Biomedical subjects

Zofia Galewska

Publications and source records attributed to Zofia Galewska.

7 recordsLinked to original sources

PubMed2006

Pre-eclampsia-associated alterations in decorin, biglycan and versican of the umbilical cord vein wall.

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. STUDY DESIGN: Study was performed on the umbilical cord veins taken from 10 newborns delivered by healthy mothers (control group) and from 10 newborns delivered by mothers with pre-eclampsia. Proteoglycans were extracted in dissociative conditions, purified by Q-Sepharose anion exchange chromatography and lyophilised. Decorin, biglycan and versican were analysed by SDS-PAGE followed by Western blotting before and after treatment with chondroitinase ABC. The amounts of decorin, biglycan and versican core proteins were assessed by ELISA method. RESULTS: We found that both control and pre-eclamptic umbilical cord vein wall contained all the three proteoglycans. ELISA assay showed the amounts of the core proteins of decorin, biglycan and versican were distinctly higher in pre-eclamptic material in comparison to control vessel. Western blotting confirmed that the expression of all these proteoglycan core proteins increased in pre-eclampsia. They featured in the same electrophoretic mobility-45 and 47 kDa for decorin, 45 kDa for biglycan, and 300 and 320 kDa for versican. CONCLUSION: The content of decorin, biglycan and versican in the umbilical cord vein wall is elevated in pre-eclampsia in comparison to the corresponding control vessel. These alterations may affect the mechanical properties of this vessel and disturb foetal blood circulation.

Adult↗

PubMed2006

The effect of Chlamydia trachomatis infection of the prostate gland on the concentration of citric acid.

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. MATERIALS AND METHODS: The study involved 60 patients with chronic prostatitis (NIH III). Urethral swabs and expressed prostatic secretions (EPS) were collected for analysis. The urethral swabs were tested for PMNs and the presence of Neisseria gonorrhoeae and C.t., while the EPS were analyzed to determine PMN count, C.t., and citric acid concentration. The DFA or LCR method was used for C.t. diagnosis. The concentration of citric acid was measured using the UV method. RESULTS: Inflammation of the prostate (PMNs >/=10/field) was diagnosed in 58.3 of the patients. C.t. infection was found in 20%, including 8.3% with only the urethra affected and 10% with only the prostate. One patient had both the urethra and the prostate infected. A reduction in the concentration of citric acid in EPS was observed in 56.7% of the men. In 88.2% of the patients, reduced citric acid concentration was accompanied by an elevated PMN count in the EPS. All patients with C.t. infection of the prostate showed a reduced concentration of citric acid. In five patients with urethral infection, lack of a decrease in this parameter was noted in one. In all the patients with chlamydial infection, irrespective of localization, a high PMN count was observed in the EPS. CONCLUSIONS: Determination of the concentration of citric acid in the prostatic fluid is a good indicator of prostatitis. C.t. infection of the prostate gland is accompanied by a decrease in the concentration of citric acid.

Adolescent↗

PubMed2005

Pre-eclampsia-associated alterations in Wharton's jelly proteoglycans.

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). The aim of the present study was to compare the proteoglycan composition of Wharton's jelly of newborns delivered by healthy mothers and those with pre-eclampsia. Proteoglycans from pre-eclamptic Wharton's jelly had a higher sulphated glycosaminoglycan/protein ratio than those of normal tissue. Pre-eclampsia is associated with a lower level of all proteoglycan core proteins, especially those of higher molecular mass (such as versican), although the same set of core proteins were found in normal and pre-eclamptic Wharton's jelly. The alterations in the proteoglycan composition of Wharton's jelly may affect the mechanical properties of the umbilical cord and, in the case of pre-eclampsia, disturb foetal blood circulation.

Adult↗

PubMed2005

Preeclampsia-associated reduction of cathepsin D activity in the umbilical cord.

