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1.
Allergy Asthma Proc ; 39(6): e71-e77, 2018 Nov 01.
Article in English | MEDLINE | ID: mdl-30401327

ABSTRACT

Background: Indoor air significantly impacts the incidence of rhinitis among residents of urban agglomerations. Objective: To assess the impact of indoor air pollution on rhinitis. Methods: Data were collected by using an European Community Respiratory Health Survey (ECRHS) and International Study of Asthma and Allergies in Childhood (ISAAC) standardized questionnaires (N = 18,617), and medical examinations were carried out (N = 4783) in selected Polish regions. For statistical analysis, the odds ratio (OR) was calculated with a 95% confidence interval to detect factors associated with rhinitis. The Wald test was performed to assess the significance of those factors. A value of p < 0.05 was considered statistically significant. Results: The most important factors associated with allergic rhinitis declared by adults, ages 20­44 years were the following: the age of the buildings (OR 1.34), presence of central heating system (OR 1.19), gas furnace used to heat the house (OR 1.19), solid-fuel stove (OR 1.92), and bottled-gas stove (OR 1.66). More frequent declarations of nonallergic rhinitis in the study group were associated with the use of a central heating system (children ages 6­7 years: OR 1.21; children ages 13­14 years: OR 1.22; and adults, ages 20­44 years: OR 1.27), solid-fuel stove (children ages 6­7 years: OR 2.95; children ages 13­14 years: OR 2.86; adults, ages 20­44 years: OR 2.02), and bottled-gas stove (children ages 6­7 years: OR 1.89; children ages 13­14 years: OR 1.88; adults, ages 20­44 years: OR 2.06). Diagnosed seasonal allergic rhinitis in adults, ages 20­44 years was associated with the year when the building was constructed (1970­1990) (OR 1.93) and the presence of a central heating system (OR 1.85). The year of construction of a building (1946­1969) (OR 4.84) as well as the use of central heating (OR 1.79) were causes of allergies to molds in the group of children ages 6­7 years, whereas sensitization to Dermatophagoides. pteronyssinus (OR 1.62) and Dermatophagoides farinae (OR 1.78) in children ages 6­7-years was associated with the presence of a central heating system. In children ages 13­14 years, the use of a solid-fuel stove was a cause of sensitization to D. farinae (OR 1.62). Conclusion: The age of the building, home heating systems, and pollution emitted by cooking appliances have a significant impact on the incidence of rhinitis. The highlights of the study included the following: (1) the age and condition of the building, the use of heating devices, stoves, and also mold allergens and house-dust mites contributed to a higher incidence of rhinitis, mainly among adults, ages 20­44 years; (2) gas-storage tanks and solid fuels contribute to rhinitis in the group of children ages 6­7 years and children ages 13­14 years.


Subject(s)
Air Pollution, Indoor/adverse effects , Rhinitis/epidemiology , Rhinitis/etiology , Urban Health , Urban Population , Adolescent , Adult , Child , Female , Humans , Male , Odds Ratio , Poland/epidemiology , Prevalence , Public Health Surveillance , Rhinitis/diagnosis , Risk Factors , Skin Tests , Young Adult
2.
J Anim Physiol Anim Nutr (Berl) ; 102(1): e364-e373, 2018 Feb.
Article in English | MEDLINE | ID: mdl-28608638

ABSTRACT

A study was conducted to investigate the influence of copper administration in ovo to chicken embryos and/or supplied in drinking water to growing chickens in the form copper nanoparticles (Cu-NP) or copper sulphate (CuSO4 ). The fertilised eggs were assigned to three groups (n = 50 per group): control (not injected), injected with 50 mg/kg Cu-NP or with 50 mg/kg CuSO4 at day 1 of incubation. Thereafter, 126 one-day-old broiler chickens were randomly assigned to seven post-hatched groups: control not injected and not provided with Cu in the drinking water, injected with 50 mg/kg Cu-NP + 20 mg/kg in water, not injected + 20 mg/kg Cu-NP in water, injected with 50 mg/kg CuSO4  + 20 mg/kg in water, not injected + 20 mg/kg CuSO4 in water, injected with 50 mg/kg Cu-NP and injected with 50 mg/kg CuSO4 . The experiment was carried out from day 1 to 35 post-hatching. The in ovo injection of Cu improved the final body weight, average daily gain and feed conversion ratio in relation to the control group. Conversely, the provision of Cu in the drinking water had less of an effect on growth performance in comparison with the injected groups. A significant improvement was shown in energy and nitrogen utilisation, being better for Cu-NP than CuSO4 . The cholesterol, urea and glucose levels in the blood were reduced by Cu-NP treatment in relation to the other groups. The relative weight of the liver was decreased, while bursa of Fabricius was increased in Cu groups in relation to the control group. Cu excretion was only reduced in chickens injected with 50 mg/kg Cu-NP + 20 mg/kg in water. The immune-related genes were not affected by the treatments. The in ovo injection of Cu-NP might improve broiler performance more efficiently than the injection of CuSO4 or the provision of Cu-NP and/or CuSO4 in drinking water.


