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

Author: Grafiati

Published: 14 March 2023

Last updated: 31 July 2025

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1

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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2

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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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

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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5

Das, Alvin S., and Wen-Quan Zou. "Prions: Beyond a Single Protein." Clinical Microbiology Reviews 29, no. 3 (2016): 633–58. http://dx.doi.org/10.1128/cmr.00046-15.

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SUMMARYSince the term protein was first coined in 1838 and protein was discovered to be the essential component of fibrin and albumin, all cellular proteins were presumed to play beneficial roles in plants and mammals. However, in 1967, Griffith proposed that proteins could be infectious pathogens and postulated their involvement in scrapie, a universally fatal transmissible spongiform encephalopathy in goats and sheep. Nevertheless, this novel hypothesis had not been evidenced until 1982, when Prusiner and coworkers purified infectious particles from scrapie-infected hamster brains and demons

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6

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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7

Gavín, Rosalina, Laia Lidón, Isidre Ferrer, and José Antonio del Río. "The Quest for Cellular Prion Protein Functions in the Aged and Neurodegenerating Brain." Cells 9, no. 3 (2020): 591. http://dx.doi.org/10.3390/cells9030591.

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Cellular (also termed ‘natural’) prion protein has been extensively studied for many years for its pathogenic role in prionopathies after misfolding. However, neuroprotective properties of the protein have been demonstrated under various scenarios. In this line, the involvement of the cellular prion protein in neurodegenerative diseases other than prionopathies continues to be widely debated by the scientific community. In fact, studies on knock-out mice show a vast range of physiological functions for the protein that can be supported by its ability as a cell surface scaffold protein. In this

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8

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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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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10

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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11

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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12

Linden, Rafael, Vilma R. Martins, Marco A. M. Prado, Martín Cammarota, Iván Izquierdo, and Ricardo R. Brentani. "Physiology of the Prion Protein." Physiological Reviews 88, no. 2 (2008): 673–728. http://dx.doi.org/10.1152/physrev.00007.2007.

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Prion diseases are transmissible spongiform encephalopathies (TSEs), attributed to conformational conversion of the cellular prion protein (PrPC) into an abnormal conformer that accumulates in the brain. Understanding the pathogenesis of TSEs requires the identification of functional properties of PrPC. Here we examine the physiological functions of PrPCat the systemic, cellular, and molecular level. Current data show that both the expression and the engagement of PrPCwith a variety of ligands modulate the following: 1) functions of the nervous and immune systems, including memory and inflamma

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13

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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14

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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15

Loh, Doris, and Russel J. Reiter. "Melatonin: Regulation of Prion Protein Phase Separation in Cancer Multidrug Resistance." Molecules 27, no. 3 (2022): 705. http://dx.doi.org/10.3390/molecules27030705.

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The unique ability to adapt and thrive in inhospitable, stressful tumor microenvironments (TME) also renders cancer cells resistant to traditional chemotherapeutic treatments and/or novel pharmaceuticals. Cancer cells exhibit extensive metabolic alterations involving hypoxia, accelerated glycolysis, oxidative stress, and increased extracellular ATP that may activate ancient, conserved prion adaptive response strategies that exacerbate multidrug resistance (MDR) by exploiting cellular stress to increase cancer metastatic potential and stemness, balance proliferation and differentiation, and amp

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16

Abi Nahed, Roland, Hasan Safwan-Zaiter, Kevin Gemy, et al. "The Multifaceted Functions of Prion Protein (PrPC) in Cancer." Cancers 15, no. 20 (2023): 4982. http://dx.doi.org/10.3390/cancers15204982.

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The cellular prion protein (PrPC) is a glycoprotein anchored to the cell surface by glycosylphosphatidylinositol (GPI). PrPC is expressed both in the brain and in peripheral tissues. Investigations on PrPC’s functions revealed its direct involvement in neurodegenerative and prion diseases, as well as in various physiological processes such as anti-oxidative functions, copper homeostasis, trans-membrane signaling, and cell adhesion. Recent findings have revealed the ectopic expression of PrPC in various cancers including gastric, melanoma, breast, colorectal, pancreatic, as well as rare cancers

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17

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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18

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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19

Robertson, Catherine, Stephanie A. Booth, Daniel R. Beniac, Michael B. Coulthart, Timothy F. Booth, and Archibald McNicol. "Cellular prion protein is released on exosomes from activated platelets." Blood 107, no. 10 (2006): 3907–11. http://dx.doi.org/10.1182/blood-2005-02-0802.

