Training health workers for magnesium sulfate use reduces case fatality from eclampsia: results from a multicenter trial.

OBJECTIVE: To investigate the effectiveness of an intervention aimed at improving the case management of eclampsia. DESIGN: A multi-center intervention study. SETTING: Six teaching hospitals in Nigeria. SAMPLE: Clinical records of cases of eclampsia treated before and 1 year after the intervention. METHODS: Doctors and midwives in selected hospitals were re-trained to manage eclampsia using magnesium sulfate according to the Pritchard protocol. MAIN OUTCOME MEASURES: Eclampsia case fatality rates, maternal and perinatal mortality rates before and after the intervention. RESULTS: A total of 219 cases of eclampsia were managed over a 12-month period. There were seven maternal deaths. The post intervention case fatality rate of 3.2% was significantly less than the pre-intervention rate of 15.1% (p < 0.001). The overall maternal and perinatal mortality ratios and rates respectively in the hospitals declined from 1199.2 to 954 per 100,000 deliveries and 141.5 to 129.8 per 1000 births, respectively (p > 0.05). CONCLUSION: An intervention to build the capacity of care-providers to use an evidence-based protocol for the treatment of eclampsia in Nigeria was successful in reducing associated case fatality rate. The increased and widespread use of such an intervention in maternity units might contribute to the reduction of maternal mortality in low-income countries.

In vitro development and characterization of a manatee bronchial cell line.

In the present study, culture conditions that promote the growth and differentiation of manatee respiratory tract epithelial cells toward a mucociliary phenotype were determined. Characterization of a manatee-specific cell line enables investigators to conduct in vitro testing where live-animal experimentation is not possible. Cell cultures were established from both explants and enzymatically dissociated cells that were isolated from manatee bronchial tissue. To modulate their differentiation, bronchial epithelial cells were grown on Transwell collagen membranes either submerged or at an air-liquid interface. Growth on a collagen membrane at an air-liquid interface and medium supplemented with retinoic acid was required to promote a mucociliary phenotype. When cells were grown in submerged cultures without retinoic acid, they appeared more squamous and were not ciliated. Intracellular keratin proteins were detected in both submerged and interface cultures. Cultured manatee bronchial epithelial cells will facilitate future studies to investigate their potential role in pulmonary disease associated with brevetoxicosis after exposure to the red-tide organism, Karenia brevis.

Isolation, characterization, and structure of a mutant 89 Arg----Cys bisphosphoglycerate mutase. Implication of the active site in the mutation.

Bisphosphoglycerate mutase (EC 5.4.2.4.) is a trifunctional enzyme which displays synthase, mutase, and phosphatase activities. The purification, characterization, and structural study of an abnormal form of the enzyme, isolated from a patient which we reported earlier (Rosa, R., Prehu, M. O., Beuzard, Y., and Rosa, J. (1978) J. Clin. Invest. 62, 907-915), is described. The abnormal enzyme, present at 50% of the level of the normal enzyme as estimated by immunological methods, showed elevated electrophoretic mobility and hybridized with erythrocyte phosphoglycerate mutase (EC 5.4.2.1.) in the same manner as the normal control. The mutant enzyme was unstable at 55 degrees C and could be protected against thermal instability by 0.5 mM glycerate 2,3-bisphoshate but not by either glycerate 3-phosphate or glycolate 2-phosphate. Two of the three functions of the mutant enzyme were distinct from those of the normal protein. The specific activity of the synthase was 0.57% of normal and that of the mutase 4.1%. By contrast, the specific phosphatase activity was not affected by the mutation. However, the phosphatase activity of the mutated protein was markedly less stimulated by glycolate-2-phosphate than that of the control. High performance liquid chromatography analysis of tryptic peptides derived from the mutant enzyme showed an abnormal profile with the absence of two peaks normally containing the T12 and T13 peptides and without the appearance of a supplementary peak. Amino acid sequence and mass spectrometric analysis demonstrated the substitution of Arg----Cys residue in position 89 producing an uncleaved T12-T13 present in the same peak as the T6. Considered together, our data suggest that Arg-89 is located at or near the active site of bisphosphoglycerate mutase and that this residue is probably involved in the binding of monophosphoglycerates.