Subject(s)
Chickens/blood , Copper Sulfate/pharmacology , Copper/pharmacology , Metal Nanoparticles/chemistry , Animal Feed , Animals , Copper/administration & dosage , Copper Sulfate/administration & dosage , Dietary Supplements , Energy Metabolism , Feces/chemistry , Weight Gain
3.
Comput Math Methods Med ; 2013: 597845, 2013.
Article in English | MEDLINE | ID: mdl-23401722

ABSTRACT

Results of epidemiological and public health surveys are often presented in the form of cross-classification tables. It is sometimes difficult to analyze data described in this way and to understand relations between variables. Graphical methods such as correspondence analysis are more convenient and useful. Our paper describes an application of correspondence analysis to epidemiological research. We apply the basic concepts of correspondence analysis like profiles, chi-square distance to medical data concerning prevalence of asthma. We aim at describing the relationship between asthma, region, and age. The data presented in this paper come from Epidemiology of Allergy in Poland (ECAP) survey in years 2006-2008. Correspondence analysis shows that there is a fundamental difference in the structure of age groups for people with symptoms compared to those who have declared asthma (regardless of the level of symptoms of asthma and the level of declaration). The variable which best differentiates declared asthma in all regions is "wheezing and whistling." Correspondence analysis also shows significant differences between locations. Our analyses are performed in the R package "ca".


Subject(s)
Asthma/epidemiology , Adolescent , Adult , Child , Data Interpretation, Statistical , Female , Geography , Health Surveys , Humans , Male , Odds Ratio , Poland , Prevalence , Public Health , Surveys and Questionnaires , Young Adult
4.
Placenta ; 26(10): 747-52, 2005 Nov.
Article in English | MEDLINE | ID: mdl-16226124

ABSTRACT

This study has assessed the amounts of insulin-like growth factor I (IGF-I), fibroblast growth factor (FGF), transforming growth factor beta (TGF-beta), platelet-derived growth factor (PDGF) and epidermal growth factor (EGF) and their binding to extracellular matrix components of Wharton's jelly. Studies were performed on the umbilical cords taken from human newborns delivered by healthy mothers. Wharton's jelly was separated and submitted to homogenisation and extraction with acetic acid and Tris-HCl buffer. The assays of growth factors were carried out with the use of ELISA commercial kits, together with SDS/polyacrylamide gel electrophoresis of tissue extracts followed by Western immunoblotting. Several growth factors, viz. acidic FGF, basic FGF, EGF, IGF-I, PDGF and TGF-beta were detected in Wharton's jelly. The amounts of these factors per gram of tissue vary from about 40 pg (EGF, PDGF) to about 200 ng (IGF-I). The amounts of peptide growth factors calculated per microgram of DNA are distinctly higher in Wharton's jelly in comparison to the umbilical cord artery. Western blot analysis demonstrated that almost the entire amount of these factors is bound to high molecular weight components. Since the number of cells in Wharton's jelly is very low and the amounts of extracellular matrix components are very high, it is concluded that the cells are strongly stimulated by peptide growth factors to produce large amounts of collagen and glycosaminoglycans.