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Cellular prion protein (PrPC) is a glycophosphatidylinositol (GPI)–anchored protein, of unknown function, found in a number of tissues throughout the body, including several blood components of which platelets constitute the largest reservoir in humans. It is widely believed that a misfolded, protease-resistant form of PrPC, PrPSc, is responsible for the transmissible spongiform encephalopathy (TSE) group of fatal neurodegenerative diseases. Although the pathogenesis of TSEs is poorly understood, it is known that PrPC must be present in order for the disease to progress; thus, it is important

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20

Zayed, Mohammed, Sung-Ho Kook, and Byung-Hoon Jeong. "Potential Therapeutic Use of Stem Cells for Prion Diseases." Cells 12, no. 19 (2023): 2413. http://dx.doi.org/10.3390/cells12192413.

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Prion diseases are neurodegenerative disorders that are progressive, incurable, and deadly. The prion consists of PrPSc, the misfolded pathogenic isoform of the cellular prion protein (PrPC). PrPC is involved in a variety of physiological functions, including cellular proliferation, adhesion, differentiation, and neural development. Prion protein is expressed on the membrane surface of a variety of stem cells (SCs), where it plays an important role in the pluripotency and self-renewal matrix, as well as in SC differentiation. SCs have been found to multiply the pathogenic form of the prion pro

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21

Poddar, Anirban, T. N. Kundu, Manaly Sinha Ray, and Rituparna Maji. "Transmissible Spongiform Encephalopathies Prion Proteins: A Systematic Review." International Journal of Applied Biology 7, no. 2 (2023): 46–53. http://dx.doi.org/10.20956/ijab.v7i2.31044.

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Prion proteins (PrPc) have been implicated as the causative agent of “Transmissible Spongiform Encephalopathies” (TSE). Apart from this devilish role, prions also have a bright facet of their own and their identity holds much more than just being a pathogenic entity. Role of prions as scaffolding proteins for ligand binding and signal transduction has been reported by several researchers. Role of prions in nerve impulse transmission at neuronal junctions, glyapse and gap junctions have been reported. Prion mediated regulation of calcium ion flux and redox status in turn regulates many major ce

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22

Kawahara, Masahiro, Midori Kato-Negishi, and Ken-ichiro Tanaka. "Neurometals in the Pathogenesis of Prion Diseases." International Journal of Molecular Sciences 22, no. 3 (2021): 1267. http://dx.doi.org/10.3390/ijms22031267.

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Prion diseases are progressive and transmissive neurodegenerative diseases. The conformational conversion of normal cellular prion protein (PrPC) into abnormal pathogenic prion protein (PrPSc) is critical for its infection and pathogenesis. PrPC possesses the ability to bind to various neurometals, including copper, zinc, iron, and manganese. Moreover, increasing evidence suggests that PrPC plays essential roles in the maintenance of homeostasis of these neurometals in the synapse. In addition, trace metals are critical determinants of the conformational change and toxicity of PrPC. Here, we r

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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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Martellucci, Stefano, Costantino Santacroce, Francesca Santilli, Valeria Manganelli, Maurizio Sorice, and Vincenzo Mattei. "Prion Protein in Stem Cells: A Lipid Raft Component Involved in the Cellular Differentiation Process." International Journal of Molecular Sciences 21, no. 11 (2020): 4168. http://dx.doi.org/10.3390/ijms21114168.

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The prion protein (PrP) is an enigmatic molecule with a pleiotropic effect on different cell types; it is localized stably in lipid raft microdomains and it is able to recruit downstream signal transduction pathways by its interaction with various biochemical partners. Since its discovery, this lipid raft component has been involved in several functions, although most of the publications focused on the pathological role of the protein. Recent studies report a key role of cellular prion protein (PrPC) in physiological processes, including cellular differentiation. Indeed, the PrPC, whose expres

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Ryskalin, Larisa, Francesca Biagioni, Carla L. Busceti, et al. "The Role of Cellular Prion Protein in Promoting Stemness and Differentiation in Cancer." Cancers 13, no. 2 (2021): 170. http://dx.doi.org/10.3390/cancers13020170.

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Cellular prion protein (PrPC) is seminal to modulate a variety of baseline cell functions to grant homeostasis. The classic role of such a protein was defined as a chaperone-like molecule being able to rescue cell survival. Nonetheless, PrPC also represents the precursor of the deleterious misfolded variant known as scrapie prion protein (PrPSc). This variant is detrimental in a variety of prion disorders. This multi-faceted role of PrP is greatly increased by recent findings showing how PrPC in its folded conformation may foster tumor progression by acting at multiple levels. The present revi

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Monette, Anne, and Andrew J. Mouland. "Zinc and Copper Ions Differentially Regulate Prion-Like Phase Separation Dynamics of Pan-Virus Nucleocapsid Biomolecular Condensates." Viruses 12, no. 10 (2020): 1179. http://dx.doi.org/10.3390/v12101179.

