PLACENTAL PROTEOMIC PROFILE DURING PHYSIOLOGICAL AND PREECLAMPSIA-COMPLICATED PREGNANCY
Objective. To reveal changes in the preeclamptic placental proteomic spectrum. Subject and methods. Thirty-two women, among whom there were 17 women with preeclampsia who formed a study group and 15 women with physiological pregnancy who were included in a control group, were examined. Placental proteomic analysis was made using two-dimensional electrophoresis and time-of-flight mass spectrometry. Results. The performed studies could reveal and identify difference proteins, the rate of whose production was considerably different in physiological pregnancy and preeclampsia. Among the proteins with decreased expression, there was α-tropomyosin, actin-related protein 2/3 complex subunit 2, cytoplasmic actin 1, annexin A4, 20S proteasome, and 60S acidic ribosomal protein. The proteins with increased expression included the molecular chaperones heat shock protein (Hsp60) and endoplasmin, as well as peroxidoxin-4, mitochondrial aconitate hydratase, and 14-3-3 protein epsilon. Conclusion. The established differences in the placental proteomic spectrum obviously reflect impaired molecular cell interactions in the maternal-placental-fetal system in preeclampsia-complicated pregnancy.