Subject(s)
Growth Substances/metabolism , Umbilical Cord/metabolism , Adult , Blotting, Western , Enzyme-Linked Immunosorbent Assay , Epidermal Growth Factor/metabolism , Extracellular Matrix/metabolism , Female , Fibroblast Growth Factor 1/metabolism , Fibroblast Growth Factor 2/metabolism , Humans , Infant, Newborn , Insulin-Like Growth Factor I/metabolism , Platelet-Derived Growth Factor/metabolism , Pregnancy , Tissue Extracts/chemistry , Transforming Growth Factor beta/metabolism
5.
Biol Neonate ; 80(3): 202-9, 2001.
Article in English | MEDLINE | ID: mdl-11585983

ABSTRACT

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.


Subject(s)
Collagen/metabolism , Pre-Eclampsia/enzymology , Umbilical Cord/enzymology , Adolescent , Adult , Female , Gelatin/metabolism , Humans , Hydrogen-Ion Concentration , Infant, Newborn , Matrix Metalloproteinase 2/metabolism , Matrix Metalloproteinase 9/metabolism , Pregnancy
6.
Pathobiology ; 69(4): 212-8, 2001.
Article in English | MEDLINE | ID: mdl-12007280

ABSTRACT

OBJECTIVE: The role of proteoglycans (PGs) of the umbilical cord arteries (UCAs) in the pathomechanism of pre-eclampsia is not known. Therefore we decided to compare the PGs of normal (control) UCAs and those of newborns delivered by mothers with pre-eclampsia. METHODS: PGs were extracted in dissociative conditions, purified by Q-Sepharose anion exchange chromatography and lyophilized. They were analyzed by gel filtration and SDS-PAGE before and after treatment with chondroitinase ABC. RESULTS: It was found that the PG preparation from pre-eclamptic UCAs had a higher amount of sulphated glycosaminoglycans (in relation to protein) than in the case of control UCAs. The predominant PG fraction included small PGs with core proteins of 45 and 47 kD, immunologically related to biglycan (45 kD) and decorin (45 and 47 kD). The expression of decorin core proteins was increased and that of biglycan slightly decreased in pre-eclamptic UCAs. Some other putative small PG core proteins (56, 53, 49, 42, 38 and 34 kD) were also found. They were present in higher amounts in pre-eclamptic UCAs. Larger PGs (core proteins of 99-110 and >150 kD), were detected in lower amounts, both in control and particularly in pre-eclamptic material. CONCLUSION: Pre-eclampsia is associated with alterations in PG composition of the UCAs. They may affect the mechanical properties of this organ and disturb fetal blood circulation.


Subject(s)
Pre-Eclampsia/metabolism , Proteoglycans/metabolism , Umbilical Arteries/metabolism , Adult , Blotting, Western , Electrophoresis, Polyacrylamide Gel , Female , Gestational Age , Humans , Infant, Newborn , Pre-Eclampsia/etiology , Pre-Eclampsia/pathology , Pregnancy , Proteoglycans/classification , Umbilical Cord/blood supply
7.
Clin Chim Acta ; 302(1-2): 23-34, 2000 Dec.
Article in English | MEDLINE | ID: mdl-11074061

ABSTRACT

Edema, proteinuria, hypertension (EPH)-gestosis, known also as preeclampsia, is the most common, pregnancy-associated pathological syndrome. It is accompanied by a significant increase in collagen content in the umbilical cord arteries and premature replacement of hyaluronic acid by sulfated glycosaminoglycans both in these arteries and in Wharton's jelly. This remodelling of the umbilical cord tissues is accompanied by a distinct increase in insulin-like growth factor-I (IGF-I) concentration in the umbilical cord serum. Such a serum introduced into the culture medium of fibroblasts growing in vitro strongly stimulated the incorporation of radioactive proline into collagen (hydroxyproline-containing and collagenase-sensitive protein). Biosynthesis of noncollagenous proteins was not stimulated. Since IGF-I is known as a stimulator of collagen and sulfated glycosaminoglycan biosynthesis, the high concentration of this growth factor in the umbilical cord plasma may be an agent responsible for preeclampsia-associated remodelling of the umbilical cord, which results in dysfunction in fetal circulation.


