A point-of-care urine test to predict adverse maternal and neonatal outcomes in Asian women with suspected preeclampsia

Wong, Natalie K. L.; Wah, Isabella Y. M.; Wong, Sani T. K.; Nguyen-Hoang, Long; Lau, Caitlyn S. L.; Ip, Patricia N. P.; Leung, Hillary H. Y.; Sahota, Daljit S.; Poon, Liona C.

doi:10.1007/s00404-023-07257-5

Cited by 2 publications

(2 citation statements)

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“…The Congo red dot (CRD) test represents a non-invasive and low-cost alternative to other methods of assessing protein misfolding load associated with PE. The clinical applicability of the CRD test, which is based on the detection of urine congophilia, as established by our lab, has been examined in fourteen studies, including one randomized control trial and one meta-analysis ( [90,91,[204][205][206][207][208][209][210][211][212][213][214][215]). In one study, our lab evaluated the performance of the CRD test at measuring misfolded protein load in urine and serum against that of Thioflavin-T (ThT)-enhanced fluorescence, a benzothiazole dye that preferentially binds to amyloid fibrils [214].…”

Section: Early Prediction and Diagnosismentioning

confidence: 99%

“…The predictive value of the test was improved when %CRR was used in combination with other markers of high disease risk, such as previous PE diagnosis, black race, body mass index, and mean arterial pressure [208]. In addition, the CRD test was not efficient at predicting PE in a term asymptomatic cohort (UK) and was determined to have low sensitivity at predicting impending MIDPE (within 28 days of initial assessment) in a randomized control trial, as well as low sensitivity at predicting adverse maternal and neonatal outcomes in women presenting with symptoms of suspected PE [205,206,210]. Finally, in a meta-analysis that included five studies, Khaliq et al concluded that the test is ineffective based on forest plot analysis [204].…”

Section: Early Prediction and Diagnosismentioning

confidence: 99%

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Protein Misfolding in Pregnancy: Current Insights, Potential Mechanisms, and Implications for the Pathogenesis of Preeclampsia

Medegan Fagla,

Buhimschi

2024

Molecules

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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’s 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.

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