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Journal articles on the topic 'Cellular prion protein physiological function, Myelin'

Author: Grafiati

Published: 14 March 2023

Last updated: 31 July 2025

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1

Nuvolone, Mario, Mario Hermann, Silvia Sorce, et al. "Strictly co-isogenic C57BL/6J-Prnp−/− mice: A rigorous resource for prion science." Journal of Experimental Medicine 213, no. 3 (2016): 313–27. http://dx.doi.org/10.1084/jem.20151610.

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Although its involvement in prion replication and neurotoxicity during transmissible spongiform encephalopathies is undisputed, the physiological role of the cellular prion protein (PrPC) remains enigmatic. A plethora of functions have been ascribed to PrPC based on phenotypes of Prnp−/− mice. However, all currently available Prnp−/− lines were generated in embryonic stem cells from the 129 strain of the laboratory mouse and mostly crossed to non-129 strains. Therefore, Prnp-linked loci polymorphic between 129 and the backcrossing strain resulted in systematic genetic confounders and led to er

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Martins, V. R., A. F. Mercadante, A. L. B. Cabral, A. R. O. Freitas, and R. M. R. P. S. Castro. "Insights into the physiological function of cellular prion protein." Brazilian Journal of Medical and Biological Research 34, no. 5 (2001): 585–95. http://dx.doi.org/10.1590/s0100-879x2001000500005.

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3

Franzmann, Titus M., Marcus Jahnel, Andrei Pozniakovsky, et al. "Phase separation of a yeast prion protein promotes cellular fitness." Science 359, no. 6371 (2018): eaao5654. http://dx.doi.org/10.1126/science.aao5654.

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Despite the important role of prion domains in neurodegenerative disease, their physiological function has remained enigmatic. Previous work with yeast prions has defined prion domains as sequences that form self-propagating aggregates. Here, we uncovered an unexpected function of the canonical yeast prion protein Sup35. In stressed conditions, Sup35 formed protective gels via pH-regulated liquid-like phase separation followed by gelation. Phase separation was mediated by the N-terminal prion domain and regulated by the adjacent pH sensor domain. Phase separation promoted yeast cell survival b

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4

Go, Gyeongyun, and Sang Hun Lee. "The Cellular Prion Protein: A Promising Therapeutic Target for Cancer." International Journal of Molecular Sciences 21, no. 23 (2020): 9208. http://dx.doi.org/10.3390/ijms21239208.

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Studies on the cellular prion protein (PrPC) have been actively conducted because misfolded PrPC is known to cause transmissible spongiform encephalopathies or prion disease. PrPC is a glycophosphatidylinositol-anchored cell surface glycoprotein that has been reported to affect several cellular functions such as stress protection, cellular differentiation, mitochondrial homeostasis, circadian rhythm, myelin homeostasis, and immune modulation. Recently, it has also been reported that PrPC mediates tumor progression by enhancing the proliferation, metastasis, and drug resistance of cancer cells.

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Miranzadeh Mahabadi, Hajar, and Changiz Taghibiglou. "Cellular Prion Protein (PrPc): Putative Interacting Partners and Consequences of the Interaction." International Journal of Molecular Sciences 21, no. 19 (2020): 7058. http://dx.doi.org/10.3390/ijms21197058.

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Cellular prion protein (PrPc) is a small glycosylphosphatidylinositol (GPI) anchored protein most abundantly found in the outer leaflet of the plasma membrane (PM) in the central nervous system (CNS). PrPc misfolding causes neurodegenerative prion diseases in the CNS. PrPc interacts with a wide range of protein partners because of the intrinsically disordered nature of the protein’s N-terminus. Numerous studies have attempted to decipher the physiological role of the prion protein by searching for proteins which interact with PrPc. Biochemical characteristics and biological functions both appe

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6

Aguzzi, Adriano, and Anna Maria Calella. "Prions: Protein Aggregation and Infectious Diseases." Physiological Reviews 89, no. 4 (2009): 1105–52. http://dx.doi.org/10.1152/physrev.00006.2009.

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Transmissible spongiform encephalopathies (TSEs) are inevitably lethal neurodegenerative diseases that affect humans and a large variety of animals. The infectious agent responsible for TSEs is the prion, an abnormally folded and aggregated protein that propagates itself by imposing its conformation onto the cellular prion protein (PrPC) of the host. PrPCis necessary for prion replication and for prion-induced neurodegeneration, yet the proximal causes of neuronal injury and death are still poorly understood. Prion toxicity may arise from the interference with the normal function of PrPC, and

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7

Westergard, Laura, Heather M. Christensen, and David A. Harris. "The cellular prion protein (PrPC): Its physiological function and role in disease." Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1772, no. 6 (2007): 629–44. http://dx.doi.org/10.1016/j.bbadis.2007.02.011.