Subject(s)
Collagen/biosynthesis , Fetal Blood , Pre-Eclampsia/blood , Adult , Carbon Radioisotopes , Cells, Cultured , Culture Media , Female , Fibroblasts/metabolism , Humans , Hydroxylation , Infant, Newborn , Insulin-Like Growth Factor I/metabolism , Pregnancy , Proline/metabolism
8.
Ginekol Pol ; 71(8): 773-6, 2000 Aug.
Article in Polish | MEDLINE | ID: mdl-11082920

ABSTRACT

EPH-gestosis is accompanied by an extensive remodelling of the extracellular matrix of the umbilical cord arteries, vein and Wharton's jelly. For better understanding of processes proceeding in it we decided to determine proteolytic activity in acidic pH range. Presented results suggest that cathepsin D is one of the main proteolytic enzymes of umbilical cord.


Subject(s)
Peptide Hydrolases/metabolism , Pre-Eclampsia/enzymology , Pregnancy Complications, Cardiovascular/enzymology , Umbilical Cord/enzymology , Female , Humans , Pregnancy
9.
Clin Chem Lab Med ; 38(7): 603-8, 2000 Jul.
Article in English | MEDLINE | ID: mdl-11028764

ABSTRACT

Wharton's jelly is abundant in extracellular matrix, which is known as a storage site to concentrate and stabilise growth factors in the vicinity of cells. It was previously found that Wharton's jelly contains significant amounts of insulin-like growth factor (IGF)-1 and IGF-binding proteins (BPs). IGF-1 is a stimulator of biosynthetics of collagen and sulphated glycosaminoglycans. Preeclampsia (edema, proteinuria, hypertension (EPH)-gestosis) is accompanied by an accumulation of sulphated glycosaminoglycans in Wharton's jelly. IGF-1 and BPs may play an important role in such a remodelling of this tissue. It was decided to evaluate the alterations in amounts of IGF-1 and BPs in Wharton's jelly of newborns delivered by mothers with preeclampsia. Studies were performed on Wharton's jelly of 10 controls and 10 newborns delivered by mothers with preeclampsia (edema, proteinuria > 500 mg/l, arterial pressure: systolic > 140 mm Hg, diastolic > 90 mmHg). Radioimmunological techniques were employed to determine IGF-1 and IGF-BPs (BP-1 and BP-3). It was found that preeclampsia is associated with a decrease in IGF-1 and IGF-BP-1 in Wharton's jelly. A slight increase in IGF-BP-3 was found. Ligand blotting demonstrated that BP-3 (not BP-1) is a main component of Wharton's jelly, which binds IGF-1. Heparin drastically inhibited the binding of IGF-1 by BP-3. It is known from our previous studies that preeclampsia is associated with an increase in the amount of sulphated glycosaminoglycans (heparin, heparan sulphate, dermatan sulphate) in Wharton's jelly. This may be a factor, which prevents the binding of IGF-1 by BPs and facilitates the binding of IGF-1 to cells, stimulating them to produce sulphated glycosaminoglycans in Wharton's jelly.


Subject(s)
Insulin-Like Growth Factor Binding Proteins/metabolism , Insulin-Like Growth Factor I/metabolism , Pre-Eclampsia/metabolism , Umbilical Cord/metabolism , Adult , Chromatography, Gel , Female , Humans , Infant, Newborn , Pregnancy , Radioligand Assay , Umbilical Cord/chemistry
10.
Mol Cell Biochem ; 206(1-2): 133-9, 2000 Mar.
Article in English | MEDLINE | ID: mdl-10839203

ABSTRACT

It is known that extracellular matrix components (ECM) may serve as a storage site to concentrate and stabilize growth factors in the vicinity of cells. IGF-I is expressed in most fetal tissues and it is involved in anabolic effects on protein and sulphated glycosaminoglycans biosynthesis, cell proliferation and differentiation. We demonstrated that human umbilical cord (UC) tissues contain large amounts of IGF-I and IGF-I-binding proteins (BP-3 and BP-1). Particularly Wharton's jelly appears to be an abundant reservoir of IGF-I and BPs. Relatively low amount of cells and large amounts of collagen and glycosaminoglycans in UC tissues (especially in Wharton's jelly) suggest that IGF-I may play a major role in stimulation of these cells to produce ECM components. The specific BPs in these tissues may be important modulators of IGF-I action during fetal development.


