Relevant bibliographies by topics / Cellular prion protein physiological function

Academic literature on the topic 'Cellular prion protein physiological function'

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Published: 14 March 2023

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

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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 (May 2001): 585–95. http://dx.doi.org/10.1590/s0100-879x2001000500005.

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Franzmann, Titus M., Marcus Jahnel, Andrei Pozniakovsky, Julia Mahamid, Alex S. Holehouse, Elisabeth Nüske, Doris Richter, et al. "Phase separation of a yeast prion protein promotes cellular fitness." Science 359, no. 6371 (January 4, 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 by rescuing the essential Sup35 translation factor from stress-induced damage. Thus, prion-like domains represent conserved environmental stress sensors that facilitate rapid adaptation in unstable environments by modifying protein phase behavior.
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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 (September 25, 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 appear to be affected by interacting protein partners. The key challenge in identifying a potential interacting partner is to demonstrate that binding to a specific ligand is necessary for cellular physiological function or malfunction. In this review, we have summarized the intracellular and extracellular interacting partners of PrPc and potential consequences of their binding. We also briefly describe prion disease-related mutations at the end of this review.
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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 (June 2007): 629–44. http://dx.doi.org/10.1016/j.bbadis.2007.02.011.

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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 (May 22, 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 regulatory influence of microRNAs, small molecules, and signaling proteins. Targeting PrPC in acute and chronic kidney disease could help improve iron homeostasis, ameliorate damage from ischemia/reperfusion injury, and enhance the efficacy of mesenchymal stem/stromal cell or extracellular vesicle-based therapeutic strategies. PrPC may also be under the influence of BMP/Smad signaling and affect the progression of TGF-β-related renal fibrosis. PrPC conveys TNF-α resistance in some renal cancers, and therefore, the coadministration of anti-PrPC antibodies improves chemotherapy. PrPC can be used to design antibody–drug conjugates, aptamer–drug conjugates, and customized tissue inhibitors of metalloproteinases to suppress cancer. With preclinical studies demonstrating promising results, further research on PrPC in the kidney may lead to innovative PrPC-based therapeutic strategies for renal disease.
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Das, Alvin S., and Wen-Quan Zou. "Prions: Beyond a Single Protein." Clinical Microbiology Reviews 29, no. 3 (May 25, 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 demonstrated that they consisted of a specific protein that he called a “prion.” Unprecedentedly, the infectious prion pathogen is actually derived from its endogenous cellular form in the central nervous system. Unlike other infectious agents, such as bacteria, viruses, and fungi, prions do not contain genetic materials such as DNA or RNA. The unique traits and genetic information of prions are believed to be encoded within the conformational structure and posttranslational modifications of the proteins. Remarkably, prion-like behavior has been recently observed in other cellular proteins—not only in pathogenic roles but also serving physiological functions. The significance of these fascinating developments in prion biology is far beyond the scope of a single cellular protein and its related disease.
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Dondapati, Divya Teja, Pradeep Reddy Cingaram, Ferhan Ayaydin, Antal Nyeste, Andor Kanyó, Ervin Welker, and Elfrieda Fodor. "Membrane Domain Localization and Interaction of the Prion-Family Proteins, Prion and Shadoo with Calnexin." Membranes 11, no. 12 (December 13, 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 been reported for the two; however, the amount of data about their exact functions is lacking. Protein–protein interactions and membrane microdomain localizations are key determinants of protein function. Accurate identification of these functions for a membrane protein, however, can become biased due to interactions occurring during sample processing. To avoid such artifacts, we apply a non-detergent-based membrane-fractionation approach to study the prion protein and Shadoo. We show that the two proteins occupy similarly raft and non-raft membrane fractions when expressed in N2a cells and that both proteins pull down the chaperone calnexin in both rafts and non-rafts. These indicate their possible binding to calnexin in both types of membrane domains, which might be a necessary requisite to aid the inherently unstable native conformation during their lifetime.
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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 (March 2, 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 review, we first summarize the most commonly described roles of cellular prion protein in neuroprotection, including antioxidant and antiapoptotic activities and modulation of glutamate receptors. Second, in light of recently described interaction between cellular prion protein and some amyloid misfolded proteins, we will also discuss the molecular mechanisms potentially involved in protection against neurodegeneration in pathologies such as Alzheimer’s, Parkinson’s, and Huntington’s diseases.
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Kovač, Valerija, and Vladka Čurin Šerbec. "Prion Protein: The Molecule of Many Forms and Faces." International Journal of Molecular Sciences 23, no. 3 (January 22, 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 as neuroprotection in ischemia. Upon proteolytic cleavage, PrPC is transformed into released and attached forms of PrP that can, depending on the contained structural characteristics of PrPC, display protective or toxic properties. In this review, we will outline prion protein and prion protein fragment properties as well as overview their involvement with interacting partners and signal pathways in myelination, neuroprotection and neurodegenerative diseases.
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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 P2X4receptor when both are coexpressed. PrPCexpression does not significantly change the ATP concentration-response curve in oocytes expressing P2X4receptors. However, the presence of PrPCreduces the inhibition by Cu2+of the ATP-elicited currents in these oocytes, confirming our previous observations with the Cu2+binding domain. Thus, our observations suggest a role for PrPCin modulating synaptic activity through binding of extracellular Cu2+.
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Dissertations / Theses on the topic "Cellular prion protein physiological function"

