Differences in the proteome profile in placenta from normal term and preeclamptic preterm pregnancies

Rose P. Webster, Brad A. Pitzer, Victoria H.J. Roberts, Diane Brockman, Leslie Myatt

    Research output: Contribution to journalArticlepeer-review

    15 Scopus citations


    The aim of this study was to use proteomic approaches to examine differences in protein expression in placentae from normal term and preterm preeclamptic pregnancies and to validate the data thus obtained by other independent methods. Using 2-DE we found that 80% of the proteins were present in both normal and preeclamptic placentae. However, 26 proteins in the normal term placentae were not matched in the preterm preeclamptic group. Six proteins showed increased intensity and one protein was down-regulated in preeclampsia. Four of the seven proteins that were altered in preeclampsia were further analyzed by Western blot and immunohistochemistry. Identification by MS techniques revealed these proteins to be involved in regulatory pathways activated by stress. This is significant because preeclampsia is a multisystem disorder in human pregnancies that results in considerable oxidative and nitrative stress. Three proteins identified by M S to be Hsp27, catalase, and glucose-regulated protein were confirmed by Western blot analysis to be significantly up-regulated in preeclampsia. Endothelial monocyte-activating polypeptide was shown to be down-regulated in preeclampsia by 2-DE and MS.

    Original languageEnglish (US)
    Pages (from-to)446-456
    Number of pages11
    JournalProteomics - Clinical Applications
    Issue number5
    StatePublished - May 1 2007


    • Catalase
    • Endothelial monocyte-activating polypeptide II
    • Glucose-regulated protein 96
    • Heat shock protein 27
    • Preeclampsia

    ASJC Scopus subject areas

    • Clinical Biochemistry

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