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8

Henzi, Anna, and Adriano Aguzzi. "The prion protein is not required for peripheral nerve de- and remyelination after crush injury." PLOS ONE 16, no. 1 (2021): e0245944. http://dx.doi.org/10.1371/journal.pone.0245944.

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The cellular prion protein (PrP) is essential to the long-term maintenance of myelin sheaths in peripheral nerves. PrP activates the adhesion G-protein coupled receptor Adgrg6 on Schwann cells and initiates a pro-myelination cascade of molecular signals. Because Adgrg6 is crucial for peripheral myelin development and regeneration after nerve injury, we investigated the role of PrP in peripheral nerve repair. We performed experimental sciatic nerve crush injuries in co-isogenic wild-type and PrP-deficient mice, and examined peripheral nerve repair processes. Generation of repair Schwann cells,

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9

Kovač, Valerija, and Vladka Čurin Šerbec. "Prion Protein: The Molecule of Many Forms and Faces." International Journal of Molecular Sciences 23, no. 3 (2022): 1232. http://dx.doi.org/10.3390/ijms23031232.

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Cellular prion protein (PrPC) is a glycosylphosphatidylinositol (GPI)-anchored protein most abundantly found in the outer membrane of neurons. Due to structural characteristics (a flexible tail and structured core), PrPC interacts with a wide range of partners. Although PrPC has been proposed to be involved in many physiological functions, only peripheral nerve myelination homeostasis has been confirmed as a bona fide function thus far. PrPC misfolding causes prion diseases and PrPC has been shown to mediate β-rich oligomer-induced neurotoxicity in Alzheimer’s and Parkinson’s disease as well a

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Rolle, Irene Giulia, Anna Burato, Merve Begüm Bacınoğlu, Fabio Moda, and Giuseppe Legname. "The Role of Prion Protein in Reelin/Dab1 Signaling: Implications for Neurodegeneration." Viruses 17, no. 7 (2025): 928. https://doi.org/10.3390/v17070928.

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The cellular prion protein (PrPC) is studied in prion diseases, where its misfolded isoform (PrPSc) leads to neurodegeneration. PrPC has also been implicated in several physiological functions. The protein is abundant in the nervous system, and it is critical for cell signaling in cellular communication, where it acts as a scaffold for various signaling molecules. The Reelin signaling pathway, implicated both in Alzheimer’s and prion diseases, engages Dab1, an adaptor protein influencing APP processing and amyloid beta deposition. Here, we show, using Prnp knockout models (Prnp0/0), that PrPC

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Yoon, Sungtae, Gyeongyun Go, Yeomin Yoon, Jiho Lim, Gaeun Lee, and Sanghun Lee. "Harnessing the Physiological Functions of Cellular Prion Protein in the Kidneys: Applications for Treating Renal Diseases." Biomolecules 11, no. 6 (2021): 784. http://dx.doi.org/10.3390/biom11060784.

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A cellular prion protein (PrPC) is a ubiquitous cell surface glycoprotein, and its physiological functions have been receiving increased attention. Endogenous PrPC is present in various kidney tissues and undergoes glomerular filtration. In prion diseases, abnormal prion proteins are found to accumulate in renal tissues and filtered into urine. Urinary prion protein could serve as a diagnostic biomarker. PrPC plays a role in cellular signaling pathways, reno-protective effects, and kidney iron uptake. PrPC signaling affects mitochondrial function via the ERK pathway and is affected by the regu

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Lorca, Ramón A., Lorena Varela-Nallar, Nibaldo C. Inestrosa, and J. Pablo Huidobro-Toro. "The Cellular Prion Protein Prevents Copper-Induced Inhibition of P2X4Receptors." International Journal of Alzheimer's Disease 2011 (2011): 1–6. http://dx.doi.org/10.4061/2011/706576.

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Although the physiological function of the cellular prion protein (PrPC) remains unknown, several evidences support the notion of its role in copper homeostasis. PrPCbinds Cu2+through a domain composed by four to five repeats of eight amino acids. Previously, we have shown that the perfusion of this domain prevents and reverses the inhibition by Cu2+of the adenosine triphosphate (ATP)-evoked currents in the P2X4receptor subtype, highlighting a modulatory role for PrPCin synaptic transmission through regulation of Cu2+levels. Here, we study the effect of full-length PrPCin Cu2+inhibition of P2X

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Caldarulo, Enrico, Alessandro Barducci, Kurt Wüthrich та Michele Parrinello. "Prion protein β2–α2 loop conformational landscape". Proceedings of the National Academy of Sciences 114, № 36 (2017): 9617–22. http://dx.doi.org/10.1073/pnas.1712155114.