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Liquid-liquid phase separation (LLPS) is a rapidly growing research focus due to numerous demonstrations that many cellular proteins phase-separate to form biomolecular condensates (BMCs) that nucleate membraneless organelles (MLOs). A growing repertoire of mechanisms supporting BMC formation, composition, dynamics, and functions are becoming elucidated. BMCs are now appreciated as required for several steps of gene regulation, while their deregulation promotes pathological aggregates, such as stress granules (SGs) and insoluble irreversible plaques that are hallmarks of neurodegenerative dise

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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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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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Benvegnù, Stefano, Paola Roncaglia, Federica Agostini, et al. "Developmental influence of the cellular prion protein on the gene expression profile in mouse hippocampus." Physiological Genomics 43, no. 12 (2011): 711–25. http://dx.doi.org/10.1152/physiolgenomics.00205.2010.

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The conversion of the cellular prion protein (PrPC) to an abnormal and protease-resistant isoform is the key event in prion diseases. Mice lacking PrPC are resistant to prion infection, and downregulation of PrPC during prion infection prevents neuronal loss and the progression to clinical disease. These results are suggestive of the potential beneficial effect of silencing PrPC during prion diseases. However, the silencing of a protein that is widely expressed throughout the central nervous system could be detrimental to brain homeostasis. The physiological role of PrPC remains still unclear,

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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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Glierova, Hana, Martin Panigaj, Jana Semberova, et al. "Impairment of Erythropoiesis In Inbred Cellular Prion Protein Deficient Mice." Blood 116, no. 21 (2010): 2032. http://dx.doi.org/10.1182/blood.v116.21.2032.2032.

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Abstract Abstract 2032 Cellular prion protein (PrPc) plays a key role in pathogenesis of prion diseases, however, its physiologic function remains unclear. The involvement of PrPc in hematopoiesis was suggested by importance of its expression for self renewal and survival of long term repopulating hematopoietic stem cells. Prion diseases were shown to deregulate transcription of several erythroid genes and we have demonstrated reduction of erythroid cell and erythropoietin production in FVB PrP-/- (Zurich I) mice in response to acute anemia (Zivny J. et al. Blood Cells Mol Dis. 2008;40:302-307

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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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Tamaki, Yoshitaka, and Makoto Urushitani. "Molecular Dissection of TDP-43 as a Leading Cause of ALS/FTLD." International Journal of Molecular Sciences 23, no. 20 (2022): 12508. http://dx.doi.org/10.3390/ijms232012508.

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TAR DNA binding protein 43 (TDP-43) is a DNA/RNA binding protein involved in pivotal cellular functions, especially in RNA metabolism. Hyperphosphorylated and ubiquitinated TDP-43-positive neuronal cytoplasmic inclusions are identified in the brain and spinal cord in most cases of amyotrophic lateral sclerosis (ALS) and a substantial proportion of frontotemporal lobar degeneration (FTLD) cases. TDP-43 dysfunctions and cytoplasmic aggregation seem to be the central pathogenicity in ALS and FTLD. Therefore, unraveling both the physiological and pathological mechanisms of TDP-43 may enable the ex

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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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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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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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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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Messerli, Mark A., and Anyesha Sarkar. "Advances in Electrochemistry for Monitoring Cellular Chemical Flux." Current Medicinal Chemistry 26, no. 26 (2019): 4984–5002. http://dx.doi.org/10.2174/0929867326666190506111629.

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The transport of molecules and inorganic ions across the plasma membrane results in chemical fluxes that reflect cellular function in healthy and diseased states. Measurement of these chemical fluxes enables the characterization of protein function and transporter stoichiometry, characterization of the viability of single cells and embryos prior to implantation, and screening of pharmaceutical agents. Electrochemical sensors are sensitive and noninvasive tools for measuring chemical fluxes immediately outside the cells in the boundary layer, that are capable of monitoring a diverse range of tr

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Puig, Berta, Denise Yang, Santra Brenna, Hermann Clemens Altmeppen, and Tim Magnus. "Show Me Your Friends and I Tell You Who You Are: The Many Facets of Prion Protein in Stroke." Cells 9, no. 7 (2020): 1609. http://dx.doi.org/10.3390/cells9071609.

