Research ArticlePreeclampsia

Protein misfolding, congophilia, oligomerization, and defective amyloid processing in preeclampsia

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Science Translational Medicine  16 Jul 2014:
Vol. 6, Issue 245, pp. 245ra92
DOI: 10.1126/scitranslmed.3008808

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  • Using polarity index method for computational identification of misfolded (amyloidogenic) proteins.

    We read with great interest the research article by Buhimschi and colleagues (1) regarding the discovery of the amyloid-like aggregates of misfolded proteins in the placentas and urine of women with preeclampsia. This work nicely summarizes the important insights related to the potential roles of aggregation of misfolded proteins in this unique human disease. It also shows the usefulness of the assessment of global prote...

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    Competing Interests: None declared.
  • Re:Unfolded Protein Response and placental pathology

    Placental stress has long been associated with pre-eclampsia, but whether the accumulation of misfolded proteins in the placenta is causative of the syndrome requires further investigation. We provided the first report of placental endoplasmic reticulum stress in complications of pregnancy, demonstrating activation of Unfolded Protein Response (UPR) pathways in cases of early-onset pre-eclampsia that were complicated by...

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    Competing Interests: None declared.
  • Preeclampsia: hypoxia and/or misfolding

    Prions and , for example neurodegeneratives diseases , arise from the same general disease mechanisme (1).In each, there is abnormal unfolding and then aggregation of proteins (2).The protein conformational changes associated with the pathogenesis of protein misfolding disorders produced Beta sheet rich oligomers that are partially resistant to proteolysis and have a high tendency to form amyloid-like aggregates (3)....

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    Competing Interests: None declared.