Divergent changes in the content and activity of MMP-26 and TIMP-4 in human umbilical cord tissues associated with preeclampsia.

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. Some reports have indicated that the expression of matrilysin 2 and tissue inhibitor of matrix metalloproteinase 4 (TIMP-4) is coordinately regulated during progression of various diseases. STUDY DESIGN: Therefore, we decided to assess the expression and activity of MMP-26 and TIMP-4 in normal and preeclamptic umbilical cord tissues - umbilical cord arteries (UCA), vein (UCV) and Wharton's jelly (WJ). Tissues obtained from 10 normal (control material) and 10 preeclamptic umbilical cords were assessed using immunoenzymatic assay, Western immunoblotting, reverse transcriptase - polymerase chain reaction and fluorometric determination of the enzyme activity. RESULTS: All umbilical cord tissues, both control and preeclamptic, expressed MMP-26 and TIMP-4 in macromolecular complexes. Preeclampsia induced a significant increase in the content and actual activity of MMP-26 in UCV and WJ, as compared to control. The content of TIMP-4 in preeclamptic UCV and WJ was reduced. The content of MMP-26 mRNA was lower in UCA and UCV, whereas higher in WJ in preeclampsia. CONCLUSIONS: Divergent changes in MMP-26 mRNA and protein expression suggest a difference in the factors controlling the matrilysin synthesis in healthy and preeclamptic subjects. The decrease in TIMP-4 content in preeclamptic UCV might be the main reason for significantly higher actual activity of MMP-26 in that tissue. Only in preeclamptic Wharton's jelly the changes were compatible in terms of the content and activity of MMP-26 and TIMP-4. It cannot be excluded that similar alterations can be observed for the whole vascular system of newborns delivered by mothers with preeclampsia.

Distribution of cathepsin L in human umbilical cord tissues.

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. Cathepsin L activity and anti-papain inhibitory effect of cysteine protease inhibitors were quantified in extracts of separated umbilical cord tissues using fluorogenic substrates. The results were calculated per DNA content. The enzyme expression was assessed by Western immunoblotting. The active cathepsin L activity (without activation by pepsin digestion), its percentage in the total activity (after pepsin activation), and the expression of the mature single-chain enzyme were the lowest in the umbilical cord arteries and the highest in Wharton's jelly. The effect of cysteine protease inhibitors showed similar distribution as in the case of the active enzyme, being the highest in Wharton's jelly. Distribution of the activity and expression of mature cathepsin L within the umbilical cord probably results from distinctions in the proenzyme activation process. Differences in the action of cysteine protease inhibitors can partly restrict divergences in the enzyme activity that could reflect its expression alone. Differential enzyme action seems to contribute to tissue-specific collagen turnover within the umbilical cord cells, especially those of Wharton's jelly.

Cathepsin B in human myometrium and in uterine leiomyomas at various stages of tumour growth.

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). Tissue extracts were assayed for cathepsin B activity and for inhibitory effect of cysteine protease inhibitors against papain using fluorogenic substrates, and calculated per DNA content. Statistical analysis was performed by Kruskal-Wallis analysis of variance followed by Dunn's post hoc tests. The enzyme expression was evaluated by SDS/polyacrylamide gel electrophoresis followed by Western immunoblotting. RESULTS: In all the investigated tissues cathepsin B exists mainly in a fully processed double-chain form. The enzyme activity and expression were similar in control myometrium and in small leiomyomas. However, they distinctly increased during tumour growth. The effect of cysteine protease inhibitors was comparable in all the tissues examined. CONCLUSION: These data suggest that the enhanced activity and expression of cathepsin B but not the action of cysteine protease inhibitors contribute to an increased remodelling of extracellular matrix and bioavailability of various growth factors, which favour leiomyoma growth.

Differential distribution of cathepsin B in human umbilical cord tissues.

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. We assessed the activity and expression of cathepsin B in the umbilical cord arteries, veins and Wharton's jelly. Extracts of separated umbilical cord components were subjected to an activity assay with the use of specific fluorogenic substrate. The expression of cathepsin B protein was qualitatively evaluated by Western immunoblotting and quantitatively determined with an immunoenzymatic method. The total cathepsin B activity and content calculated per gram of DNA were higher in Wharton's jelly than in the umbilical cord vessels, and the latter parameter was the lowest in the umbilical cord arteries. Moreover, the expression and the activity of latent cathepsin B (following activation by pepsin digestion) calculated per gram of DNA were the highest in Wharton's jelly and the lowest in the umbilical cord arteries. High expression and activity of latent, pepsin-activatable cathepsin B related to DNA content in Wharton's jelly seem to reflect the stimulation of its cells by high amounts of collagen I and growth factors.

