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1.
Med Oncol ; 34(1): 4, 2017 Jan.
Article in English | MEDLINE | ID: mdl-27900590

ABSTRACT

Patients with multiple myeloma (MM) are at increased risk of thrombosis. Growing evidence indicates that oxidative and nitrative modifications of proteins, including fibrinogen, may lead to changes in hemostasis. The study compares samples from patients with MM at diagnosis and healthy volunteers with regard to the oxidative/nitrative modifications of proteins, ROTEM and thrombin-catalyzed fibrin polymerization. The content of carbonyl groups in plasma proteins of patients with MM was significantly higher than in controls (2.981 vs. 1.807 nmol/mg of protein, p = 0.005), while no differences were seen in the concentrations of nitrated proteins. Maximum clot firmness readings were significantly higher in the samples of patients than in controls according to FIBTEM test (23.5 vs. 15 mm, p = 0.006). The lag time of the fibrin polymerization process and the velocity of clot lysis (V Lys) were found to be significantly higher in the group of MM patients than controls. In contrast, no marked differences were identified between studied groups in reference to maximal velocity of fibrin polymerization process (V max), maximal absorbance (A max) and plasmin amidolytic activity values. In conclusion, our study demonstrates that at the time of diagnosis, patients with MM demonstrated greater oxidative stress than healthy volunteers, which is reflected in a higher amount of carbonylated proteins. Some prothrombotic features found in ROTEM tests in MM patients were not confirmed by turbidimetry.


Subject(s)
Blood Proteins/metabolism , Fibrinogen/metabolism , Multiple Myeloma/blood , Oxidative Stress/physiology , Adult , Aged , Aged, 80 and over , Biomarkers, Tumor/blood , Case-Control Studies , Enzyme-Linked Immunosorbent Assay , Female , Humans , Male , Middle Aged , Multiple Myeloma/diagnosis , Multiple Myeloma/diagnostic imaging , Nitrosation , Plasminogen/metabolism , Streptokinase/blood , Thrombelastography/methods
3.
Ginekol Pol ; 72(12): 1092-5, 2001 Dec.
Article in Polish | MEDLINE | ID: mdl-11883216

ABSTRACT

OBJECTIVES: We present data of three years experience of management and outcome of preterm labour. MATERIALS AND METHODS: The study comprised 335 pregnant women with preterm labour. We analyzed the pharmacological therapy and way of labour. There were two groups of patients: I group--180 patients who had cesarean delivery, II group--155 patients who had vaginal delivery. RESULTS: It has been found 7.54% more cesarean delivery than vaginal delivery of preterm labour.


Subject(s)
Delivery, Obstetric/methods , Delivery, Obstetric/statistics & numerical data , Obstetric Labor, Premature/epidemiology , Adolescent , Adult , Cesarean Section/statistics & numerical data , Decision Making , Female , Humans , Infant, Newborn , Poland/epidemiology , Pregnancy , Pregnancy Outcome
4.
Ginekol Pol ; 71(11): 1373-8, 2000 Nov.
Article in Polish | MEDLINE | ID: mdl-11216146

ABSTRACT

The course of multiple pregnancies and multiple fetus labor were analyzed in 111 women delivered in the Department of Obstetrics, School of Medicine in Lublin in the years 1991-1998. It has been found that the most frequent patients were those aged 25-29 coming from the cities and after the infertility treatment. The aim of this research was to characterize twin pregnant patients, and present the outcome of multiple pregnancy. The studies were performed on 67 women from the cities and 44 women from the villages. It is significant that almost 55% pregnant women underwent the cesarean section and their average birth weight was 2490 g. These results indicate that multiple pregnancy is in high risk pregnancy.