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Thurm, Dana Kathrin [Verfasser], and Markus [Akademischer Betreuer] Glatzel. "Novel Physiological Function of the Cellular Prion Protein (PrPC) in Exosomal Trafficking / Dana Kathrin Thurm. Betreuer: Markus Glatzel." Hamburg : Staats- und Universitätsbibliothek Hamburg, 2012. http://d-nb.info/1022684361/34.

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Thurm, Dana Kathrin Verfasser], and Markus [Akademischer Betreuer] [Glatzel. "Novel Physiological Function of the Cellular Prion Protein (PrPC) in Exosomal Trafficking / Dana Kathrin Thurm. Betreuer: Markus Glatzel." Hamburg : Staats- und Universitätsbibliothek Hamburg, 2012. http://nbn-resolving.de/urn:nbn:de:gbv:18-56417.

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Isaacs, J. D. "Immunogenicity and immune function of the cellular prion protein." Thesis, University College London (University of London), 2007. http://discovery.ucl.ac.uk/1444752/.

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Prion protein (PrP) is the only factor known to be essential in the pathogenesis of the transmissible spongiform encephalopathies (TSEs) or prion diseases. The cellular isoform (PrPc), a GPI-anchored sialoglycoprotein of unknown function, has an identical primary structure to the disease-associated conformer (PrPSc). Thus, animals are tolerant to PrPSc and TSEs do not trigger a classical immune response. Vaccine development for human TSEs requires elucidation of the immunodominant human T cell epitopes within PrP. Further, successful immunotherapy requires that the function of PrPc in lymphocytes is understood, as therapeutic targeting of prion protein risks interfering with immune function. Peripheral blood leukocytes from healthy donors were cultured with PrP sequence peptides to elicit proliferative and cytokine responses. Responses were seen to peptides clustered around the position 129 polymorphism and the C-terminus, in accordance with a predictive algorithm. The substitution of methionine by valine at position 129 altered both epitope immunogenicity and cytokine profile. Studies in murine T cell activation models demonstrated transcriptional and late surface protein upregulation of PrPc. Memory T cells expressed higher PrPc levels than naive cells and there was also a strong correlation at both protein and transcriptional levels between expression of PrPc and the regulatory T cell marker, Foxp3. Embryonic deletion of Prnp did not lead to deficits in T cell conjugation, proliferation or cytokine production, although memory cell numbers were slightly reduced. In PrP*7" mice regulatory T cells developed normally but may have enhanced suppressor function. However, neither PrP ablation nor anti-PrP monoclonal antibodies altered the phenotype of T cell mediated autoimmune disease. These findings demonstrate that tolerance to PrP is not complete in humans and raise the prospect of generating protective immunity through vaccination. However, PrPc is a potentially important memory, regulatory and T cell activation antigen, therapeutic disruption of which may precipitate immunopathology.
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Dodelet, Vincent C. "Distribution and function of the normal cellular isoform of the prion protein." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1998. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape10/PQDD_0023/NQ50322.pdf.

