{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,7]],"date-time":"2026-07-07T16:17:44Z","timestamp":1783441064369,"version":"3.54.6"},"reference-count":247,"publisher":"MDPI AG","issue":"3","license":[{"start":{"date-parts":[[2024,1,26]],"date-time":"2024-01-26T00:00:00Z","timestamp":1706227200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Department of Obstetrics and Gynecology at the University of Illinois at Chicago","award":["T32 GM079086-15"],"award-info":[{"award-number":["T32 GM079086-15"]}]},{"DOI":"10.13039\/100000002","name":"NIH Medical Scientist Training Program (MSTP)","doi-asserted-by":"publisher","award":["T32 GM079086-15"],"award-info":[{"award-number":["T32 GM079086-15"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"name":"UIC College of Medicine","award":["T32 GM079086-15"],"award-info":[{"award-number":["T32 GM079086-15"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>Protein misfolding disorders are a group of diseases characterized by supra-physiologic accumulation and aggregation of pathogenic proteoforms resulting from improper protein folding and\/or insufficiency in clearance mechanisms. Although these processes have been historically linked to neurodegenerative disorders, such as Alzheimer\u2019s disease, evidence linking protein misfolding to other pathologies continues to emerge. Indeed, the deposition of toxic protein aggregates in the form of oligomers or large amyloid fibrils has been linked to type 2 diabetes, various types of cancer, and, in more recent years, to preeclampsia, a life-threatening pregnancy-specific disorder. While extensive physiological mechanisms are in place to maintain proteostasis, processes, such as aging, genetic factors, or environmental stress in the form of hypoxia, nutrient deprivation or xenobiotic exposures can induce failure in these systems. As such, pregnancy, a natural physical state that already places the maternal body under significant physiological stress, creates an environment with a lower threshold for aberrant aggregation. In this review, we set out to discuss current evidence of protein misfolding in pregnancy and potential mechanisms supporting a key role for this process in preeclampsia pathogenesis. Improving our understanding of this emerging pathophysiological process in preeclampsia can lead to vital discoveries that can be harnessed to create better diagnoses and treatment modalities for the disorder.<\/jats:p>","DOI":"10.3390\/molecules29030610","type":"journal-article","created":{"date-parts":[[2024,1,26]],"date-time":"2024-01-26T10:54:27Z","timestamp":1706266467000},"page":"610","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":17,"title":["Protein Misfolding in Pregnancy: Current Insights, Potential Mechanisms, and Implications for the Pathogenesis of Preeclampsia"],"prefix":"10.3390","volume":"29","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-7085-6355","authenticated-orcid":false,"given":"Bani","family":"Medegan Fagla","sequence":"first","affiliation":[{"name":"Department of Obstetrics and Gynecology, College of Medicine, University of Illinois at Chicago, Chicago, IL 60612, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1701-1326","authenticated-orcid":false,"given":"Irina Alexandra","family":"Buhimschi","sequence":"additional","affiliation":[{"name":"Department of Obstetrics and Gynecology, College of Medicine, University of Illinois at Chicago, Chicago, IL 60612, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2024,1,26]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1146\/annurev-biochem-060614-033955","article-title":"The Biology of Proteostasis in Aging and Disease","volume":"84","author":"Labbadia","year":"2015","journal-title":"Annu. 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