Extracellular matrix remodeling of the umbilical cord in pre-eclampsia as a risk factor for fetal hypertension.

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. Matrix metalloproteinases (MMPs) are engaged in degradation of extracellular matrix proteins and activation/inactivation of certain cytokines and enzymes. These enzymes will probably play a central role in the release of matrix-embedded cytokines and growth factors. MMP-2 (gelatinase A) is the main collagenolytic enzyme of both umbilical artery and vein. Other metalloproteinases are present in several times lower amounts. Reduced activity of collagen-degrading enzymes may be a factor, which enhances the accumulation of collagen and some other proteins in the pre-eclamptic umbilical cord tissues. It seems to be possible that similar alterations occur in other fetal blood vessels. It may result in an increase in peripheral resistance as well as an increase in the blood pressure in the fetal vascular system. Some observations suggest that the raised pressure may persist after birth. Pre-eclampsia may be a factor that evokes an initiation of hypertension in utero and its amplification through childhood and adulthood.

Matrix metalloproteinases, MMP-7 and MMP-26, in plasma and serum of control and preeclamptic umbilical cord blood.

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. STUDY DESIGN: Studies were performed on the umbilical cord blood taken from 10 control (healthy) newborns and 10 newborns of preeclamptic women. We used Western immunoblotting, immunoenzymatic assay (ELISA) and zymography techniques for detection of matrilysins. The results were submitted to Student's t-test and Mann-Whitney test. RESULTS: Umbilical cord blood plasma and serum of control and preeclamptic newborns contained MMP-7 and MMP-26. Both enzymes existed in the form of complexes with other extracellular matrix components and/or their tissue inhibitors in control and preeclamptic subjects. Free latent forms of both matrilysins were observed after the action of reducing agent. Furthermore, we found a distinct increase in the amount of MMP-26 in preeclamptic umbilical cord (UC) blood. No significant differences in MMP-7 content and activity in control and preeclamptic UC blood were observed. CONCLUSIONS: MMP-7 and MMP-26 could activate MMP-9 by cleavage of some sites in pro-MMP-9. Our results suggest that the high activity of MMP-9 participates in a proteolytic release of peptide growth factors from their complexes with extracellular matrix components, which facilitate their interaction with membrane receptors and stimulate cell division and extracellular matrix synthesis in these cells. It may be one of the mechanisms of extracellular matrix remodelling in the umbilical cord of preeclamptic newborns.

The evaluation of markers of prostatic inflammation and function of the prostate gland in patients with chronic prostatitis.

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. trachomatis infection (ligase chain reaction). RESULTS: Increased PMN cell counts (> or =10 per high-power field) were found in 73.9% of patients and increased PMN elastase concentration (<250 ng/ml) in 78.3%. In 44.4% of the patients the elastase concentration indicated moderate (250-1000 ng/ml) and in 55.6% acute infection (> or =1000 ng/ml). Decreased citric acid concentration (<18.12 mg/ml) in the EPS was found in 65.2% of the men. C. trachomatis prostate infection was detected in 17.4% of the patients and all of these men had higher inflammation parameters and lower citric acid concentrations. CONCLUSIONS: C. trachomatis prostate inflammation was accompanied by an increase in inflammation markers and a decrease in citric acid concentration.

Gelatinase matrix metalloproteinase (MMP)-2 and MMP-9 of the umbilical cord blood in preeclampsia.

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. RESULTS: We found that both umbilical cord blood plasma and serum of controls and preeclamptic newborns contained MMP-2 and MMP-9, as well tissue inhibitors of metalloproteinase (TIMP)-1 and TIMP-2. The umbilical cord plasma of preeclamptic subjects contained large amounts of MMP-9 in a form of complexes with other plasma components, and zymographic analysis demonstrated increased gelatinolytic activity at a position corresponding to MMP-9, compared to control samples. By contrast, MMP-2, TIMP-1 and TIMP-2 data showed no significant differences between preeclamptic and control samples. CONCLUSIONS: The high activity of MMP-9 in preeclamptic plasma suggests its participation in the proteolytic release of peptide growth factors from their complexes with other matrix components, with subsequent stimulation of cell division and matrix biosynthesis. We suggest this might represent one of the mechanisms for matrix remodeling in the umbilical cord of preeclamptic newborns.

Fatty acid composition of triacylglycerols from Wharton's jelly determined by high-performance liquid chromatography.

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. The quantitative determination of those derivatives was performed at 254 nm. Preeclampsia, the most common pregnancy complication, did not affect triacylglycerol content in the umbilical cord Wharton's jelly in comparison to the control material. However, it changed the composition of fatty acids, bound to that lipid class. The method allows the determination of almost all fatty acids forming the investigated neutral lipid class, contained in a solid tissue sample. The use of TEAP buffer excluded precipitation and flow stoppage in the HPLC system. The method reduced time and costs and might be useful for all other lipid classes and different tissues.