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In transmissible spongiform encephalopathies (TSEs), which are lethal neurodegenerative diseases that affect humans and a wide range of other mammalian species, the normal “cellular” prion protein (PrPC) is transformed into amyloid aggregates representing the “scrapie form” of the protein (PrPSc). Continued research on this system is of keen interest, since new information on the physiological function of PrPC in healthy organisms is emerging, as well as new data on the mechanism of the transformation of PrPC to PrPSc. In this paper we used two different approaches: a combination of the well-t

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14

Khosravani, Houman, Yunfeng Zhang, Shigeki Tsutsui, et al. "Prion protein attenuates excitotoxicity by inhibiting NMDA receptors." Journal of Cell Biology 181, no. 3 (2008): 551–65. http://dx.doi.org/10.1083/jcb.200711002.

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It is well established that misfolded forms of cellular prion protein (PrP [PrPC]) are crucial in the genesis and progression of transmissible spongiform encephalitis, whereas the function of native PrPC remains incompletely understood. To determine the physiological role of PrPC, we examine the neurophysiological properties of hippocampal neurons isolated from PrP-null mice. We show that PrP-null mouse neurons exhibit enhanced and drastically prolonged N-methyl-d-aspartate (NMDA)–evoked currents as a result of a functional upregulation of NMDA receptors (NMDARs) containing NR2D subunits. Thes

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15

Dondapati, Divya Teja, Pradeep Reddy Cingaram, Ferhan Ayaydin, et al. "Membrane Domain Localization and Interaction of the Prion-Family Proteins, Prion and Shadoo with Calnexin." Membranes 11, no. 12 (2021): 978. http://dx.doi.org/10.3390/membranes11120978.

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The cellular prion protein (PrPC) is renowned for its infectious conformational isoform PrPSc, capable of templating subsequent conversions of healthy PrPCs and thus triggering the group of incurable diseases known as transmissible spongiform encephalopathies. Besides this mechanism not being fully uncovered, the protein’s physiological role is also elusive. PrPC and its newest, less understood paralog Shadoo are glycosylphosphatidylinositol-anchored proteins highly expressed in the central nervous system. While they share some attributes and neuroprotective actions, opposing roles have also b

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Prado, Mariana Brandão, Maria Isabel Melo Escobar, Rodrigo Nunes Alves, et al. "Prion Protein at the Leading Edge: Its Role in Cell Motility." International Journal of Molecular Sciences 21, no. 18 (2020): 6677. http://dx.doi.org/10.3390/ijms21186677.

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Cell motility is a central process involved in fundamental biological phenomena during embryonic development, wound healing, immune surveillance, and cancer spreading. Cell movement is complex and dynamic and requires the coordinated activity of cytoskeletal, membrane, adhesion and extracellular proteins. Cellular prion protein (PrPC) has been implicated in distinct aspects of cell motility, including axonal growth, transendothelial migration, epithelial–mesenchymal transition, formation of lamellipodia, and tumor migration and invasion. The preferential location of PrPC on cell membrane favor

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17

Varela-Nallar, Lorena, Enrique M. Toledo, Luis F. Larrondo, Ana L. B. Cabral, Vilma R. Martins, and Nibaldo C. Inestrosa. "Induction of cellular prion protein gene expression by copper in neurons." American Journal of Physiology-Cell Physiology 290, no. 1 (2006): C271—C281. http://dx.doi.org/10.1152/ajpcell.00160.2005.

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Prion diseases are caused by the conformational transition of the native α-helical cellular prion protein (PrPC) into a β-sheet pathogenic isoform. However, the normal physiological function of PrPC remains elusive. We report herein that copper induces PrPC expression in primary hippocampal and cortical neurons. PrPC induced by copper has a normal glycosylation pattern, is proteinase K-sensitive and reaches the cell surface attached by a glycosyl phosphatidylinositol anchor. Immunofluorescence analysis revealed that copper induces PrPC levels in the cell surface and in an intracellular compart

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18

Khosravani, Houman, Yunfeng Zhang, Shigeki Tsutsui, et al. "Modulation of NMDA receptors by prion proteins." Clinical & Investigative Medicine 30, no. 4 (2007): 85. http://dx.doi.org/10.25011/cim.v30i4.2859.