Subject(s)
Insulin-Like Growth Factor Binding Proteins/analysis , Insulin-Like Growth Factor I/analysis , Umbilical Cord/chemistry , Chromatography, Gel , Electrophoresis, Polyacrylamide Gel , Female , Humans , Infant, Newborn , Insulin-Like Growth Factor Binding Proteins/isolation & purification , Insulin-Like Growth Factor I/isolation & purification , Pregnancy , Radioimmunoassay , Radioligand Assay , Tissue Extracts
11.
Eur J Clin Invest ; 30(5): 389-96, 2000 May.
Article in English | MEDLINE | ID: mdl-10809899

ABSTRACT

BACKGROUND: Extracellular matrix (ECM)-components serve as a storage site to concentrate and stabilise growth factors in the vicinity of cells. Human umbilical cord (UC) tissues contain significant amounts of IGF-I and IGF-binding proteins (BPs). IGF-I is known as a stimulator of collagen and sulphated glycosaminoglycans (GAGs) biosynthesis. Pre-eclampsia, the most common pregnancy associated syndrome, is accompanied by an accumulation of collagen and sulphated glycosaminoglycans in the UC. One may expect that IGF-I and BPs play an important role in such a remodelling of the UC tissue. For this reason it was decided to evaluate the alterations in amounts of IGF-I and BPs in UC serum and in the UC arterial wall of newborns delivered by mothers with pre-eclampsia. MATERIALS AND METHODS: Studies were performed on the UCs of 12 control and 12 investigated newborns, delivered by mothers with pre-eclampsia (edema, proteinuria > 500 mg l-1, arterial pressure: systolic > 140 mmHg, diastolic > 100 mmHg). Radioimmunological techniques were employed to determine IGF-I and IGF-BPs (BP-1 and BP-3). RESULTS: It was found that pre-eclampsia is associated with an increase of IGF-I concentration in the UC serum and with simultaneous decrease of its content in the umbilical cord artery (UCA). The decrease of IGF-I content in the UCA wall was accompanied by an increase of BP-3 and BP-1 in this tissue. The increase in BPs content in the UCA wall was not associated with an enhancement of IGF binding by extracts from the homogenates of arterial wall. Heparin drastically decreased the binding of IGF-I by BP-3. CONCLUSIONS: Pre-eclampsia is associated with an increase of IGF-I-concentration in the umbilical cord blood and an elevation of BPs contents in the UCA wall. Despite a high concentration of binding proteins, IGF-I is not accumulated in this tissue. High amounts of sulphated GAGs in the UCA wall may be a factor that prevents the binding of IGF-I by BPs. Free IGF-I can easily bind to cell receptors and stimulate the cells to produce collagen and sulphated GAGs in the arterial wall.


Subject(s)
Insulin-Like Growth Factor I/metabolism , Pre-Eclampsia/metabolism , Umbilical Cord/metabolism , Adult , Chromatography, Gel , Female , Humans , Infant, Newborn , Insulin-Like Growth Factor Binding Protein 1/analysis , Insulin-Like Growth Factor Binding Protein 1/blood , Insulin-Like Growth Factor Binding Protein 3/analysis , Insulin-Like Growth Factor Binding Protein 3/blood , Insulin-Like Growth Factor I/analysis , Iodine Radioisotopes , Ligands , Pregnancy , Radioimmunoassay
12.
Ginekol Pol ; 71(2): 78-84, 2000 Feb.
Article in Polish | MEDLINE | ID: mdl-10765603

ABSTRACT

It has been observed high risk of infections in neonates as a result from lymphocytes immaturity. It is connected to phenotype differences of lymphocytes between neonates and adults. This high susceptibility to infections is especially high in premature neonates. With the use of flow cytometry we have evaluated the phenotype of cord blood lymphocytes in premature neonates. In comparison to results of healthy newborns we have observed significant decrease in CD7+, CD3+, CD4+, CD25+, CD57+ lymphocytes an increase in total number of CD8+ cells as well as alteration in CD4/CD8 ratio. Our results suggest deeply damage of cellular immunity in preterm infants.


Subject(s)
Antigens, CD/immunology , Fetal Blood/immunology , Lymphocytes/immunology , Antibodies, Monoclonal/immunology , Female , HLA-DR Antigens/immunology , Humans , Immunity, Cellular/immunology , Infant, Newborn , Infant, Premature , Male , Phenotype
13.
Eur J Obstet Gynecol Reprod Biol ; 88(2): 189-95, 2000 Feb.
Article in English | MEDLINE | ID: mdl-10690679

ABSTRACT

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.


