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

Author:

Buhimschi Irina A.12,Nayeri Unzila A.2,Zhao Guomao1,Shook Lydia L.2,Pensalfini Anna3,Funai Edmund F.4,Bernstein Ira M.5,Glabe Charles G.67,Buhimschi Catalin S.24

Affiliation:

1. Center for Perinatal Research, The Research Institute at Nationwide Children’s Hospital and Department of Pediatrics, The Ohio State University College of Medicine, Columbus, OH 43215, USA.

2. Department of Obstetrics, Gynecology and Reproductive Sciences, Yale University School of Medicine, New Haven, CT 06520, USA.

3. Center for Dementia Research, Nathan Kline Institute for Psychiatric Research and Department of Psychiatry, New York University School of Medicine, New York, NY 10016, USA.

4. Department of Obstetrics and Gynecology, The Ohio State University College of Medicine, Columbus, OH 43210, USA.

5. Department of Obstetrics, Gynecology and Reproductive Sciences, University of Vermont College of Medicine, Burlington, VT 05405, USA.

6. Department of Molecular Biology and Biochemistry, University of California, Irvine, Irvine, CA 92617, USA.

7. Department of Biochemistry and Experimental Biochemistry Unit, King Abdulaziz University, Jeddah 22254, Saudi Arabia.

Abstract

Preeclampsia is characterized by protein misfolding, aggregation, and amyloid-like plaque formation, suggesting that this pregnancy-related condition shares pathophysiologic features with protein conformational disorders.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

General Medicine

Reference70 articles.

1. WHO analysis of causes of maternal death: a systematic review

2. ACOG Practice Bulletin 33. Diagnosis and Management of Preeclampsia and Eclampsia (American College of Obstetricians and Gynecologists Washington DC 2002).

3. Diagnosis and management of atypical preeclampsia-eclampsia

4. Pre-eclampsia

5. Preeclampsia, Hypoxia, Thrombosis, and Inflammation

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