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Background: The precise physiological function of endogenous cellular prion protein (PrPC) remains unclear. It has been shown that PrP-null mice exhibit reduced LTP and greater susceptability to seizure mortality in several in vivo (e.g. kainic acid) models of epilepsy. In addition, PrP-null mice exhibit greater exctitotoxic cell death in response to kainic acid exposure. Methods: In our study we investigated the synaptic properties of WT and PrP-null mice.  Results: Recordings in the CA1 layer of adult hippocampal slices showed that PrP-null mice exhibit a reduced threshold to evoked re

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Smirnova, Evgeniya V., Vladimir I. Timofeev, Tatiana V. Rakitina, et al. "Myelin Basic Protein Attenuates Furin-Mediated Bri2 Cleavage and Postpones Its Membrane Trafficking." International Journal of Molecular Sciences 25, no. 5 (2024): 2608. http://dx.doi.org/10.3390/ijms25052608.

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Myelin basic protein (MBP) is the second most abundant protein in the central nervous system and is responsible for structural maintenance of the myelin sheath covering axons. Previously, we showed that MBP has a more proactive role in the oligodendrocyte homeostasis, interacting with membrane-associated proteins, including integral membrane protein 2B (ITM2B or Bri2) that is associated with familial dementias. Here, we report that the molecular dynamics of the in silico-generated MBP-Bri2 complex revealed that MBP covers a significant portion of the Bri2 ectodomain, assumingly trapping the fu

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Khosravani, H., Y. Zhang, S. Tsutsui, et al. "LACK OF CELLULAR PRION PROTEIN UNMASKS NMDA NR2D SUBUNIT RECEPTOR FUNCTION WITH CONSEQUENCES TOWARD SYNAPTIC TRANSMISSION AND EXCITOTOXICITY." Clinical & Investigative Medicine 31, no. 4 (2008): 14. http://dx.doi.org/10.25011/cim.v31i4.4811.

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Background: The physiological functions of endogenous cellular prion protein (PrPC)is incompletely understood. Previously, it has been shown that PrP-null mice exhibit reduced long-term (synaptic) potentiation and greater susceptibility to seizure mortality in several in vivo models of epilepsy. In addition, PrP-null neurons in culture exhibit greater excito toxic cell death in response to kainic acid exposure, and in several models of oxidative stress. Although PrP seems toplay a protective role against various forms of cellular insults, the precise mechanism of such action is unknown. Method

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D’Alessio, Stefania, Stefanía Thorgeirsdóttir, Igor Kraev, Karl Skírnisson, and Sigrun Lange. "Post-Translational Protein Deimination Signatures in Plasma and Plasma EVs of Reindeer (Rangifer tarandus)." Biology 10, no. 3 (2021): 222. http://dx.doi.org/10.3390/biology10030222.

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The reindeer (caribou) Rangifer tarandus is a Cervidae in the order Artiodactyla. Reindeer are sedentary and migratory populations with circumpolar distribution in the Arctic, Northern Europe, Siberia and North America. Reindeer are an important wild and domesticated species, and have developed various adaptive strategies to extreme environments. Importantly, deer have also been identified to be putative zoonotic carriers, including for parasites, prions and coronavirus. Therefore, novel insights into immune-related markers are of considerable interest. Peptidylarginine deiminases (PADs) are a

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Weise, Jens, Thorsten R. Doeppner, Tilo Müller, et al. "Overexpression of cellular prion protein alters postischemic Erk1/2 phosphorylation but not Akt phosphorylation and protects against focal cerebral ischemia." Restorative Neurology and Neuroscience 26, no. 1 (2008): 57–64. https://doi.org/10.3233/rnn-2008-00421.

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Purpose: The physiological function of the cellular prion protein (PrP $^{C}$ ) is still unclear. A growing body of evidence suggests that PrP $^{C}$ has neuroprotective properties and that its deletion increases susceptibility to focal cerebral ischemia. The purpose of this study was to elucidate the role of PrP $^{C}$ overexpression in ischemic brain injury in vivo. Methods: PrP $^{C}$ overexpressing (TG35) and wild type (WT) mice were subjected to a 90-minute transient focal cerebral ischemia followed by infarct volume analysis 24 hours after lesion. To identify effects of PrP $^{C}$ overex

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Gonzalez-Gronow, Mario, and Salvatore Vincent Pizzo. "Physiological Roles of the Autoantibodies to the 78-Kilodalton Glucose-Regulated Protein (GRP78) in Cancer and Autoimmune Diseases." Biomedicines 10, no. 6 (2022): 1222. http://dx.doi.org/10.3390/biomedicines10061222.