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Weiß, Eva Annabelle. "Analyse der Proteinexpression zur Untersuchung der physiologischen Funktion des zellulären Prionproteins (PrPc)." Doctoral thesis, 2012. http://hdl.handle.net/11858/00-1735-0000-0006-B2B7-B.

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Glier, Hana. "Exprese a funkce buněčného prionového proteinu na krevních buňkách." Doctoral thesis, 2012. http://www.nusl.cz/ntk/nusl-322648.

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The cellular prion protein (PrPc) is essential for pathogenesis of fatal neurodegenerative prion diseases. Recently reported four cases of vCJD transmission by blood transfusion raise concerns about the safety of blood products. Proper understanding of PrPc in blood is necessary for development of currently unavailable blood screening tests for prion diseases. Flow cytometry is an attractive method for prion detection, however, the reports on the quantity of PrPc on human blood cells are contradictory. We showed that the majority of PrPc in resting platelets is present in the intracellular pool and is localized in α-granules. We demostrated that both, human platelets and red blood cells (RBC) express significant amount of PrPc and thus may play an important role in the transmission of prions by blood transfusion. Our results suggest a unique modification of PrPc on human RBC. Such modification of pathological prion protein could distort the results of blood screening tests for prions. Further we showed that the storage of blood prior to analysis and the choice of anti-prion antibody greatly affect the detection of PrPc by flow cytometry and we identified platelet satellitism as a factor contributing to the heterogeneity of PrPc detection in blood cells. Moreover, we demonstrated existence of...
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Books on the topic "Cellular prion protein physiological function"

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R, Means Anthony, ed. Calcium regulation of cellular function. New York: Raven Press, 1995.

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Means, Anthony R. Calcium regulation of cellular function. New York: Raven Press, 1995.

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A, Wirtz Karel W., and NATO Advanced Study Institute on New Developments in Lipid-Protein Interactions and Receptor Function (1992 : Spetsai, Greece), eds. New developments in lipid-protein interactions and receptor function. New York: Plenum Press, 1993.

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NATO, Advanced Study Institute on Structure and Function of Interacting Protein Domains in Signal and Energy Transduction (1996 Acquafredda di Maratea Italy). Interacting protein domains: Their role in signal and energy transduction : [proceedings of the NATO Advanced Study Institute on Structure and Function of Interacting Protein Domains in Signal and Energy Transduction, held at Acquafredda di Maratea, Italy, September 10-19, 1996]. Berlin: Springer, 1997.

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Book chapters on the topic "Cellular prion protein physiological function"

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Landrier, Jean-François, Jacques Grober, Isabelle Zaghini, and Philippe Besnard. "Regulation of the ileal bile acid-binding protein gene: An approach to determine its physiological function(s)." In Cellular Lipid Binding Proteins, 149–55. Boston, MA: Springer US, 2002. http://dx.doi.org/10.1007/978-1-4419-9270-3_19.

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"7. Function of Cellular Prion Protein (PrPC) in Copper Homeostasis and Redox Signaling at the Synapse." In Prions in Humans and Animals, edited by Beat Hörnlimann, Detlev Riesner, and Hans A. Kretzschmar. Berlin, New York: Walter de Gruyter, 2006. http://dx.doi.org/10.1515/9783110200171.2.95.

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Oyindamola, Eyitayo Adeyemi, Maxwell Kwadwo Agyemang, Joseph Owusu-Sarfo, Oduro Kofi Yeboah, and Newman Osafo. "Microglial Mitophagy and Neurodegenerative Disorders." In Quality Control of Cellular Protein in Neurodegenerative Disorders, 88–128. IGI Global, 2020. http://dx.doi.org/10.4018/978-1-7998-1317-0.ch004.