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Ischemic stroke belongs to the leading causes of mortality and disability worldwide. Although treatments for the acute phase of stroke are available, not all patients are eligible. There is a need to search for therapeutic options to promote neurological recovery after stroke. The cellular prion protein (PrPC) has been consistently linked to a neuroprotective role after ischemic damage: it is upregulated in the penumbra area following stroke in humans, and animal models of stroke have shown that lack of PrPC aggravates the ischemic damage and lessens the functional outcome. Mechanistically, th

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Carulla, Patricia, Ana Bribián, Alejandra Rangel, et al. "Neuroprotective role of PrPC against kainate-induced epileptic seizures and cell death depends on the modulation of JNK3 activation by GluR6/7–PSD-95 binding." Molecular Biology of the Cell 22, no. 17 (2011): 3041–54. http://dx.doi.org/10.1091/mbc.e11-04-0321.

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Cellular prion protein (PrPC) is a glycosyl-phosphatidylinositol–anchored glycoprotein. When mutated or misfolded, the pathogenic form (PrPSC) induces transmissible spongiform encephalopathies. In contrast, PrPC has a number of physiological functions in several neural processes. Several lines of evidence implicate PrPC in synaptic transmission and neuroprotection since its absence results in an increase in neuronal excitability and enhanced excitotoxicity in vitro and in vivo. Furthermore, PrPC has been implicated in the inhibition of N-methyl-d-aspartic acid (NMDA)–mediated neurotransmission

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Minasov, George, Nicole L. Inniss, Ludmilla Shuvalova, Wayne F. Anderson, and Karla J. F. Satchell. "Structure of the Monkeypox virus profilin-like protein A42R reveals potential functional differences from cellular profilins." Acta Crystallographica Section F Structural Biology Communications 78, no. 10 (2022): 371–77. http://dx.doi.org/10.1107/s2053230x22009128.

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The infectious disease human monkeypox is spreading rapidly in 2022, causing a global health crisis. The genomics of Monkeypox virus (MPXV) have been extensively analyzed and reported, although little is known about the virus-encoded proteome. In particular, there are no reported experimental MPXV protein structures other than computational models. Here, a 1.52 Å resolution X-ray structure of the MPXV protein A42R, the first MPXV-encoded protein with a known structure, is reported. A42R shows structural similarity to profilins, which are cellular proteins that are known to function in the regu

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Lidón, Laia, Laura Llaó-Hierro, Mario Nuvolone та ін. "Tau Exon 10 Inclusion by PrPC through Downregulating GSK3β Activity". International Journal of Molecular Sciences 22, № 10 (2021): 5370. http://dx.doi.org/10.3390/ijms22105370.

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Tau protein is largely responsible for tauopathies, including Alzheimer’s disease (AD), where it accumulates in the brain as insoluble aggregates. Tau mRNA is regulated by alternative splicing, and inclusion or exclusion of exon 10 gives rise to the 3R and 4R isoforms respectively, whose balance is physiologically regulated. In this sense, one of the several factors that regulate alternative splicing of tau is GSK3β, whose activity is inhibited by the cellular prion protein (PrPC), which has different physiological functions in neuroprotection and neuronal differentiation. Moreover, a relation

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Chrobak, Adrian Andrzej, Patrycja Pańczyszyn-Trzewik, Patrycja Król, Magdalena Pawelec-Bąk, Dominika Dudek, and Marcin Siwek. "New Light on Prions: Putative Role of PrPc in Pathophysiology of Mood Disorders." International Journal of Molecular Sciences 25, no. 5 (2024): 2967. http://dx.doi.org/10.3390/ijms25052967.

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Mood disorders are highly prevalent and heterogenous mental illnesses with devastating rates of mortality and treatment resistance. The molecular basis of those conditions involves complex interplay between genetic and environmental factors. Currently, there are no objective procedures for diagnosis, prognosis and personalization of patients’ treatment. There is an urgent need to search for novel molecular targets for biomarkers in mood disorders. Cellular prion protein (PrPc) is infamous for its potential to convert its insoluble form, leading to neurodegeneration in Creutzfeldt-Jacob disease

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de Rooij, Laura Adriana, Dirk Jan Mastebroek, Nicky ten Voorde, Elsken van der Wall, Paul Joannes van Diest, and Cathy Beatrice Moelans. "The microRNA Lifecycle in Health and Cancer." Cancers 14, no. 23 (2022): 5748. http://dx.doi.org/10.3390/cancers14235748.