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The 78 kDa glucose-regulated protein (GRP78), a member of the 70 kDa heat-shock family of molecular chaperones (HSP70), is essential for the regulation of the unfolded protein response (UPR) resulting from cellular endoplasmic reticulum (ER) stress. During ER stress, GRP78 evades retention mechanisms and is translocated to the cell surface (csGRP78) where it functions as an autoantigen. Autoantibodies to GRP78 appear in prostate, ovarian, gastric, malignant melanoma, and colorectal cancers. They are also found in autoimmune pathologies such as rheumatoid arthritis (RA), neuromyelitis optica (N

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Holada, Karel, Jan Simak, and Jaroslav G. Vostal. "The Post-Transfusion Recovery and Survival of Red Blood Cells in Mice Is Affected by the Expression of Cellular Prion Protein." Blood 108, no. 11 (2006): 959. http://dx.doi.org/10.1182/blood.v108.11.959.959.

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Abstract Three documented transfusion cases of vCJD underline the need of better insight in blood prion protein biology. Cellular prion protein (PrPc) plays key role in the pathophysiology of prion diseases. Its expression by cells is necessary for amplification of infectious prions and the disease process itself. Physiological function of PrPc remains obscure. Its clarification may provide important clues for the development of urgently needed blood test and effective disease treatment. PrPc is expressed on CD34+ hematopoietic stem cells and its expression is regulated during blood cell diffe

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Noori, Leila, Kamila Filip, Zohreh Nazmara, et al. "Contribution of Extracellular Vesicles and Molecular Chaperones in Age-Related Neurodegenerative Disorders of the CNS." International Journal of Molecular Sciences 24, no. 2 (2023): 927. http://dx.doi.org/10.3390/ijms24020927.

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Many neurodegenerative disorders are characterized by the abnormal aggregation of misfolded proteins that form amyloid deposits which possess prion-like behavior such as self-replication, intercellular transmission, and consequent induction of native forms of the same protein in surrounding cells. The distribution of the accumulated proteins and their correlated toxicity seem to be involved in the progression of nervous system degeneration. Molecular chaperones are known to maintain proteostasis, contribute to protein refolding to protect their function, and eliminate fatally misfolded protein

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Carlston, Colleen, Robin Weinmann, Natalia Stec, et al. "PQN-59 antagonizes microRNA-mediated repression during post-embryonic temporal patterning and modulates translation and stress granule formation in C. elegans." PLOS Genetics 17, no. 11 (2021): e1009599. http://dx.doi.org/10.1371/journal.pgen.1009599.

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microRNAs (miRNAs) are potent regulators of gene expression that function in a variety of developmental and physiological processes by dampening the expression of their target genes at a post-transcriptional level. In many gene regulatory networks (GRNs), miRNAs function in a switch-like manner whereby their expression and activity elicit a transition from one stable pattern of gene expression to a distinct, equally stable pattern required to define a nascent cell fate. While the importance of miRNAs that function in this capacity are clear, we have less of an understanding of the cellular fac

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Soukup, Alexandra, Kirby D. Johnson, Daniel J. Conn, et al. "GATA2-Dependent Developmental and Regenerative Networks." Blood 134, Supplement_1 (2019): 1182. http://dx.doi.org/10.1182/blood-2019-126875.

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Coding and regulatory human GATA2 mutations that deregulate protein expression and/or function cause immunodeficiency that often progresses to MDS/AML (McReynolds et al., 2018). In the mouse, decreased GATA2 expression impairs hematopoietic stem/progenitor cell (HSPC) genesis and function (de Pater et al., 2013; Gao et al., 2013; Tsai et al., 1994). While prior studies demonstrated Gata2 +9.5 and -77 enhancers are essential for HSC emergence (+9.5) and/or progenitor cell fate (+9.5 and -77) (Johnson et al., 2012; Johnson et al., 2015; Mehta et al., 2017) and hematopoietic regeneration (+9.5) (

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Jaffré, Nina, Jérôme Delmotte, Jacqueline Mikol, Jean-Philippe Deslys, and Emmanuel Comoy. "Unexpected decrease of full-length prion protein in macaques inoculated with prion-contaminated blood products." Frontiers in Molecular Biosciences 10 (May 5, 2023). http://dx.doi.org/10.3389/fmolb.2023.1164779.

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The presence of prion infectivity in the blood of patients affected by variant Creutzfeldt–Jakob disease (v-CJD), the human prion disease linked to the bovine spongiform encephalopathy (BSE), poses the risk of inter-human transmission of this fatal prion disease through transfusion. In the frame of various experiments, we have previously described that several cynomolgus macaques experimentally exposed to prion-contaminated blood products developed c-BSE/v-CJD, but the vast majority of them developed an unexpected, fatal disease phenotype focused on spinal cord involvement, which does not fulf

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Tsutsui, Shigeki, Megan Morgan, Hugo Tedford, Haitao You, Gerald W. Zamponi та Peter K. Stys. "Copper ions, prion protein and Aβ modulate Ca levels in central nervous system myelin in an NMDA receptor-dependent manner". Molecular Brain 15, № 1 (2022). http://dx.doi.org/10.1186/s13041-022-00955-2.