Subject(s)
Collagen/metabolism , Gelatinases/metabolism , Pre-Eclampsia/enzymology , Umbilical Arteries/metabolism , Adult , Electrophoresis, Polyacrylamide Gel , Enzyme Activation/drug effects , Female , Humans , Hydrogen-Ion Concentration , Infant, Newborn , Phenylmercuric Acetate/analogs & derivatives , Phenylmercuric Acetate/pharmacology , Pregnancy , Sulfhydryl Reagents/pharmacology , Trypsin/pharmacology , p-Chloromercuribenzoic Acid/pharmacology
14.
Z Geburtshilfe Neonatol ; 204(6): 229-31, 2000.
Article in English | MEDLINE | ID: mdl-11199152

ABSTRACT

BACKGROUND: alpha 1-antitrypsin (A-1-AT) is an acute-phase protein. It is present in plasma and other extracellular fluids and in human trophoblastic tissue. It accounts for 80 to 90 per cent of antiprotease reactions occurring in plasma. It has the ability to greatly affect enzyme activity and plays an important role in immunomodulatory processes. MATERIALS AND METHODS: The purpose of the study was to determine the plasma concentration of A-1-AT in mothers giving birth to hypotrophic (small for gestational age, SGA), and eutrophic (appropriate for gestational age, AGA) infants. 33 women who gave birth to SGA infants and 36 women who gave birth to AGA infants participated in the study. The control group consisted of 30 non-pregnant women who were of reproductive age. All women gave birth at term. To measure A-1-AT concentration, we used the diffusion method described by Mancini et al. RESULTS: The highest concentration of A-1-AT (379 mg/dl) was found in women giving birth to SGA infants, compared with 345 mg/dl for women giving birth to AGA infants. In the control group, the concentration was found to be 270 mg/dl. CONCLUSIONS: Statistical analysis of the results showed a significant difference between the two groups of women gave birth and between each parturient compared with control subjects. Increasing concentration of A-1-AT in the plasma of women in labor may be the result of an acute phase reaction triggered by the stress during parturition. Additionally, increased concentrations of A-1-AT in women who gave birth to SGA rather than AGA infants suggest that it may play a role in the processes of intrauterine growth retardation (IUGR).


Subject(s)
Fetal Growth Retardation/blood , Infant, Small for Gestational Age , alpha 1-Antitrypsin/metabolism , Acute-Phase Reaction/blood , Adult , Birth Weight , Female , Humans , Infant, Newborn , Postpartum Period/blood , Pregnancy , Reference Values
15.
Acta Biochim Pol ; 47(4): 1081-91, 2000.
Article in English | MEDLINE | ID: mdl-11996098

ABSTRACT

Proteoglycans (PGs) were dissociatively extracted from human umbilical cord arteries (UCAs) with 4 M guanidine hydrochloride containing Triton X-100 and protease inhibitors, purified by Q-Sepharose anion exchange chromatography and lyophilized. They were analysed by gel filtration, SDS/PAGE and agarose gel electrophoresis before and after treatment with chondroitinase ABC. It was found that the PG preparation was especially enriched in chondroitin/dermatan sulphate PGs. The predominant PG fraction included small PGs that emerged from Sepharose CL-2B with Kav = 0.74. Their molecular mass, estimated by SDS/PAGE, was 160-200 kDa and 90-150 kDa, i.e. it was typical for biglycan and decorin, respectively. Treatment with chondroitinase ABC yielded the core proteins of 45 and 47 kDa, characteristic for both small PGs. Remarkable amounts of the 45 kDa protein were detected in non-treated PG samples, suggesting the presence of free core proteins of biglycan and decorin. Large PGs were present in lower amounts. In intact form they were eluted from Sepharose CL-2B with Kav = 0.17 and 0.43. Digestion with chondroitinase ABC yielded the core proteins with a molecular mass within the range of 180-360 kDa but predominant were the bands of 200, 250 and 360 kDa. The large PGs probably represent various forms of versican or perlecan bearing chondroitin sulphate chains.


