1.Pesticide poisoning – an epidemiological and histopathological study.
Nigam MK ; Jain BB ; Banerjee U ; Roy DG ; Chatterjee S.
Pacific Journal of Medical Sciences 2013;12(1):3-9
The objectives of this hospital based cross-sectional study were to evaluate the socio-demographic profile, manner of death and histopathological changes in the lungs, liver and kidneys of individuals who died of pesticide poisoning. All fatal cases of pesticide poisoning from February 2011 to January 2012 were evaluated. Socio-demographic profile, type of exposure and manner of death were recorded for each of the cases. Autopsy was performed with detailed internal and external examinations. Random portion of Lung, Liver and Kidney were collected and fixed in 10.0% Formalin. Hematoxylin and Eosin stained sections were examined and findings recorded.
The total number of deaths due to fatal pesticide poisoning was 9.6%. Highest frequency of poisoning (23.4%) was seen in the age group 20 - 29 years. The peak time of consumption of poisoning was between 6.00am and 12.00noon. The manner of poisoning was suicidal in majority of the cases. Histological findings indicated that congestion was the most common histopathological change; being observed in 60.0%, 66.0% and 74.0% of cases of liver, lung and kidney respectively. Histopathological features are supportive in establishing the diagnosis but further studies with larger sample size may be more illuminative in explaining the histopathological changes occurring due to these chemicals.
2.A small molecule UPR modulator for diabetes identified by high throughput screening.
Valeria MARROCCO ; Tuan TRAN ; Siying ZHU ; Seung Hyuk CHOI ; Ana M GAMO ; Sijia LI ; Qiangwei FU ; Marta Diez CUNADO ; Jason ROLAND ; Mitch HULL ; Van NGUYEN-TRAN ; Sean JOSEPH ; Arnab K CHATTERJEE ; Nikki ROGERS ; Matthew S TREMBLAY ; Weijun SHEN
Acta Pharmaceutica Sinica B 2021;11(12):3983-3993
Unfolded protein response (UPR) is a stress response that is specific to the endoplasmic reticulum (ER). UPR is activated upon accumulation of unfolded (or misfolded) proteins in the ER's lumen to restore protein folding capacity by increasing the synthesis of chaperones. In addition, UPR also enhances degradation of unfolded proteins and reduces global protein synthesis to alleviate additional accumulation of unfolded proteins in the ER. Herein, we describe a cell-based ultra-high throughput screening (uHTS) campaign that identifies a small molecule that can modulate UPR and ER stress in cellular and