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AbstractAs in neurons, CNS myelin expresses N-Methyl-D-Aspartate Receptors (NMDARs) that subserve physiological roles, but have the potential to induce injury to this vital element. Using 2-photon imaging of myelinic Ca in live ex vivo mouse optic nerves, we show that Cu ions potently modulate Ca levels in an NMDAR-dependent manner. Chelating Cu in the perfusate induced a substantial increase in Ca levels, and also caused significant axo-myelinic injury. Myelinic NMDARs are shown to be regulated by cellular prion protein; only in prion protein KO optic nerves does application of NMDA + D-serin

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Didonna, Alessandro. "Prion protein and its role in signal transduction." Cellular and Molecular Biology Letters 18, no. 2 (2013). http://dx.doi.org/10.2478/s11658-013-0085-0.

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AbstractPrion diseases are a class of fatal neurodegenerative disorders that can be sporadic, genetic or iatrogenic. They are characterized by the unique nature of their etiologic agent: prions (PrPSc). A prion is an infectious protein with the ability to convert the host-encoded cellular prion protein (PrPC) into new prion molecules by acting as a template. Since Stanley B. Prusiner proposed the “protein-only” hypothesis for the first time, considerable effort has been put into defining the role played by PrPC in neurons. However, its physiological function remains unclear. This review summar

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Schneider, Benoit, Anne Baudry, Mathéa Pietri, et al. "The Cellular Prion Protein—ROCK Connection: Contribution to Neuronal Homeostasis and Neurodegenerative Diseases." Frontiers in Cellular Neuroscience 15 (April 12, 2021). http://dx.doi.org/10.3389/fncel.2021.660683.

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Amyloid-based neurodegenerative diseases such as prion, Alzheimer's, and Parkinson's diseases have distinct etiologies and clinical manifestations, but they share common pathological events. These diseases are caused by abnormally folded proteins (pathogenic prions PrPSc in prion diseases, β-amyloids/Aβ and Tau in Alzheimer's disease, α-synuclein in Parkinson's disease) that display β-sheet-enriched structures, propagate and accumulate in the nervous central system, and trigger neuronal death. In prion diseases, PrPSc-induced corruption of the physiological functions exerted by normal cellular

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Wu, Shuangchan, and Wensheng Lin. "The physiological role of the unfolded protein response in the nervous system." Neural Regeneration Research, January 8, 2024. http://dx.doi.org/10.4103/1673-5374.393105.

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Abstract The unfolded protein response (UPR) is a cellular stress response pathway activated when the endoplasmic reticulum, a crucial organelle for protein folding and modification, encounters an accumulation of unfolded or misfolded proteins. The UPR aims to restore endoplasmic reticulum homeostasis by enhancing protein folding capacity, reducing protein biosynthesis, and promoting protein degradation. It also plays a pivotal role in coordinating signaling cascades to determine cell fate and function in response to endoplasmic reticulum stress. Recent research has highlighted the significanc

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Bizingre, Chloé, Clara Bianchi, Anne Baudry, Aurélie Alleaume-Butaux, Benoit Schneider, and Mathéa Pietri. "Post-translational modifications in prion diseases." Frontiers in Molecular Neuroscience 17 (July 1, 2024). http://dx.doi.org/10.3389/fnmol.2024.1405415.

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More than 650 reversible and irreversible post-translational modifications (PTMs) of proteins have been listed so far. Canonical PTMs of proteins consist of the covalent addition of functional or chemical groups on target backbone amino-acids or the cleavage of the protein itself, giving rise to modified proteins with specific properties in terms of stability, solubility, cell distribution, activity, or interactions with other biomolecules. PTMs of protein contribute to cell homeostatic processes, enabling basal cell functions, allowing the cell to respond and adapt to variations of its enviro

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Gielnik, Maciej, Michał Taube, Lilia Zhukova, et al. "Zn(II) binding causes interdomain changes in the structure and flexibility of the human prion protein." Scientific Reports 11, no. 1 (2021). http://dx.doi.org/10.1038/s41598-021-00495-0.

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AbstractThe cellular prion protein (PrPC) is a mainly α-helical 208-residue protein located in the pre- and postsynaptic membranes. For unknown reasons, PrPC can undergo a structural transition into a toxic, β-sheet rich scrapie isoform (PrPSc) that is responsible for transmissible spongiform encephalopathies (TSEs). Metal ions seem to play an important role in the structural conversion. PrPC binds Zn(II) ions and may be involved in metal ion transport and zinc homeostasis. Here, we use multiple biophysical techniques including optical and NMR spectroscopy, molecular dynamics simulations, and

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Bose, Rumela, Madhubanti Ghosh, and Rupasri Ain. "Pleiotropic Function of Cellular Prion Protein: Encompassing Endoplasmic‐Reticulum Stress, Cell Proliferation in Vascular Smooth Muscle Cells." Journal of Cellular Biochemistry 126, no. 1 (2025). https://doi.org/10.1002/jcb.30692.