Subject(s)
Proteoglycans/chemistry , Umbilical Cord/blood supply , Umbilical Cord/metabolism , Chondroitin ABC Lyase/pharmacology , Chondroitin Sulfate Proteoglycans/chemistry , Electrophoresis, Agar Gel , Electrophoresis, Polyacrylamide Gel , Heparan Sulfate Proteoglycans/chemistry , Humans , Infant, Newborn , Kinetics , Lectins, C-Type , Octoxynol/pharmacology , Protease Inhibitors/pharmacology , Proteoglycans/isolation & purification , Proteoglycans/metabolism , Versicans
16.
Przegl Lek ; 57(12): 717-9, 2000.
Article in Polish | MEDLINE | ID: mdl-11398594

ABSTRACT

We tested the concentration of alpha-2-macroglobulin in sera of 33 women bearing eutrophic newborns, 36 women bearing hypotrophic newborns and 30 healthy not pregnant women in reproductive age. The concentration of this inhibitor was measured using radial immunodiffusion method according to Mancini et al. We found distinct decrease of alpha-2-macroglobulin concentration in sera of bearing women. In women bearing eutrophic newborns we found 154 mg/dl, in women bearing hypo-trophic newborns 171 mg/dl whereas in controls 250 mg/dl. We have noted statistically significant differences between tested groups to controls and between investigated groups. Taking under consideration the role of alpha-2-macroglobulin as the modulator of immune system as well as the activity of several cytokins, therefore one can suppose that alpha-2-M may affect on cellular growth developed foetus in intrauterine.


Subject(s)
Fetal Growth Retardation/physiopathology , Infant, Small for Gestational Age/growth & development , alpha-Macroglobulins/analysis , Adult , Female , Humans , Infant, Newborn , Maternal-Fetal Exchange , Pregnancy
17.
Pathobiology ; 68(6): 264-9, 2000.
Article in English | MEDLINE | ID: mdl-11493759

ABSTRACT

OBJECTIVE: Edema, proteinuria, hypertension (EPH) gestosis, also known as preeclampsia, is the most common, pregnancy-associated pathological syndrome. It is accompanied by a significant increase in collagen content in the umbilical cord arteries and early replacement of hyaluronic acid by sulfated glycosaminoglycans (GAGs) both in these arteries and in Wharton's jelly. Such a remodelling of the umbilical cord tissues is accompanied by an increase in insulin-like growth factor-I (IGF-I) concentration in the umbilical cord serum. METHODS: Contact-inhibited human fibroblasts were incubated in Dulbecco culture medium containing control or EPH umbilical cord serum and supplemented with (14)C-glucosamine or (35)S-sulfate. Radioactive GAGs were isolated, submitted to electrophoretic fractionation and quantified. RESULTS: The presence of umbilical cord serum in culture medium strongly stimulated the incorporation of (14)C-glucosamine and (35)S-sulfate into GAGs synthesized by these cells. EPH serum was much more active in stimulation of sulfated GAGs biosynthesis than control serum, whereas the biosynthesis of hyaluronic acid was stimulated by both sera to a similar degree. CONCLUSION: Since IGF-I is known as a stimulator of collagen and sulfated GAG biosynthesis, the high concentration of this growth factor in the umbilical cord plasma may be responsible for preeclampsia-associated remodeling of the umbilical cord.


Subject(s)
Fetal Blood/physiology , Glycosaminoglycans/biosynthesis , Pre-Eclampsia/blood , Pre-Eclampsia/metabolism , Umbilical Cord/metabolism , Adult , Cells, Cultured , Female , Fibroblasts/metabolism , Humans , Hyaluronic Acid/biosynthesis , Infant, Newborn , Insulin-Like Growth Factor I/biosynthesis , Maternal-Fetal Exchange , Pregnancy
18.
Ginekol Pol ; 70(9): 600-3, 1999 Sep.
Article in Polish | MEDLINE | ID: mdl-10534922

ABSTRACT

Alpha-2-antiplasmin is a main inhibitor of plasmin and play a crucial role in regulation of intravascular fibrinolysis. It is important to know, in pregnant women as well in the immediate post partum period the activation of hemostasis takes place and is observed thrombotic incidences. In our studies we have included 33 pregnant women whose delivered eutrophic newborns alpha-2-AP 7.79 mg/dl and 36 pregnant women whose delivered small-for-date newborns, alpha-2-AP 7.49 mg/dl. We found no significant statistically differences between tested groups and in comparison to control group 6.0 mg/dl. The presented results seems to indicate, the determination of concentration of alpha-2-AP in sera of women in immediate post partum period does not reflect the changes in the mechanisms of fibrinolytic system in the course of the partum.