Separation and Determination of Fatty Acids from Lipid Fractions by High-Performance Liquid Chromatography: Cholesterol Esters of Umbilical Cord Arteries.

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.We decided to develop a method for separation and determination of fatty acids from different tissues by high-performance liquid chromatography. That method allowed us to determine cholesteryl ester composition and content in umbilical cord arteries. Studies were performed on the umbilical cord arteries taken from 10 newborns delivered by healthy mothers and 10 newborns delivered by mothers with preeclampsia. Cholesteryl esters were isolated by thin layer chromatography. Fatty acids were liberated by basic hydrolysis and analyzed by HPLC of their p-bromophenacyl derivatives using detection at 254 nm. It was found that saturated fatty acids were the main group of fatty acids incorporated to cholesteryl esters in all control and preeclamptic umbilical cord arteries. Preeclampsia caused a significant increase in cholesteryl ester content in the umbilical cord arteries. An increase of neutral lipid content in vessel walls of newborns delivered by mothers with preeclampsia may be one of the factors that evoke the initiation of hypertension in utero and its amplification throughout childhood and adult life. The described method reduces time and cost consumption and allows us to determine almost all fatty acids forming cholesteryl esters contained in the tissue sample.

Antichlamydial antibodies and citric acid in patients with chronic prostatitis.

INTRODUCTION: The aim of the study was to evaluate the correlation between the presence of anti-C. trachomatis (C.t.) antibodies in serum and expressed prostatic secretions (EPS) and the concentration of citric acid in patients with chronic prostatitis. MATERIALS AND METHODS: The study involved 34 men with chronic prostatitis. The leukocyte count, presence of anti-C.t. antibodies (IgA, IgG), and citric acid concentration were determined in the EPS. The serum was examined for IgM, IgA, and IgG anti-C.t. antibodies. Specific antibodies were determined using the EIA method. The concentration of citric acid was measured using the ultraviolet method. RESULTS: Inflammation of the prostate (210 PMN) was found in 61.8% of the patients. A reduction in citric acid concentration in the EPS was detected in 58.8% of the men. Specific serum antibodies were detected in 58.8% of the patients, including 23.5% with IgM, 32.4% with IgA, and 44.1% with IgG. In all patients, serum IgM and IgA antibody titers were low, while those of IgG antibodies were strongly positive in 46.7% of the patients. Anti-C.t. antibodies in the EPS were detected in 44.1% of the patients, including 32.4% with IgA and 35.3% with IgG. In contrast to serum, the titers of IgG antibodies in the EPS were low in all the patients, while those of IgA were strongly positive in 54.5% of cases. In patients with positive serological outcomes, 85% had reduced concentrations of citric acid. CONCLUSIONS: The occurrence of anti-C.t. antibodies is usually accompanied by a decrease in the concentration of citric acid in the prostatic secretion.

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.

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.

The inhibitory effect of preeclamptic umbilical cord blood serum on matrix metalloproteinase-1 in arterial slices incubated in vitro.

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. A significant role in collagen degradation is attributed to matrix metalloproteinase (MMP)-1 (collagenase 1) and tissue inhibitors of metalloproteinases (TIMPs). OBJECTIVE: To compare the effects of umbilical cord (UC) blood serum of control and preeclamptic newborns on the content and activity of MMP-1, TIMP-1 and TIMP-2 in UCA wall slices incubated in vitro. METHODS: Polyacrylamide gel electrophoresis (PAGE) followed by Western immunoblotting allowed to detect MMP-1 as well as TIMP-1 and TIMP-2. The amounts of MMP-1, TIMP-1 and TIMP-2 in UCA slices were measured by immunoenzymatic method (ELISA). MMP-1 activity in the arterial wall was measured using a collagenase-1-specific substrate. RESULTS: Western immunoblot analyses detected MMP-1, TIMP-1 and TIMP-2 in the incubation fluids and in extracts from the UCA wall. Both 43- and 55-kDa (a zymogen) bands of MMP-1 were visible. The control UC serum stimulated both the amount as well as actual and potential activities of MMP-1 in the arterial wall in a time-dependent manner. In contrast to controls, the preeclamptic serum did not exert such an effect. CONCLUSIONS: The small amount and low activity of MMP-1 accompanied by elevated amounts of TIMPs (especially TIMP-1) decelerate the degradation and enhance the accumulation of collagen in the preeclamptic UCA wall.

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.

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.

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.

[Gelatinolitic and proteolytic activity of Wharton's jelly in EPH-gestosis (preeclampsia)]. / Aktywnosc enzymów zelatynolitycznych i proteolitycznych galarety Whartona w przebiegu gestozy EPH (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.

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.