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ABSTRACTCellular prion protein (PRNP) has been implicated in various physiological processes in different cell types, for decades. Little has been known how PRNP functions in multiple, yet related processes within a particular system. In our current study, with the aid of high‐throughput RNA‐sequencing technique, we have presented an overall transcriptome profile of rat vascular smooth muscle cells (VSMCs) with Prnp knockdown. Fifty‐one genes were found to be differentially regulated, of which, genes involved in cell proliferation and endoplasmic reticulum (ER) stress pathway, show significant

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Yang, Dongming, Jie Li, Zhiping Li, et al. "Cardiolipin externalization mediates prion protein (PrP) peptide 106–126-associated mitophagy and mitochondrial dysfunction." Frontiers in Molecular Neuroscience 16 (June 2, 2023). http://dx.doi.org/10.3389/fnmol.2023.1163981.

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Proper mitochondrial performance is imperative for the maintenance of normal neuronal function to prevent the development of neurodegenerative diseases. Persistent accumulation of damaged mitochondria plays a role in prion disease pathogenesis, which involves a chain of events that culminate in the generation of reactive oxygen species and neuronal death. Our previous studies have demonstrated that PINK1/Parkin-mediated mitophagy induced by PrP106−126 is defective and leads to an accumulation of damaged mitochondria after PrP106−126 treatment. Externalized cardiolipin (CL), a mitochondria-spec

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Torii, Tomohiro, Yuki Miyamoto, and Junji Yamauchi. "Myelination by signaling through Arf guanine nucleotide exchange factor." Journal of Neurochemistry, June 18, 2024. http://dx.doi.org/10.1111/jnc.16141.

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AbstractDuring myelination, large quantities of proteins are synthesized and transported from the endoplasmic reticulum (ER)‐trans‐Golgi network (TGN) to their appropriate locations within the intracellular region and/or plasma membrane. It is widely believed that oligodendrocytes uptake neuronal signals from neurons to regulate the endocytosis‐ and exocytosis‐mediated intracellular trafficking of major myelin proteins such as myelin‐associated glycoprotein (MAG) and proteolipid protein 1 (PLP1). The small GTPases of the adenosine diphosphate (ADP) ribosylation factor (Arf) family constitute a

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Seeker, Luise A., Nadine Bestard-Cuche, Sarah Jäkel, et al. "Brain matters: unveiling the distinct contributions of region, age, and sex to glia diversity and CNS function." Acta Neuropathologica Communications 11, no. 1 (2023). http://dx.doi.org/10.1186/s40478-023-01568-z.

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AbstractThe myelinated white matter tracts of the central nervous system (CNS) are essential for fast transmission of electrical impulses and are often differentially affected in human neurodegenerative diseases across CNS region, age and sex. We hypothesize that this selective vulnerability is underpinned by physiological variation in white matter glia. Using single nucleus RNA sequencing of human post-mortem white matter samples from the brain, cerebellum and spinal cord and subsequent tissue-based validation we found substantial glial heterogeneity with tissue region: we identified region-s

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Santarelli, Stefania, Chiara Londero, Alessia Soldano, et al. "Drosophila melanogaster as a model to study autophagy in neurodegenerative diseases induced by proteinopathies." Frontiers in Neuroscience 17 (May 18, 2023). http://dx.doi.org/10.3389/fnins.2023.1082047.

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Proteinopathies are a large group of neurodegenerative diseases caused by both genetic and sporadic mutations in particular genes which can lead to alterations of the protein structure and to the formation of aggregates, especially toxic for neurons. Autophagy is a key mechanism for clearing those aggregates and its function has been strongly associated with the ubiquitin-proteasome system (UPS), hence mutations in both pathways have been associated with the onset of neurodegenerative diseases, particularly those induced by protein misfolding and accumulation of aggregates. Many crucial discov

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Matamoros-Angles, A., A. Hervera, J. Soriano, et al. "Analysis of co-isogenic prion protein deficient mice reveals behavioral deficits, learning impairment, and enhanced hippocampal excitability." BMC Biology 20, no. 1 (2022). http://dx.doi.org/10.1186/s12915-021-01203-0.

