Publications by authors named "Zofia Galewska"

Objectives: Preeclampsia is the most common disorder associated with pregnancy. Our earlier findings revealed a substantial increase in the amount of matrix metalloproteinase-26 (matrilysin 2; MMP-26) in preeclamptic umbilical cord blood. The role of MMP-26 in preeclamptic umbilical cord tissue has not been fully elucidated.

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The extracellular matrix components show specific distribution patterns within various structures of the umbilical cord, among which Wharton's jelly is especially collagen-rich tissue. Cathepsin L is a potent cysteine protease engaged in degradation of extracellular matrix proteins, including collagens. We evaluated the activity and expression of cathepsin L, and the inhibitory effect of cysteine protease inhibitors in the umbilical cord arteries, vein and Wharton's jelly.

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Objective: Cathepsin B is a major cysteine protease involved in the degradation of extracellular matrix proteins, as well as in the activation of precursor forms of other proteases and in release of matrix-bound growth factors. We assessed the expression and activity of cathepsin B, and the inhibitory effect of cysteine protease inhibitors in human myometrium and uterine leiomyomas at various stages of tumour growth.

Study Design: Studies were performed on human myometrium collected from 12 patients and on uterine leiomyomas of various weights: small (less than or equal to 25 g, taken from 10 patients) and large (more than or equal to 100 g, obtained from 13 patients).

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The extracellular matrix components are differentially distributed among various structures of the umbilical cord. Wharton's jelly is especially rich in collagens and growth factors. Cathepsin B is a major cysteine protease involved in collagen degradation, as well as in the activation of precursor forms of other collagenolytic enzymes and growth factors.

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The human umbilical cord forms a connection between the placenta and the foetus. It is composed of two arteries and one vein surrounded by Wharton's jelly. Pre-eclampsia is accompanied by extensive remodeling of extracellular matrix of umbilical cord.

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Objective: Our previous paper demonstrated that preeclampsia-associated accumulation of collagen and proteoglycans in the umbilical cord tissues is a result of increased biosynthesis and decreased degradation of these components. Metalloproteinases (MMPs) are enzymes engaged in degradation of collagen and protein cores of proteoglycans, including those which bind peptide growth factors. Some MMPs, among them matrilysins MMP-7 and MMP-26, participate in activation other members of the MMP family.

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Preeclampsia is accompanied by an extensive remodeling of the extracellular matrix of umbilical cord. It is associated with an increase in collagen content in the umbilical cord artery. Furthermore, preeclampsia distinctly reduces proteolytic and gelatinolytic activity, especially after activation with various agents.

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Introduction: The aim of the study was to determine the numbers of polymorphonuclear (PMN) leukocytes and PMN elastase and citric acid concentrations in chronic prostatitis patients regardless of etiology and in those with Chlamydia trachomatis infection of the prostate gland.

Materials And Methods: The study involved 46 patients with chronic prostatitis. Expressed prostatic secretions (EPS) were obtained to determine the leukocyte count, PMN elastase (ELISA) and citric acid concentrations (UV method), and the occurrence of C.

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Background: Preeclampsia is associated with accumulation of collagen and proteoglycans in the umbilical cord tissues as a result of increased biosynthesis and decreased degradation of these components. Matrix metalloproteinases (MMPs) are enzymes engaged in the degradation of collagen and the protein core structures of proteoglycans, including those which bind peptide growth factors.

Methods: We used Western immunoblots, immunoenzymatic assay (ELISA) and zymography techniques for the detection of gelatinases and their inhibitors.

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The improved method for HPLC determination of fatty acids was proposed. The chromatographic separation of p-bromophenacyl derivatives of fatty acids under a gradient elution was achieved at 40 degrees C with an RP-18 LiChroCART 5 column and organic mobile phase containing methanol, acetonitrile, water and TEAP buffer pH 5.6.

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Background: Our previous studies demonstrated that preeclampsia is accompanied by significant alterations in the amounts of peptide growth factors in the umbilical cord serum. Some of these factors (especially IGF-1) are known as regulators of collagen metabolism. The umbilical cord arteries (UCAs) of newborns delivered by mothers with preeclampsia contain more than twice the amount of collagen in comparison to newborns delivered by healthy mothers.

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Introduction: The aim of the study was to evaluate the correlation between the presence of anti-C. trachomatis (C.t.

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Objective: The role of proteoglycans in the rearrangement of the extracellular matrix of the umbilical cord vein wall in pre-eclampsia is not known. Decorin, biglycan and versican are the main proteoglycans of the umbilical cord vein wall. We decided to test whether the amounts of these proteoglycans alter in pre-eclampsia.

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Introduction: The objective of the study was to assess the relationship between Chlamydia trachomatis (C.t.) infection of the prostate and the concentration of citric acid.

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Proteoglycans of Wharton's jelly contain mainly chondroitin/dermatan sulphate chains. The predominant proteoglycan is decorin (core proteins of 45 and 47 kDa), although the core proteins of biglycan (45 kDa), versican (260 kDa) and of other proteoglycans (90, 110, 220 kDa) were also detected (Gogiel et al., 2003).

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Background: Preeclampsia is accompanied by an increase of collagen contents in the umbilical cord (UC) arteries and in Wharton's jelly. Cathepsin D is one of the enzymes which participates in collagen degradation and activates precursor forms of collagenolytic metalloproteinases. It was decided to evaluate the activity of cathepsin D within umbilical cord arteries, veins and Wharton's jelly and its alterations in preeclampsia.

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Background: It was found in our previous paper that pre-eclampsia-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.

Methods: For this reason it was decided to evaluate the effect of pre-eclampsia on the content and activity of metalloproteinases by immunoenzymatic method (ELISA), zymographic technique and with the use of specific substrates.

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EPH-gestosis is accompanied by an extensive remodeling of the extracellular matrix of Wharton's jelly. The gelatinolytic and proteolytic activities were measured. A decrease in gelatinolityc activity and an increase in proteolytic activity in EPH-gestosis were observed.

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Preeclampsia is the most common pathological syndrome associated with pregnancy. It is accompanied by remodelling of the extracellular matrix of the umbilical cord. A decrease of collagen content in the umbilical cord vein was described.

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