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MicroRNAs (miRNAs) are small non-coding RNAs of ~22 nucleotides that regulate gene expression at the post-transcriptional level. They can bind to around 60% of all protein-coding genes with an average of 200 targets per miRNA, indicating their important function within physiological and pathological cellular processes. miRNAs can be quickly produced in high amounts through canonical and non-canonical pathways that involve a multitude of steps and proteins. In cancer, miRNA biogenesis, availability and regulation of target expression can be altered to promote tumour progression. This can be due

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Lee, Simon C., Christine A. Robson-Doucette, and Michael B. Wheeler. "Uncoupling protein 2 regulates reactive oxygen species formation in islets and influences susceptibility to diabetogenic action of streptozotocin." Journal of Endocrinology 203, no. 1 (2009): 33–43. http://dx.doi.org/10.1677/joe-09-0117.

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Currently, the physiological function of uncoupling protein-2 (UCP2) in pancreatic islets and its role in the development of diabetes is a matter of great debate. To further investigate the impact of UCP2 on diabetes development, we used streptozotocin (STZ) to experimentally generate diabetes in both wild-type (WT) and UCP2-knockout (UCP2KO) mice. While multiple low-dose STZ injections led to hyperglycemia development over a 14-day period in both WT and UCP2KO mice, we found the development of hyperglycemia to be significantly less severe in the UCP2KO mice. Measurement of insulin and glucago

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Peña Ccoa, Willmor J., and Glen M. Hocky. "Assessing models of force-dependent unbinding rates via infrequent metadynamics." Journal of Chemical Physics 156, no. 12 (2022): 125102. http://dx.doi.org/10.1063/5.0081078.

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Protein–ligand interactions are crucial for a wide range of physiological processes. Many cellular functions result in these non-covalent “bonds” being mechanically strained, and this can be integral to proper cellular function. Broadly, two classes of force dependence have been observed—slip bonds, where the unbinding rate increases, and catch bonds, where the unbinding rate decreases. Despite much theoretical work, we cannot predict for which protein–ligand pairs, pulling coordinates, and forces a particular rate dependence will appear. Here, we assess the ability of MD simulations combined

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Fries, Erik, and Aneta Kaczmarczyk. "Inter-alpha-inhibitor, hyaluronan and inflammation." Acta Biochimica Polonica 50, no. 3 (2003): 735–42. http://dx.doi.org/10.18388/abp.2003_3664.

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Inter-alpha-inhibitor is an abundant plasma protein whose physiological function is only now beginning to be revealed. It consists of three polypeptides: two heavy chains and one light chain called bikunin. Bikunin, which has antiproteolytic activity, carries a chondroitin sulphate chain to which the heavy chains are covalently linked. The heavy chains can be transferred from inter-alpha-inhibitor to hyaluronan molecules and become covalently linked. This reaction seems to be mediated by TSG-6, a protein secreted by various cells upon stimulation by inflammatory cytokines. Inter-alpha-inhibito

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Gidon-Jeangirard, Carole, Bénédicte Hugel, Vincent Holl, et al. "Annexin V Delays Apoptosis While Exerting an External Constraint Preventing the Release of CD4+ and PrPc+ Membrane Particles in a Human T Lymphocyte Model." Journal of Immunology 162, no. 10 (1999): 5712–18. http://dx.doi.org/10.4049/jimmunol.162.10.5712.

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Abstract Phosphatidylserine exposure in the exoplasmic leaflet of the plasma membrane is one of the early hallmarks of cells undergoing apoptosis. The shedding of membrane particles carrying Ags testifying to their tissue origin is another characteristic feature. Annexin V, a protein of as yet unknown specific physiologic function, presents a high Ca2+-dependent affinity for phosphatidylserine and forms two-dimensional arrays at the membrane surface. In this study, we report the delaying action of annexin V on apoptosis in the CEM human T cell line expressing CD4 and the normal cellular prion

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Griffoni, Cristiana, Mattia Toni, Enzo Spisni, et al. "The Cellular Prion Protein: Biochemistry, Topology, and Physiologic Functions." Cell Biochemistry and Biophysics 38, no. 3 (2003): 287–304. http://dx.doi.org/10.1385/cbb:38:3:287.

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Zomosa-Signoret, Viviana, Jacques-Damien Arnaud, Pascaline Fontes, Maria-Terresa Alvarez-Martinez, and Jean-Pierre Liautard. "Physiological role of the cellular prion protein." Veterinary Research 39, no. 4 (2007): 09. http://dx.doi.org/10.1051/vetres:2007048.

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