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Abstract Background Cellular prion protein (PrPC) is a cell surface GPI-anchored protein, usually known for its role in the pathogenesis of human and animal prionopathies. However, increasing knowledge about the participation of PrPC in prion pathogenesis contrasts with puzzling data regarding its natural physiological role. PrPC is expressed in a number of tissues, including at high levels in the nervous system, especially in neurons and glial cells, and while previous studies have established a neuroprotective role, conflicting evidence for a synaptic function has revealed both reduced and e

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Bosch, Assumpció, and Raúl Estévez. "Megalencephalic Leukoencephalopathy: Insights Into Pathophysiology and Perspectives for Therapy." Frontiers in Cellular Neuroscience 14 (January 22, 2021). http://dx.doi.org/10.3389/fncel.2020.627887.

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Megalencephalic leukoencephalopathy with subcortical cysts (MLC) is a rare genetic disorder belonging to the group of vacuolating leukodystrophies. It is characterized by megalencephaly, loss of motor functions, epilepsy, and mild mental decline. In brain biopsies of MLC patients, vacuoles were observed in myelin and in astrocytes surrounding blood vessels. It is mainly caused by recessive mutations in MLC1 and HEPACAM (also called GLIALCAM) genes. These disease variants are called MLC1 and MLC2A with both types of patients sharing the same clinical phenotype. Besides, dominant mutations in HE

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Patwardhan, Supriya, Jeannette Delva, Letitia Beckett, et al. "The Impact of Redox Modification on the Global Substrate Selection of PKA C Alpha." FASEB Journal 30, S1 (2016). http://dx.doi.org/10.1096/fasebj.30.1_supplement.868.3.

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Reactive oxygen species (ROS), such as hydrogen peroxide (H2O2), impact many aspects of cellular physiology. Aside from the incidental generation of ROS that occurs during cellular respiration, regulated ROS production by professional ROS‐generating enzymes is now recognized as a key step in redox‐dependent signaling pathways. While our understanding of the mechanisms controlling cellular ROS levels has grown considerably in recent years, less is known about the molecular signaling events that occur downstream of ROS generation.Oxidation of redox‐sensitive Cys residues can directly impact cell

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Corraliza-Gomez, Miriam, Beatriz Bendito, David Sandonis-Camarero, et al. "Dual role of Apolipoprotein D as long-term instructive factor and acute signal conditioning microglial secretory and phagocytic responses." Frontiers in Cellular Neuroscience 17 (January 26, 2023). http://dx.doi.org/10.3389/fncel.2023.1112930.

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Microglial cells are recognized as very dynamic brain cells, screening the environment and sensitive to signals from all other cell types in health and disease. Apolipoprotein D (ApoD), a lipid-binding protein of the Lipocalin family, is required for nervous system optimal function and proper development and maintenance of key neural structures. ApoD has a cell and state-dependent expression in the healthy nervous system, and increases its expression upon aging, damage or neurodegeneration. An extensive overlap exists between processes where ApoD is involved and those where microglia have an a

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Baena-Montes, Jara M., Sahar Avazzadeh та Leo R. Quinlan. "α-synuclein pathogenesis in hiPSC models of Parkinson’s disease". Neuronal Signaling 5, № 2 (2021). http://dx.doi.org/10.1042/ns20210021.

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Abstract α-synuclein is an increasingly prominent player in the pathology of a variety of neurodegenerative conditions. Parkinson’s disease (PD) is a neurodegenerative disorder that affects mainly the dopaminergic (DA) neurons in the substantia nigra of the brain. Typical of PD pathology is the finding of protein aggregations termed ‘Lewy bodies’ in the brain regions affected. α-synuclein is implicated in many disease states including dementia with Lewy bodies (DLB) and Alzheimer’s disease. However, PD is the most common synucleinopathy and continues to be a significant focus of PD research in

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Lichtenthaler, Stefan F., Pieter Giesbertz, Ana Graf, Matthew E. Kennedy, Naotaka Horiguchi, and Stephan A. Müller. "Human CSF pharmacoproteomics establishes in vivo‐relevant BACE1 substrates as pharmacodynamic biomarkers for chronic BACE inhibition in clinical trials." Alzheimer's & Dementia 19, S24 (2023). http://dx.doi.org/10.1002/alz.082943.

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AbstractBackgroundBACE1 is a major drug target for Alzheimer’s disease, but several late‐stage clinical trials with BACE‐inhibitors were associated with adverse events, most notably worsening in measures of cognitive function. Inhibition of BACE1‐dependent processing of a set of CNS membrane proteins is possibly responsible for these adverse findings. It is however unknown, which physiological BACE1 substrates are affected in humans at clinically relevant doses of a BACE inhibitor. To identify such substrates, we carried out a quantitative proteomic analysis of cerebrospinal fluid (CSF) from a

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