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Biomedical subjects

Z Galewska

Publications and source records attributed to Z Galewska.

13 recordsLinked to original sources
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↗
PubMed2000

EPH-gestosis (pre-eclampsia)-induced decrease of gelatinase activity may promote an accumulation of collagen in the umbilical cord artery.

It was found in our previous paper that edema, proteinuria, hypertension (EPH)-gestosis-associated accumulation of collagen in the umbilical cord artery (UCA) is a result of increased biosynthesis and decreased degradation of this protein. It is known that the activity of collagenolytic enzymes is a main factor regulating collagen degradation rate in various tissues. For this reason it was decided to evaluate the effect of EPH-gestosis on the activity of proteolytic enzymes which may be involved in collagen degradation in the UCA wall. Proteolytic activity against bovine serum albumin, reconstituted collagen fibres and gelatin were evaluated. Latent forms of proteolytic enzymes were activated by the action of trypsin, p-chloromercuric benzoate (PCMB) and p-aminophenylmercuric acetate (APMA). A low activity of gelatinase (type IV collagenase) was detected in the extracts from the wall of the umbilical cord artery. This enzyme increased its activity several times after the action of trypsin, PCMB and APMA. EPH-gestosis results in a distinct reduction in gelatinase activity. Despite the action of activating agents the gelatinase from EPH-gestosis UCAs was considerably lower in comparison to control UCAs. It can be concluded that gelatinase of the umbilical cord artery forms an inactive complex with a tissue inhibitor of metalloproteinases. Such a complex dissociates under the action of trypsin, PCMB or APMA or sodium dodecyl sulphate. The decrease of gelatinolytic activity in the umbilical cord artery may be a factor that reduces the breakdown of collagen in the arterial wall and promotes an accumulation of this protein. The accumulation of collagen with simultaneous reduction in elastin content in the UCA may be the factors which reduce the elasticity of arterial wall and decrease the blood flow in the fetus of woman with EPH-gestosis.

Adult↗
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↗
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↗
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↗
PubMed1990

The effect of some antiinflammatory drugs on collagen of rat fibrous cartilage.

The use of SDS-polyacrylamide gel electrophoresis of the cyanogen bromide derived peptides from fibrous cartilage collagens enabled to calculate type I to type II collagen ratio in this tissue. Some of the investigated drugs (acetylsalicylic acid, colchicine) changed this ratio without having a significant effect on total collagen content in fibrous cartilage.

Animals↗
PubMedDate not supplied

[Increased proteolytic activity of cathepsin D in the skin of rats after administration of various anti-inflammatory drugs].

Cathepsin D activity and type I and III collagens content in the skin of rats treated with some antiinflammatory drugs (acetylsalicylic acid, phenylbutazone, indomethacin, colchicine and prednisone) were evaluated. It was found that investigated drugs evoke increased activity of cathepsin D and decreased collagen content (mainly type I) in this tissue. The correlation between type I collagen content and proteolytic activity was noticed.

Animals↗
PubMedDate not supplied

The effect of some antiinflammatory drugs on collagen of rat skin.

Collagen content and mutual relationship between type I and type III collagens in the skin of rats chronically treated with some antiinflammatory drugs were evaluated. It was found that prednisone, colchicine, acetylsalicylic acid, indomethacin and phenylbutazone induce a decrease of collagen content in rat skin. In the case of prednisone, acetylsalicylic acid and phenylbutazone modification of type I to type III collagen ratio in rat skin was observed. These observations suggest that non-steroid antiinflammatory drugs may exert similar effects on skin collagen as steroid hormones.

Animals↗