Research ArticlePreeclampsia

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

See allHide authors and affiliations

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

eLetters is an online forum for ongoing peer review. Submission of eLetters are open to all. Please read our Terms of Service before submitting your own eLetter.

Compose eLetter

Plain text

  • Plain text
    No HTML tags allowed.
  • Web page addresses and e-mail addresses turn into links automatically.
  • Lines and paragraphs break automatically.
Author Information
First or given name, e.g. 'Peter'.
Your last, or family, name, e.g. 'MacMoody'.
Your email address, e.g. higgs-boson@gmail.com
Your role and/or occupation, e.g. 'Orthopedic Surgeon'.
Your organization or institution (if applicable), e.g. 'Royal Free Hospital'.
Statement of Competing Interests
CAPTCHA

This question is for testing whether or not you are a human visitor and to prevent automated spam submissions.

Image CAPTCHA
Enter the characters shown in the image.

Vertical Tabs

  • 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...

    Show More
    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...

    Show More
    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)....

    Show More
    Competing Interests: None declared.