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Analysis of Punicalin and Punicalagin Interaction with PDIA3 and PDIA1.
Int J Mol Sci
September 2024
Department of Biochemical Science "A. Rossi Fanelli", Faculty of Farmacy and Medicine, Sapienza University of Rome, Pl. A. Moro 5, 00185 Rome, Italy.
Article Synopsis
- PDIA3 is an important protein in the endoplasmic reticulum that plays a key role in protein folding and is linked to diseases like cancer and neurodegeneration.
- Punicalagin is a promising but non-selective PDIA3 inhibitor, prompting the exploration of its derivative, punicalin, which has a simpler structure and better selectivity towards PDIA3.
- Studies show that punicalin effectively binds and inhibits PDIA3, demonstrating higher selectivity compared to PDIA1, and causes significant changes in PDIA3's thermal stability, highlighting its potential for developing selective PDIA3 inhibitors.
Protein Disulfide Isomerase Endoplasmic Reticulum Protein 57 (ERp57) is Protective Against ALS-Associated Mutant TDP-43 in Neuronal Cells.
Neuromolecular Med
June 2024
Motor Neuron Disease Research Centre, Macquarie Medical School, Faculty of Medicine, Health and Human Sciences, Macquarie University, Sydney, 2109, Australia.
Amyotrophic Lateral Sclerosis (ALS) is a severe neurodegenerative disease affecting motor neurons. Pathological forms of Tar-DNA binding protein-43 (TDP-43), involving its mislocalisation to the cytoplasm and the formation of misfolded inclusions, are present in almost all ALS cases (97%), and ~ 50% cases of the related condition, frontotemporal dementia (FTD), highlighting its importance in neurodegeneration. Previous studies have shown that endoplasmic reticulum protein 57 (ERp57), a member of the protein disulphide isomerase (PDI) family of redox chaperones, is protective against ALS-linked mutant superoxide dismutase (SOD1) in neuronal cells and transgenic SOD1 mouse models.
View Article and Find Full Text PDFERp57 chaperon protein protects neuronal cells from Aβ-induced toxicity.
J Neurochem
August 2022
Department of Biochemical Sciences, Sapienza University of Roma, Rome, Italy.
Alzheimer's disease (AD) is a neurodegenerative disorder whose main pathological hallmark is the accumulation of Amyloid-β peptide (Aβ) in the form of senile plaques. Aβ can cause neurodegeneration and disrupt cognitive functions by several mechanisms, including oxidative stress. ERp57 is a protein disulfide isomerase involved in the cellular stress response and known to be present in the cerebrospinal fluid of normal individuals as a complex with Aβ peptides, suggesting that it may be a carrier protein which prevents aggregation of Aβ.
View Article and Find Full Text PDFReversal of Alpha-Synuclein Fibrillization by Protein Disulfide Isomerase.
Front Cell Dev Biol
July 2020
Burnett School of Biomedical Sciences, College of Medicine, University of Central Florida, Orlando, FL, United States.
Aggregates of α-synuclein contribute to the etiology of Parkinson's Disease. Protein disulfide isomerase (PDI), a chaperone and oxidoreductase, blocks the aggregation of α-synuclein. An S-nitrosylated form of PDI that cannot function as a chaperone is associated with elevated levels of aggregated α-synuclein and is found in brains afflicted with Parkinson's Disease.
View Article and Find Full Text PDFOverexpression of quality control proteins reduces prion conversion in prion-infected cells.
J Biol Chem
October 2018
From the Calgary Prion Research Unit, University of Calgary, Calgary, Alberta T2N 4Z6, Canada,
Prion diseases are fatal infectious neurodegenerative disorders in humans and other animals and are caused by misfolding of the cellular prion protein (PrP) into the pathological isoform PrP These diseases have the potential to transmit within or between species, including zoonotic transmission to humans. Elucidating the molecular and cellular mechanisms underlying prion propagation and transmission is therefore critical for developing molecular strategies for disease intervention. We have shown previously that impaired quality control mechanisms directly influence prion propagation.
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