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Microglia are important in the regulation of the inflammatory response in regulating the release of proinflammatory mediators in the brain. Through their phagocytic actions, microglia are significant in the CNS when it comes to the body's response to physiological insults by promoting repair of impaired brain function. They do so by engulfing and degrading microbes as well as brain-derived debris and proteins such as myelin and axonal fragments, amyloid-beta, and apoptotic cells. This mitophagic activity of microglia is of importance in neurodegeneration. In most neurodegenerative disorders, mitophagy is impaired with resultant accumulation of dysfunctional mitochondria as well as processes such as lysosomal fusion and autophagosomes. In Parkinson's and Alzheimer's for example, impaired mitophagy accounts for the build-up of α-synuclein and amyloid respectively in affected individuals. The chapter discusses extensively the link between microglia mitophagy and neurodegeration and how dysfunctional mitophagy increases the likelihood of their occurrence.
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Brenton, James D., and Tim Eisen. "The nature and development of cancer: Cancer mutations and their implications." In Oxford Textbook of Medicine, edited by Tim Eisen, 445–55. Oxford University Press, 2020. http://dx.doi.org/10.1093/med/9780198746690.003.0046.

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Cancer is a genetic disease in which progressive accumulation of mutations in the genome of somatic cells induces abnormal biological capabilities. Cancer-inducing mutations may originate from single base substitutions or large chromosomal rearrangements; but ultimately they disrupt normal cellular processes by altering protein function or disturbing the regulation of gene expression. Loss-of-function mutations in tumour suppressor genes inactivate physiological control of cell processes, whereas gain-of-function mutations directly affect physiological networks and, for example, induce pathological activation of signalling pathways. For many common cancers, we are now close to defining unique sets of somatic alterations which confer a specific signature of the cancer type and are also highly specific to the individual patient.
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Murugesan, Janaranjani, Ajithkumar Balakrishnan, Premkumar Kumpati, and Hemamalini Vedagiri. "Cellular Functions of ER Chaperones in Regulating Protein Misfolding and Aggregation: An Emerging Therapeutic Approach for Preeclampsia." In Preeclampsia. IntechOpen, 2022. http://dx.doi.org/10.5772/intechopen.101271.

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Proteinuria is one of the hallmarks of preeclampsia (PE) that differentiates other hypertensive disorders of pregnancy. Protein misfolding and aggregation is an emerging pathological condition underlying many chronic metabolic diseases and neurodegenerative diseases. Recent studies indicate protein aggregation as an emerging biomarker of preeclampsia, wherein several proteins are aggregated and dysregulated in the body fluids of preeclamptic women, provoking the multi-systemic clinical manifestations of the disease. At the cellular level, these misfolded and aggregated proteins are potentially toxic interfering with the normal physiological process, eliciting the unfolded protein response (UPR) pathway activators in the endoplasmic reticulum (ER) that subsequently augments the ER quality control systems to remove these aberrant proteins. ER resident chaperones, folding enzymes and other proteins serve as part of the ER quality control machinery in restoring nascent protein folding. These ER chaperones are crucial for ER function aiding in native protein folding, maintaining calcium homeostasis, as sensors of ER stress and also as immune modulators. Consequently, ER chaperones seems to be involved in many cellular processes, yet the association is expanding to be explored. Understanding the role and mechanism of ER chaperones in regulating protein misfolding and aggregation would provide new avenues for therapeutic intervention as well as for the development of new diagnostic approaches.
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Simons, Peter, and Charlotte M. Vines. "Analysis of GTP-Binding Protein–Coupled Receptor Assemblies by Flow Cytometry." In Flow Cytometry for Biotechnology. Oxford University Press, 2005. http://dx.doi.org/10.1093/oso/9780195183146.003.0022.

