Glycosylation pattern and axin expression in normal and IUGR placentae

The aim of this study was to investigate the protein glycosylation pattern and AXIN1 protein expression in human placentae of normal pregnancies and compare them with placentae of pregnancies complicated with intrauterine growth restriction (IUGR). A total of 38 placentae (17 placentae of IUGR fetus...

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Published inThe journal of maternal-fetal & neonatal medicine Vol. 28; no. 5; p. 558
Main Authors Vukasovic, Andreja, Grbesa, Durdica, Nikuseva Martic, Tamara, Kusec, Vesna, Miskovic, Berivoj, Serman, Alan, Soken, Nikolina, Serman, Ljiljana
Format Journal Article
LanguageEnglish
Published England 01.03.2015
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Summary:The aim of this study was to investigate the protein glycosylation pattern and AXIN1 protein expression in human placentae of normal pregnancies and compare them with placentae of pregnancies complicated with intrauterine growth restriction (IUGR). A total of 38 placentae (17 placentae of IUGR fetuses from singleton pregnancies and gestational age-matched 21 control placentae from normal singleton pregnancies) were collected from the Clinical Hospital Sveti Duh, Department of Gynecology and Obstetrics, Zagreb, Croatia. Gestational age was determined according to the last menstrual period (LMP) and by ultrasound measurements. Expression of glycoproteins was measured by Western blotting with SNA, UEA-I, PHA-E and DBA lectins as probes whereas expression of AXIN1 was determined by immunohistochemistry. Comparison of detected sugars revealed differences in protein glycosylation between normal and IUGR placentae. Higher expression of AXIN1 protein located mostly in the cytoplasm of syncytiotrophoblast and to a lesser extent in its nuclei was found in IUGR placentae. Results of our study suggest that changes in glycoprotein content may contribute to restricted placenta growth and development. Higher expression of AXIN1 protein in IUGR placentae indicates a role of Wnt/β-catenin signaling pathway in pathology of placental development.
ISSN:1476-4954
DOI:10.3109/14767058.2014.926326