin: chondroitin-4-sulphate, chondroitin-6-sulphate, keratan sulphate, dermatan sulphate, heparan sulphate and heparin. It was found that the amount of all glycosaminoglycans distinctly increased during tumour growth. At the same time the amount of collagen significantly decreased. It is suggested that some of the GAGs participate in the creation of a storage depot for biologically active molecules (growth factors, enzymes) which are thereby stabilized and protected. Hydrolytic degradation of some GAGs may result in the release of some cytokines which may stimulate or inhibit the tumour growth. The changes in the quantities of various glycosaminoglycans during the tumour growth may be responsible for a dual-phase growth of this tumour.

Animals↗
PubMed1996

Alterations in glycosaminoglycans in wounded skin of diabetic rats. A possible role of IGF-I, IGF-binding proteins and proteolytic activity.

In the skin of diabetic animal tissues the amount of extracellular matrix (ECM) components is drastically decreased as a result of a reduced rate of their biosynthesis or increased degradation. In the present study we have investigated the mechanism of poor wound healing in diabetic rats. We have found that wounded skin of diabetic rats shows a significant decrease in glycosaminoglycan (GAG) content compared to that of control animals. This decrease was accompanied by significant depletion of insulin-like growth factor-I (IGF-I), known as a stimulator of GAG biosynthesis, and a distinct decrease in the content of high molecular weight IGF-binding proteins (HMW-BPs) with a simultaneous increase in low molecular weight IGF-binding proteins (LMW-BPs) in the sera of diabetic animals. Basing on determination of proteolytic activities we suggest that insulin shortage in diabetes results in increased proteolytic activity in various tissues. Proteolytic enzymes may cleave the HMW-BPs and convert them to LMW-BPs. The LMW-BPs may inactivate IGF-I and eliminate its stimulatory effects on GAG biosynthesis. The proteolytic enzymes may also digest the protein cores of proteoglycans releasing the GAGs and making them more susceptible to the action of glycosidases. These phenomena may be responsible for the observed marked decrease in GAG content in the skin of diabetic rats and disturb the wound-healing process.

Animals↗
PubMed1995

[Proteolytic activity of the vitreous body].

It was found that the human and bovine vitreous contains a proteolytic enzyme(s) which demonstrates characteristic features of cathepsin D. It acts in acidic pH with various activity, dependent on the condition of the eye and actively digests native and denatured protein substrates. It demonstrates a high susceptibility to the inhibitory action of pepstatin. The role of this enzyme in physiology and pathology of the eye is discussed.

Animals↗
PubMed1995

Collagen, elastin and glycosaminoglycans in aortic aneurysms.

The walls of human abdominal aortas and atherosclerosis-induced aneurysms contain similar amounts of collagen. The quantitative ratio between collagens of various types of this protein does not differ significantly either, whereas solubility of the collagen in aneurysmal wall and its susceptibility to the action of EDTA are distinctly decreased. In contrast with collagen, the amount of elastin in aneurysms is significantly lower. Total amount of glycosaminoglycans slightly decreased as compared with that of normal tissue, but the ratio of particular compounds varies. The percentage of chondroitin sulphate is increased and that of heparan sulphate significantly decreased. The significance of these changes in pathogenesis of aneurysms is discussed.

Adult↗
PubMed1995

Cathepsin D and an alkaline protease activities in subretinal fluid.

It was found that subretinal fluid contains at least two different proteolytic enzymes which digest various protein substrates. The main of them was identified as cathepsin D. This protease is very active towards the denatured haemoglobin. The highest activity is apparent at pH 3-4 and it is completely inhibited by the action of pepstatin. The cathepsin activity increases with the duration of retinal detachment. The other proteolytic enzyme acts at slightly alkaline pH. Its activity is lower and does not change with the duration of the disease.

Body Fluids↗
PubMed1994

Rat fibrosarcoma as a source of stable co-polymer of type I and type III collagens.

During conventional procedures for the extraction of collagen from rat fibrosarcoma it was observed that a significant fraction of the acid-soluble collagen remained insoluble when subsequently fractionated at neutral pH. Analysis of this collagenous component, using amino acid analysis, cyanogen bromide peptide mapping, proteinase susceptibility and the action of denaturing and reducing agents, revealed different properties when compared to other collagen species. The results indicate that the tumour collagen fraction is probably a stable complex of type I and III collagens. This native collagen heteropolymer represented approximately 18% of the total collagen from rat fibrosarcoma and as such provides a unique natural source of this collagen complex for further analytical studies.

Amino Acids↗
PubMed1994

Collagen in liver fibrosis induced by ethanol.

Liver fibrosis is accompanied by significant increase of collagen content in this organ. Chronic intoxication with ethanol is probably the most popular cause of liver fibrosis. Some experimental and clinical data suggest that acetaldehyde (an intermediary product of ethanol oxidation) is responsible for stimulation of collagen biosynthesis in the liver. It increases collagen gene transcription in fibroblasts. About 90% of exogenous ethanol is oxidized in liver providing an enhanced amount of acetaldehyde which triggers the fibrotic response.

Acetaldehyde↗
PubMed1994

Cathepsin D--a main proteolytic enzyme of the bovine vitreous.

It was found that the bovine vitreous contains a proteolytic enzyme which demonstrates characteristic features of cathepsin D. It acts in acidic pH, actively digests denatured protein substrates and demonstrates a high susceptibility on the inhibitory action of pepstatin. It is localized in liquid part of the bovine vitreous. A role of this enzyme in physiology and pathology of the eye is discussed.

Animals↗
PubMed1994

Glycosaminoglycans of umbilical cord arteries and their alterations in EPH-gestosis.

It was found that the umbilical cord arteries (UCAs) contained several types of glycosaminoglycans (GAGs), including hyaluronic acid and sulphated glycosaminoglycans. EPH-gestosis is accompanied by significant changes in the composition of extracellular matrix of the UCAs. Significant increase in collagen content was found. Total amount of GAGs did not change much but the quantitative ratio between various GAGs distinctly altered. A decrease in hyaluronic acid content and an increase in the amount of sulphated GAGs as well as a diminution of GAGs/collagen ratio were observed. These observations were confirmed by histochemical methods. The significance of these phenomena for collagen fibrillogenesis in the arterial wall is discussed.

Adolescent↗
PubMed1994

Solcoseryl prevents early postradiation changes in the lungs.

The aim of the study was to test the influence of Solcoseryl on early postradiation changes in the lungs of rats. The chests of the rats were irradiated with Co-60, fractional dose 250 cGy/DT, total dose 2500 cGy/DT. Solcoseryl was given intraperitoneally in quantities of 0,1ml daily, during 60 days of the experiment. Morphological examinations of the lungs revealed that Solcoseryl decreased significantly the effects of early postradiation damage of the respiratory organ in rats.

Actihaemyl↗