Subject(s)
Pregnancy Outcome , Pregnancy, Multiple/statistics & numerical data , Adult , Birth Weight , Cesarean Section/statistics & numerical data , Female , Humans , Infertility, Female/therapy , Maternal Age , Obstetrics and Gynecology Department, Hospital/statistics & numerical data , Poland , Pregnancy , Pregnancy, High-Risk , Retrospective Studies , Risk Factors , Urban Health
5.
Clin Nephrol ; 23(3): 142-7, 1985 Mar.
Article in English | MEDLINE | ID: mdl-2985309

ABSTRACT

The aim of this work was to determine the activity of helix-destabilizing protein (HD-protein), which is indispensable in basic genetic processes such as DNA replication, genetic recombination and transcription, in lymphocytes of patients with different morphological types of glomerulonephritis and with chronic renal insufficiency, treated conservatively and by maintenance hemodialysis. The estimation was done on 44 patients with glomerulonephritis and on 20 patients with chronic renal insufficiency. The control group consisted of 20 healthy individuals. The investigations prove the fact that in human lymphocytes helix-destabilizing protein occurs, and its quantity enables us to determine its activity in the diseased and healthy state. Measurement of HD-protein activity seems to be a good marker of the altered lymphocyte function. Especially high HD-protein activity was noticed in cases of acute glomerulonephritis, lupus glomerulonephritis and in the active forms of chronic glomerulopathies. Generally, the tested parameter showed a positive correlation with the activity of the glomerulonephritic process. In lymphocytes of patients with chronic renal insufficiency treated conservatively, a greater activity of helix-destabilizing protein occurred than in the control group. Lymphocytes from patients with chronic renal insufficiency, treated with repetitive maintenance hemodialysis, did not reveal significant differences in HD-protein activity, determined directly before hemodialysis and after its completion, in comparison to the control group of healthy individuals.


Subject(s)
DNA Helicases/blood , DNA-Binding Proteins , Glomerulonephritis/blood , Kidney Failure, Chronic/blood , Lymphocytes/metabolism , Ribonucleoproteins , Thymus Hormones , Viral Proteins , Adolescent , Adult , Female , Heterogeneous Nuclear Ribonucleoprotein A1 , Heterogeneous-Nuclear Ribonucleoprotein Group A-B , Humans , Male , Middle Aged , Pyelonephritis/blood , Time Factors
6.
Int Urol Nephrol ; 15(3): 273-9, 1983.
Article in English | MEDLINE | ID: mdl-6654634

ABSTRACT

Studies on the adenosine deaminase (ADA) and aldolase activities in lymphocytes were performed in 67 patients with glomerulonephritis (gn) and in 20 healthy individuals from the control group to get an insight into the lymphocyte metabolism. Statistically significant decrease of ADA activity was found in the groups of patients with chronic proliferative gn, membranoproliferative gn, membranous gn and lupus nephritis in comparison with the healthy individuals from the control group. As far as decrease of aldolase activity is concerned it has reached statistical significance in patients with mesangial gn, membranoproliferative gn, membranous gn and lupus nephritis. The lymphocyte metabolism did not show any abnormalities in the enzymatic indicators only in patients with acute proliferative gn and submicroscopic gn. The activity comparison between both enzymes in the lymphocytes, contrasted on the basis of high and low clinical dynamics of gn, revealed a tendency to lower ADA and aldolase activities in patients with high clinical dynamics. However, this difference was at the limit of statistical significance (p less than or equal to 0.10).


Subject(s)
Adenosine Deaminase/blood , Fructose-Bisphosphate Aldolase/blood , Glomerulonephritis/enzymology , Lymphocytes/enzymology , Nucleoside Deaminases/blood , Adult , Female , Humans , Male , Middle Aged
7.
Acta Biochim Pol ; 28(3-4): 275-84, 1981.
Article in English | MEDLINE | ID: mdl-6805183

ABSTRACT

1. Penicillin amidase from Proteus rettgeri was purified 580-fold by a four-step chromatographic procedure. Titration with phenylmethanesulphonyl fluoride showed that the purified preparation contains 53% of the enzyme. 2. The molecular weight of the amidase was found to be 65.000. The enzyme is strongly inhibited by N-bromosuccinimide and zinc ions. It hydrolyses penicillins, cephalosporins and some synthetic substrates, and in addition it catalyses synthesis of ampicillin from methyl ester of phenylglycine and 6-aminopenicillanic acid. 3. The immobilized amidase obtained by copolymerization of the chemically modified enzyme with acrylamide was applied for preparative hydrolysis of benzylpenicillin.


Subject(s)
Amidohydrolases/isolation & purification , Penicillin Amidase/isolation & purification , Proteus/enzymology , Bacteria/enzymology , Metals/pharmacology , Molecular Weight , Penicillin Amidase/antagonists & inhibitors , Penicillin G/metabolism , Penicillin V/metabolism , Substrate Specificity , Time Factors
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