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GTP-binding protein–coupled receptors (GPCRs) represent the largest family of integral membrane signal-transducing molecules in the human genome, with estimates of at least 600 members. As such, they represent the targets of approximately 30%–50% of the prescription drugs on the market. They are involved in virtually every physiological process in the human body, with ligands including light, odorants, amines, peptides, proteins, lipids, and nucleotides. Binding of these ligands on the extracellular surface of the receptor leads to conformational changes within the receptor, resulting in a multitude of cellular responses. GPCRs, as their name implies, function through the actions of heterotrimeric GTP-binding proteins (G proteins). These G proteins then couple to a diverse array of effector molecules at the cell surface and inside the cell. GPCRs contain a common structural motif, with seven transmembrane alpha helices. With the recent description of the three-dimensional crystal structure of rhodopsin in its inactive state, a greater, though still incomplete, understanding of the functions of this receptor family has been achieved. In addition to the activation of G proteins, GPCRs undergo extensive regulation mediated primarily by a variety of kinases, including second messenger kinases and the family of G protein–coupled receptor kinases (GRKs). Following receptor phosphorylation by GRKs, additional proteins named arrestins associate with GPCRs. The traditional role of these molecules has been to serve as desensitizing agents, preventing further association of the receptor with G proteins. However, recent studies have demonstrated that arrestins can serve as adapters in the process of receptor internalization as well as scaffolds in the activation of numerous kinase pathways. Interactions between GPCRs and cellular proteins such as adaptins, rab GTPases, phosphatases, and ion channels have also been described. Thus, it has become apparent that understanding the interactions between GPCRs and their associated proteins is critical for any detailed understanding of receptor function. An overview of the activation and regulation of GPCRs is shown in figure 17.1 to provide a context for the approaches to be described in the remainder of this chapter.
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LeBar, Kristen, and Zhijie Wang. "Extracellular Matrix in Cardiac Tissue Mechanics and Physiology: Role of Collagen Accumulation." In Extracellular Matrix - Developments and Therapeutics [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.96585.

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The extracellular matrix (ECM) forms a mesh surrounding tissue, made up of fibrous and non-fibrous proteins that contribute to the cellular function, mechanical properties of the tissue and physiological function of the organ. The cardiac ECM remodels in response to mechanical alterations (e.g., pressure overload, volume overload) or injuries (e.g., myocardial infarction, bacterial infection), which further leads to mechanical and functional changes of the heart. Collagen, the most prevalent ECM protein in the body, contributes significantly to the mechanical behavior of myocardium during disease progression. Alterations in collagen fiber morphology and alignment, isoform, and cross-linking occur during the progression of various cardiac diseases. Acute or compensatory remodeling of cardiac ECM maintains normal cardiac function. However, chronic or decompensatory remodeling eventually results in heart failure, and the exact mechanism of transition into maladaptation remains unclear. This review aims to summarize the primary role of collagen accumulation (fibrosis) in heart failure progression, with a focus on its effects on myocardial tissue mechanical properties and cellular and organ functions.
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Zhou, Lang, Pengyu Chen, and Aleksandr Simonian. "Advanced Biosensing towards Real-Time Imaging of Protein Secretion from Single Cells." In Biosensor - Current and Novel Strategies for Biosensing [Working Title]. IntechOpen, 2020. http://dx.doi.org/10.5772/intechopen.94248.

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Protein secretion of cells plays a vital role in intercellular communication. The abnormality and dysfunction of cellular protein secretion are associated with various physiological disorders, such as malignant proliferation of cells, aberrant immune function, and bone marrow failure. The heterogeneity of protein secretion exists not only between varying populations of cells, but also in the same phenotype of cells. Therefore, characterization of protein secretion from single cell contributes not only to the understanding of intercellular communication in immune effector, carcinogenesis and metastasis, but also to the development and improvement of diagnosis and therapy of relative diseases. In spite of abundant highly sensitive methods that have been developed for the detection of secreted proteins, majority of them fall short in providing sufficient spatial and temporal resolution for comprehensive profiling of protein secretion from single cells. The real-time imaging techniques allow rapid acquisition and manipulation of analyte information on a 2D plane, providing high spatiotemporal resolution. Here, we summarize recent advances in real-time imaging of secretory proteins from single cell, including label-free and labelling techniques, shedding light on the development of simple yet powerful methodology for real-time imaging of single-cell protein secretion.
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Ross, John, Igor Schreiber, and Marcel O. Vlad. "Mini-Introduction to Bioinformatics." In Determination of Complex Reaction Mechanisms. Oxford University Press, 2006. http://dx.doi.org/10.1093/oso/9780195178685.003.0015.