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. MATERIALS AND METHODS: Umbilical cord components were separated and submitted to homogenisation/extraction with 0.05 M Tris-HCl+0.2% Triton X-100, pH 7.5. Proteolytic activities of the extracts were studied with a use of cathepsin D-specific substrate. Western immunoblot technique was employed to detect this enzyme. RESULTS: It was found that human umbilical cord tissues contain both active and inactive forms of cathepsin D. Preeclampsia is associated with a distinct increase in the amount of this enzyme in the umbilical cord, whereas its activity deeply decreased. Activation with trypsin augments cathepsin D activity in preeclamptic umbilical cord to the values observed in control arteries or even exceeds the control values (veins, Wharton's jelly). CONCLUSIONS: Preeclampsia is associated with a reduction in the activity of cathepsin D in human umbilical cord. The low activity of cathepsin D may reduce collagen degradation and enhance its accumulation in the umbilical cord, especially in the arteries. Similar changes in other foetal blood vessels may result in an increase of vascular resistance and hypertension, which may persist after birth.

Adult↗

PubMed2003

Pre-eclampsia (EPH-gestosis)-induced decrease of MMP-s content in the umbilical cord artery.

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. RESULTS: A low amount of MMP-1 (collagenase 1), MMP-9 (gelatinase B) and MMP-3 (stromelysin 1) was detected in the extracts from the wall of the umbilical cord artery. MMP-2 (gelatinase A) is the main collagenolytic enzyme in UCA wall (both latent and active form). Pre-eclampsia is associated with a distinct reduction in those metalloproteinases content in comparison to control UCAs. It can be concluded from zymography that MMP-2 (gelatinase A) of the umbilical cord artery forms an inactive complex with a tissue inhibitor of metalloproteinases (TIMP). Such a complex dissociates under the action of p-aminophenylmercuric acetate (APMA) or sodium dodecyl sulphate. CONCLUSIONS: The decrease of metalloproteinases content and activity in the umbilical cord artery may be a factor that reduces the breakdown of collagen in the arterial wall and promotes the accumulation of this protein. The accumulation of collagen with simultaneous reduction in elastin content in the UCA may be the factor that reduces the elasticity of arterial wall and decreases the blood flow in the fetus of women with pre-eclampsia.

Adult↗

PubMed2002

Preeclampsia-associated decrease of potential collagenolytic and gelatinolytic activities in the wall of the umbilical cord vein.

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. This decrease may result from reduced collagen biosynthesis or enhanced collagen degradation. It was decided to evaluate whether or not this phenomenon is associated with alterations in the activities of collagenolytic, gelatinolytic and non-specific proteolytic enzymes that may be involved in collagen degradation, as well as the activity of prolidase which provides proline as a substrate for collagen biosynthesis. Studies were performed on the umbilical cord veins of newborns delivered by healthy mothers and those with preeclampsia. The control vein extract, activated with trypsin, degraded reconstituted collagen fibres (64.4+/-2.9 nmol Hyp x mg(-1) protein), whereas the preeclamptic material demonstrated only a trace activity. The venous wall extract contained a latent form of gelatinase that might have been activated by trypsin and 4-aminophenylmercuric acetate. A decrease in the gelatinolytic and proteolytic activities of preeclamptic vein extract at neutral pH was found. Prolidase activity was almost 3-fold lower in the preeclamptic extract (240.6+/-29.3 nmol Pro x min(-1) x mg(-1) protein) in comparison to the control (608.2+/-63.7 nmol Pro x min(-1) x mg(-1)protein). It was concluded that the umbilical cord vein contains a latent form of gelatinase A. The decrease in prolidase activity may reduce collagen biosynthesis, resulting in a decrease of this protein in the preeclamptic umbilical cord vein.

Case-Control Studies↗

PubMed2002

[Gelatinolitic and proteolytic activity of Wharton's jelly in EPH-gestosis (preeclampsia)].

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. The decrease in gelatinase activity in EPH-gestosis may be one of factors involved in extracellular matrix rebuilding of Wharton's jelly.

Female↗