Subject(s)
Postpartum Period/physiology , alpha-2-Antiplasmin/analysis , Female , Fibrinolysis/physiology , Humans , Pregnancy
19.
Biol Neonate ; 76(3): 144-52, 1999 Sep.
Article in English | MEDLINE | ID: mdl-10460952

ABSTRACT

Oedema, proteinuria, hypertension (EPH)-gestosis (pre-eclampsia) is associated with a premature replacement of hyaluronic acid by sulphated glycosaminoglycans (GAGs), both in the umbilical cord arteries and in Wharton's jelly. It may be concluded from our previous report that such a phenomenon may be the result of reduction in degradation of these compounds. In order to support such a conclusion the activities of GAG-degrading enzymes in normal umbilical cord arteries and those taken from newborns delivered by mothers with EPH-gestosis were compared. It was found that EPH-gestosis results in a significant reduction in the activities of neutral endoglycosidases degrading most of the sulphated GAGs (except keratan sulphate). In the case of acidic endoglycosidases, no characteristic alterations have been found. Only the activity of heparan sulphate-degrading endoglycosidase significantly decreased. In contrast to the above-mentioned endoglycosidases, the activities of arylsulphatase B and 6-sulphatase distinctly increased. The decrease in the activities of endoglycosidases are thought to be responsible for EPH-gestosis-associated accumulation of sulphated GAGs in extracellular matrix of Wharton's jelly. This leads to the suspicion that EPH-gestosis-induced changes in the GAGs composition may alter the fibrillogenesis conditions in Wharton's jelly. The sulphated GAGs accumulated in Wharton's jelly may interact with some growth factors which modify the myofibroblasts' proliferation, gene expression, protein biosynthesis and other processes. A significance of EPH-gestosis-induced alteration in Wharton's jelly is discussed.


Subject(s)
Glycosaminoglycans/metabolism , Glycoside Hydrolases/metabolism , Pre-Eclampsia/enzymology , Sulfatases/metabolism , Umbilical Cord/enzymology , Chondroitin Sulfates/metabolism , Dermatan Sulfate/metabolism , Female , Heparin/metabolism , Heparitin Sulfate/metabolism , Humans , Hydrogen-Ion Concentration , Infant, Newborn , Keratan Sulfate/metabolism , Pregnancy , beta-Galactosidase/metabolism , beta-N-Acetylhexosaminidases/metabolism
20.
Clin Chem Lab Med ; 37(4): 417-21, 1999 Apr.
Article in English | MEDLINE | ID: mdl-10369112

ABSTRACT

Edema, proteinuria, hypertension (EPH)-gestosis is associated with a premature replacement of hyaluronic acid by sulphated glycosaminoglycans (GAGs), both in the umbilical cord arteries (UCAs) and in Wharton's jelly. This phenomenon may be considered as a sign of premature ageing of the umbilical cord tissues. The decrease in hyaluronic acid content in the UCA was found to be the result of reduced biosynthesis of this substance, whereas an increase in sulphated GAGs-content is rather a result of slower degradation of newly synthesised GAGs. In this study the activities of GAGs-degrading enzymes in normal umbilical cord arteries and those taken from newborns delivered by mothers with EPH-gestosis were compared. It was found that EPH-gestosis results in a significant reduction in the activities of neutral endoglycosidases degrading most of the sulphated glycosaminoglycans (with the exception of heparan sulphate). The activities of exoglycosidases also decrease but to a lesser degree. These alterations are thought to be responsible for EPH-gestosis-associated accumulation of sulphated glycosaminoglycans in the extracellular matrix of the arterial wall. Such remodelling of the arterial wall may affect foetal blood circulation. The significance of these phenomena in the pathological mechanism of EPH-gestosis is discussed.


Subject(s)
Endothelium, Vascular/enzymology , Endothelium, Vascular/metabolism , Glycosaminoglycans/metabolism , Pre-Eclampsia/metabolism , Umbilical Arteries/enzymology , Umbilical Arteries/metabolism , Female , Glycoside Hydrolases/metabolism , Humans , Infant, Newborn , Male , Pre-Eclampsia/enzymology , Pregnancy
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