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Biomedical subjects

M Wolańska

Publications and source records attributed to M Wolańska.

At least 19 recordsLinked to original sources
PubMed2005

Fibroblast growth factors (FGF) in human myometrium and uterine leiomyomas in various stages of tumour growth.

We previously described that the growth of human uterine leiomyomas was associated with a significant remodelling of the extracellular matrix of these tumours. Significant weight-related increase of collagen and heparan sulphate contents was detected. The latter was known as a component, which bound some peptide growth factors, mainly FGFs, therefore it was decided to evaluate the amounts of acidic FGF (aFGF) and basic FGF (bFGF) in human myometrium and in leiomyomas of various weight and FGF-binding to tissue components. It was found that myometrium and uterine leiomyomas contain picogram amount of aFGF and nanogram amounts of bFGF. No free aFGF was found. Slight amounts of free bFGF were detected both in myometrium and in the tumours. The aFGF and most of bFGF existed in a form of complex with a high molecular component(s). These complexes were very stable and they did not dissociate in denaturation conditions. In comparison to myometrium the tumours contained several times more FGFs and their amounts distinctly increased during the tumour growth. The expression of FGF-receptor I (FGF RI) in the tumours was more distinct in comparison to myometrium. The extracts from myometrium did not bind exogenous 125I-bFGF. In contrast to that the tumours of different weights contained at least two high molecular weight FGF-binding components. One of them (150 kDa) corresponded to FGF-receptor. The other one (190-200 kDa) might be a heparan sulphate-proteoglycan. It seems that aFGF and bFGF play an important role in transformation of normal myometrium into leiomyoma and further growth of this tumour. The action of FGFs on tumour cells enhances biosynthesis of collagen and sulphated glycosaminoglycans, especially heparan sulphate which binds FGFs in the vicinity of cells and facilitates their interaction with membrane receptors. The effect of these processes may be further stimulation of tumour growth and remodelling of tumour extracellular matrix.

Animals↗
PubMed2001

The activity of collagen-degrading enzymes of Wharton's jelly in EPH gestosis (pre-eclampsia).

Oedema/proteinuria/hypertension (EPH) gestosis is one of the more common complications observed during pregnancy. Our previous studies demonstrated some qualitative and quantitative changes in the extracellular matrix of Wharton's jelly in newborns delivered by mothers with EPH gestosis. For this reason it was decided to evaluate the effect of EPH gestosis on the activity of gelatinolytic and proteolytic enzymes which may be involved in collagen degradation in Wharton's jelly. Zymographic analysis of control and EPH gestosis samples of Wharton's jelly demonstrates different electrophoretic patterns of gelatinolytic enzymes. The control Wharton's jelly contains two latent forms of gelatinolytic enzymes: gelatinase A [metalloproteinase (MMP)-2, 72 kD] and gelatinase B (MMP-9, 92 kD). In contrast to control tissue, the main gelatinolytic enzyme of EPH gestosis Wharton's jelly is gelatinase A (MMP-2). It was found that the proteolytic activity in EPH gestosis Wharton's jelly differs from control. The decrease in gelatinase activity may be one of the factors which promote the accumulation of collagen in this tissue.

Adolescent↗
PubMed2001

Glycosaminoglycans of normal veins and their alterations in varicose veins and varicose veins complicated by thrombophlebitis.

The aim of the study was to examine the content and molecular differentiation of glycosaminoglycans (GAGs) in the wall of varicose veins. The studied material consisted of normal, varicose veins and varicose veins complicated by thrombophlebitis collected during operations on 26 patients. In the wall of varicose veins the mean GAGs' content as well as the content of sulphated GAGs, except heparan sulphate was increased, whereas the amount of hyaluronic acid was decreased. Furthermore, the increased quantitative ratio between sulphated and nonsulphated GAGs was demonstrated. The results indicate an evident extracellular matrix remodelling in the wall of varicose veins particularly those complicated by thrombophlebitis, that is characterised by alterations in the content and molecular differentiation of GAGs.

Adult↗
PubMed2001

[Integrins and prolidase activity in uterine leiomyoma during tumor growth].

Collagens and proteoglycans are the main components of connective tissue. Prolidase plays an important role in the balance between collagen biosynthesis and degradation and its activity reflects the rate of collage turn-over. The activity of this enzyme is known to be regulated by interaction of collagen with beta 1 integrin receptor. It was found that increase in the uterine leiomyoma weight is accompanied by increased beta 1 integrin receptor expression and prolidase activity. It suggests that collagen turn-over is altered in uterine leiomyoma growth.

Cell Division↗
PubMed1999

[Extracellular matrix components in ovarian tumors].

This report describes the collagen, glycosaminoglycans and elastin--composition of ovarian tumours. Rearrangement of extracellular matrix in ovarian tumour has been found. There was an increase of total collagen content in comparison to control. Type I collagen was found to be predominant in both tissues. Both tissues, normal and neoplastic one, contain all known glycosaminoglycans. Among them dermatan sulphate was found to be the most abundant. In ovarian tumour an increase of this glycosaminoglycan content was observed.

Adult↗
PubMed1999

Accumulation of collagen in ovarian benign tumours.

