ABSTRACT
The aim of this study was to investigate the relationship between plasma endothelin 1 (ET-1) levels and T helper (Th)-1:Th2 cell immunity in women with preeclampsia. The percentage of Th1 and Th2 cells and the Th1:Th2 cell ratios in peripheral blood from 11 normal pregnant women and 11 patients with preeclampsia at 29-34 weeks of gestation were calculated using flow cytometry. The plasma ET-1 level was also determined using a modified radioimmunoassay. The plasma ET-1 concentrations and the Th1:Th2 cell ratios in normal pregnancies were significantly lower than those in patients with preeclampsia. Negative correlations were found between plasma ET-1 levels and Th2 cells in both the preeclamptic pregnancy groups and in the normal pregnant women. Our results indicate that elevated ET-1 levels are associated with a Th1:Th2 imbalance in preeclampsia.
Subject(s)
Endothelin-1/blood , Pre-Eclampsia/immunology , Th1 Cells/immunology , Th2 Cells/immunology , Adult , Birth Weight , Female , Flow Cytometry , Gestational Age , Humans , Infant, Newborn , Lymphocyte Count , PregnancyABSTRACT
The percentages of Th1 and Th2 cells and the Th1:Th2 ratios in peripheral blood from 22 patients with a singleton pregnancy at 30 and 36 weeks' gestation, on admission for the spontaneous onset of labor pains, at 1 minute after placental delivery and on day 7 after delivery were determined using flow cytometry. The percentages of Th1 and Th2 cells and the ratio of Th1:Th2 did not markedly change during 30 weeks' gestation and 1 minutes after placental delivery. However, the percentage of Th2 cells had decreased significantly at 7 days after delivery. In addition, the Th1:Th2 cell ratios were significantly elevated on day 7 after delivery. Thus, the termination of pregnancy may not be associated with a change in maternal Th1:Th2-immunity.
Subject(s)
Labor, Obstetric/immunology , Th1 Cells/cytology , Th2 Cells/cytology , Adult , Birth Weight , CD4 Lymphocyte Count , Female , Humans , PregnancySubject(s)
Hemodynamics/drug effects , Hypertension, Pulmonary/physiopathology , Nifedipine/pharmacology , Oxygen/pharmacology , Pulmonary Emphysema/physiopathology , Tuberculosis, Pulmonary/physiopathology , Chronic Disease , Humans , Hypertension, Pulmonary/etiology , Oxygen/blood , Oxygen Consumption/drug effects , Pulmonary Emphysema/complications , Tuberculosis, Pulmonary/complicationsSubject(s)
Electromyography , Gastrectomy/methods , Gastric Mucosa/surgery , Stomach/physiology , Animals , DogsABSTRACT
It was found that the absorption spectrum of beta-naphthyl triphosphate is different from that of beta-naphthyl diphosphate in the range 290-335 nm. Thus, beta-naphthyl triphosphate hydrolysis by heavy meromyosin can be recorded continuously as a function of time by means of a spectrophotometer. By analyzing the time course, the apparent kinetic parameters were easily and rapidly obtained. If necessary, the true kinetic parameters, including the product dissociation constants, can be estimated spectrophotometrically. Beta-Naphthyl triphosphate hydrolysis was inhibited competitively by ATP. By analyzing the time course, it was, therefore, possible to estimate the kinetic parameters of ATP hydrolysis indirectly, and resonable values were obtained. Beta-Naphthyl triphosphate hydrolysis by heavy meromyosin was performed under various conditions. Unlike that of ATP, the hydrolysis of beta-naphthyl triphosphate was inhibited monotonously by treatment of heavy meromyosin with p-hydroxymercuribenzoate.
Subject(s)
Myosin Subfragments/metabolism , Naphthols/metabolism , Organophosphorus Compounds/metabolism , Adenosine Triphosphatases/metabolism , Hot Temperature , Hydrolysis , Hydroxymercuribenzoates/pharmacology , Kinetics , Protein Denaturation , Spectrophotometry, Ultraviolet , TemperatureABSTRACT
Fluorescent organic phosphates, beta-naphthyl diphosphate, beta-naphthyl triphosphate, and beta-naphthyl tetraphosphate, were synthesized from beta-naphthyl monophosphate using Pi and N,N'-dicyclohexylcarbodiimide. These organic phosphates were interacted with bovine oxyhemoglobin, all in no buffer, 0.1 M NaCl, at 25 degrees and in the pH range 5.5-7.0. Equilibrium binding parameters were determined by measuring the fluorescence quenching upon their interaction. It is indicated that bovine oxyhemoglobin has more than one binding site, one of which is very strong. The strength of binding to the stronger site is in the order beta-naphthyl tetraphosphate greater than beta-naphthyl triphosphate greater than beta-naphthyl diphosphate. The logarithms of association constants of these phosphates depend linearly on the net charges of these phosphates at any pH. The results were accounted for by electrostatic effects using a simple charge model. In that model, the average positive net charges in oxyhemoglobin involved in the binding of beta-naphthyl phosphate are shown as a function of pH. It is shown that the binding of these fluorescent organic phosphates is prevented reversibly by the excess addition of nonfluorescent organic and iorganic phosphates, inositol hexaphosphate, tripolyphosphate, and pyrophosphate. Assuming competitive binding in a single strong site, the association constants of these nonfluorescent phosphates were also determined by measuring the recovery of the fluorescence intensity upon the release of fluorescent phosphates. At pH 6.18, the association constant of pyrophosphate is lower than that of tripolyphosphate by one order.
