Knowledge of phenotypic changes the cellular prion protein (PrP(C)) contributes to may provide novel avenues for understanding its function. Here we consider data from functional knockout/down studies and protein-protein interaction analyses from the perspective of PrP's relationship to its ancestral ZIP metal ion transporting proteins. When approached in this manner, a role of PrP(C) as a modulator of a complex morphogenetic program that underlies epithelial-to-mesenchymal transition (EMT) emerges. To execute EMT, cells have to master the challenge to shift from cell-cell to cell-substrate modes of adherence. During this process, cell-cell junctions stabilized by E-cadherins are replaced by focal adhesions that mediate cell-substrate contacts. A similar reprogramming occurs during distinct organogenesis events that have been shown to rely on ZIP transporters. A model is presented that sees ZIP transporters, and possibly also PrP(C), affect this balance of adherence modes at both the transcriptional and post-translational levels.
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http://dx.doi.org/10.3389/fcell.2014.00053 | DOI Listing |
Acta Neuropathol Commun
December 2024
Laboratory of Neurological Infections and Immunity, National Institute of Allergy and Infectious Diseases, Division of Intramural Research, Rocky Mountain Laboratories, National Institutes of Health, Hamilton, MT, USA.
Misfolding of normal prion protein (PrP) to pathological isoforms (prions) causes prion diseases (PrDs) with clinical manifestations including cognitive decline and mood-related behavioral changes. Cognition and mood are linked to the neurophysiology of the limbic system. Little is known about how the disease affects the synaptic activity in brain parts associated with this system.
View Article and Find Full Text PDFBMC Cancer
December 2024
Laboratory of Neurobiology and Stem Cells, Department of Cell and Developmental Biology, Institute of Biomedical Sciences, University of Sao Paulo, Sao Paulo, SP, Brazil.
Background: Glioblastoma (GBM) is an aggressive brain tumor driven by glioblastoma stem cells (GSCs), which represent an appealing target for therapeutic interventions. The cellular prion protein (PrP), a scaffold protein involved in diverse cellular processes, interacts with various membrane and extracellular matrix molecules, influencing tumor biology. Herein, we investigate the impact of PrP expression on GBM.
View Article and Find Full Text PDFZh Nevrol Psikhiatr Im S S Korsakova
December 2024
Siberian State Medical University, Tomsk, Russia.
Creutzfeldt-Jakob disease (CJD) is a classic representative of the group of prion diseases and is characterized by progressive degeneration of the structures of the nervous system with a variety of neurological symptoms, steady progression and inevitable death. The disease is based on a change in the tertiary structure of the protein, which leads to disruption of the normal functioning of cells. Despite the fact that the etiology and pathogenesis of CJD are now well studied, intravital diagnosis of this serious disease remains difficult due to the peculiarities of the pathological process (unusually long incubation period, variety of clinical symptoms), the lack of pathognomonic markers that make it possible to make a diagnosis with a high degree of confidence, and also insufficient awareness of medical workers.
View Article and Find Full Text PDFCells
November 2024
Centro de Biología Molecular Severo Ochoa (CBM), Consejo Superior de Investigaciones Científicas, Universidad Autónoma de Madrid (CSIC/UAM), C/Nicolás Cabrera 1, 28049 Madrid, Spain.
T-cell intracellular antigen 1 (TIA1) is an RNA-binding protein (RBP) that plays a multifunctional role in RNA metabolism. TIA1 has three RNA-Recognition Motifs (RRMs) and a prion-like carboxyl C-terminal domain (LCD) with intrinsically disordered regions (IDR) implicated in the dynamics (i.e.
View Article and Find Full Text PDFAnimals (Basel)
November 2024
Korea Zoonosis Research Institute, Jeonbuk National University, 820-120 Hana-ro, Iksan 54531, Republic of Korea.
Prion diseases are fatal neurodegenerative disorders caused by the misfolding of the normal cellular prion protein (PrP) into its infectious isoform (PrP). Although prion diseases in humans, sheep, goats, and cattle have been extensively studied, feline spongiform encephalopathy (FSE) remains poorly understood. Genetic factors, particularly polymorphisms in the prion protein gene () and protein gene (), have been linked to prion disease susceptibility in various species.
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