Extracellular matrix components of benign ovarian tumours (cystadenoma, adenofibroma, cystadenofibroma) were analysed. The investigated tumours contained twice as much collagen than control ovarian tissues. Significant alterations in mutual quantitative relationships between collagens of various types were observed. The proportion of type I collagen decreased and that of type III collagen increased. The accumulation of collagen was accompanied by a reduction in sulphated glycosaminoglycan content whereas the amount of hyaluronic acid was not changed. Dermatan sulphate was the most abundant glycosaminoglycan component. It is suggested that the accumulation of collagen (natural barrier to the migration of tumour cells) and underexpression of glycosaminoglycans/proteoglycans (binding some growth factors and interleukins) may exert an inhibitory effect on tumour growth.

Adenofibroma↗
PubMed1998

Extracellular matrix components in uterine leiomyoma and their alteration during the tumour growth.

It was found that both normal human myometrium and uterine leiomyoma contain several glycosaminoglycans. In contrast to many normal and tumour tissues the amount of hyaluronic acid is very low and the proportional amount of sulphated glycosaminoglycans is distinctly higher. It is of interest that heparan sulphate is the major glycosaminoglycan component both in normal myometrium, and in leiomyoma. The amount of hyaluronic acid in myometrium and in the leiomyoma is very low. No significant change in hyaluronate content was observed during the tumour growth. In contrast to that the amount of some sulphated glycosaminoglycans (heparan sulphate, keratan sulphate, chondroitin sulphates and heparin) distinctly increased. 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 promote the tumour growth and stimulate collagen biosynthesis by tumour cells.

Collagen↗
PubMed1998

[Glycosaminoglycans in uterine leiomyoma].

During development of leiomyoma, a reorganisation of main components of connective tissue has been found. All types of glycosaminoglycans are present in this tissue. Among them the heparan sulphate is the most abundant. Its content was found to increase with uterine myoma weight. It is worthy of note that the increase of keratan sulphate is observed in big leiomyoma.

Female↗
PubMed1998

[Extracellular matrix components in leiomyosarcoma].

This report describes the glycosaminoglycans, collagen and elastin--composition of leiomyosarcoma. Studies were performed on leiomyosarcoma removed during surgery. The material was taken from 7 patients. Rearrangement of extracellular matrix in leiomyosarcoma has been found. There was an increase of total collagen content in comparison to control uterus. In both tissues type I collagen was found to be the predominant one. Both tissues, normal and neoplastic contain all known glycosaminoglycans types. Among them heparan sulphate was found to be the most abundant. A slight decrease in the content of this glycosaminoglycan was observed in leiomyosarcoma. A possible role of these alterations in tumour biology is discussed.

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↗
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↗
PubMed1993

Changes in IGF-binding proteins in rats with experimental diabetes.

The effects of streptozotocin-induced diabetes on proteolytic activity and collagen biosynthesis in skin lesions in rats and on IGF-I binding proteins in their serum were evaluated. It was found that both collagen in intact skin and collagen biosynthesis in skin lesions were lower compared to control animals. Concurrently, there was an increase in proteolytic activity both in intact and lesioned skin. The livers and sera of diabetic animals also showed higher proteolytic activity. Inhibitors of cathepsin D (pepstatin and potato-derived inhibitor) prevent the decrease of collagen biosynthesis in the skin of diabetic rats. These observations indicate the co-existence of two phenomena in the investigated animals: an increase in proteolytic activity in tissues and a decrease in collagen biosynthesis. Furthermore, the diabetic rats showed significant changes in the composition of IGF-I serum binding proteins. The amount of high molecular weight binding proteins (HMW-BPs) was distinctly decreased, whereas the content of low molecular weight binding proteins (LMW-BPs) was significantly increased. Large amounts of LMW-BPs have been previously found in the sera of fasted and scorbutic animals. They are inhibitors of IGF-I activity. It is suggested that the increase in LMW-BP concentration in diabetic serum may be responsible for the inactivation of IGF-I resulting in decreased collagen biosynthesis. The role of proteolysis in the production of LMW-BPs in diabetic serum is discussed.

Animals↗
PubMed1992

[Proteolytic and collagenolytic activities of the bovine vitreous body].

The vitreous contains collagen and soluble non-collagen proteins. The degeneration of collagen takes place in a different manner than in the other proteins. It has been detected that the cattle vitreous does not show any collagenolytic activity against the basic types of collagen (I, II, IX, and XI). The vitreous digests haemoglobin only in the acidic section of pH (optimum 3.5-4.5). No proteolytic activity towards Hb in physiological pH has been found.

Animals↗
PubMed1992

[Vitreous body proteins. IV. Proteolytic activity of the vitreous body in pathological conditions of the eye].

Two groups of proteins are present in the vitreous: collagen and non-collagen, deriving probably from the blood serum. The authors examined the proteolytic activity against haemoglobin in the course of some ocular pathological conditions. It was demonstrated that the vitreous digests haemoglobin in the acid division of pH (optimum--3.0-4.5) with various activity dependent on the pathological condition of the eye.

Cataract↗
PubMed1991

Proteolytic activity of vitreous-humour.

It has been found that the bovine vitreous--humour did not digest in vitro collagen at physiological and acidic pH. A proteolytic activity against haemoglobin in acid pH was found both in bovine and human vitreous-humours. The activity of human vitreous-humour increased significantly in endophtalmitis and glaucoma. In all pathological conditions studied the pH optima were at more acidic values than in control.

Animals↗