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There is enormous interest in the biology of complex reaction systems, be it in metabolism, signal transduction, gene regulatory networks, protein synthesis, and many others. The field of the interpretation of experiments on such systems by application of the methods of information science, computer science, and biostatistics is called bioinformatics (see for a presentation of this subject). Part of it is an extension of the chemical approaches that we have discussed for obtaining information on the reaction mechanisms of complex chemical systems to complex biological and genetic systems. We present here a very brief introduction to this field, which is exploding with scientific and technical activity. No review is intended, only an indication of several approaches on the subject of our book, with apologies for the omission of vast numbers of publications. A few reminders: The entire complement of DNA molecules constitute the genome, which consists of many genes. RNA is generated from DNA in a process called transcription; the RNA that codes for proteins is known as messenger RNA, abbreviated tomRNA. Other RNAs code for functional molecules such as transfer RNAs, ribosomal components, and regulatory molecules, or even have enzymatic function. Protein synthesis is regulated by many mechanisms, including that for transcription initiation, RNA splicing (in eukaryotes), mRNA transport, translation initiation, post-translational modifications, and degradation of mRNA. Proteins perform perhaps most cellular functions. Advances in microarray technology, with the use of cDNA or oligonucleotides immobilized in a predefined organization on a solid phase, have led to measurements of mRNA expression levels on a genome-wide scale (see chapter 3). The results of the measurements can be displayed on a plot on which a row represents one gene at various times, a column the whole set of genes, and the time of gene expression is plotted along the axis of rows. The changes in expression levels, as measured by fluorescence, are indicated by colors, for example green for decreased expression, black for no change in expression, and red for increased expression. Responses in expression levels have been measured for various biochemical and physiological conditions. We turn now to a few methods of obtaining information on genomic networks from microarray measurements.
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Conference papers on the topic "Cellular prion protein physiological function"

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Carruthers, Christopher A., Bryan Good, Antonio D’Amore, Rouzbeh Amini, Joseph H. Gorman, and Michael S. Sacks. "Physiological Micromechanics of the Anterior Mitral Valve Leaflet." In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53637.

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An improved understanding of mitral valve (MV) function remains an important goal for determining mechanisms underlying valve disease and for developing novel therapies. Critical to heart valve tissue homeostasis is the valvular interstitial cells (VICs), which reside in the interstitium and maintain the extracellular matrix (ECM) through both protein synthesis and enzymatic degradation [1]. There is scant experimental data on the alterations of the MV fiber network reorganization as a function of load, which is critical for implementation of computational strategies that attempt to link this meso-micro scale phenomenon. The observed large scale deformations experienced by VICs could be implicated in mechanotransduction [2], i.e., translation of mechanical stimuli into biochemical signals. Consequently, our goal is to quantitatively connect organ level loads to cellular deformation as a function of the ECM fiber network. We hypothesize that cellular deformations are likely a complex function of collagen and elastin fiber mechanical properties, architecture, and cellular coupling to these fibers.
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Tran, Phat L., Jessica R. Gamboa, Katherine E. McCracken, Jeong-Yeol Yoon, and Marvin J. Slepian. "Interaction With Nanoscale Topography: The Use of Nanowell-Trapped Charged Ligand-Bearing Nanoparticle Surfaces To Modulate Physiological Focal Adhesions in Endothelial Cells." In ASME 2013 2nd Global Congress on NanoEngineering for Medicine and Biology. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/nemb2013-93345.

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Abstract:
Achieving cell adhesion, growth and homeostasis on an underlying biomaterial surface may be a desirable feature in implant device design and tissue engineering. Insight has been gained from numerous cell patterning strategies where spatial cues and physical constraints have been shown to regulate the structure and function of cells. Despite significant advances in modifying substrates for cellular attachment, migration and proliferation, the achievement of confluent and aligned growth of functional endothelial cells on cardiovascular blood-contacting implants under physiologically significant wall shear stress has proven difficult. Recently we have reported on a method that enhances cellular adhesion under flow conditions on synthetic polymer surfaces, without reliance on pro-adhesive protein biomaterials, which are often thrombogenic. In this method we utilize electron beam lithography and size-dependent self-assembly to fabricate line arrays of nanowells allowing entrapment and retention of charged nanoparticles, covalently conjugated with a RGD adhesive ligand, GRGDSPK. This approach is an additive strategy of combining substrata topographic alteration, electrostatic charge and biochemical ligands, all uniquely incorporated as an ensemble of charged, ligand-bearing nanoparticles entrapped in arrays of nanowells. However, the modulation of endothelial cell physiologic mechanisms as a result of ensemble surface exposure remains to be characterized. In this report, we extend our studies and probe cell physiologic mechanisms altered as a result of nanofeatured surface exposure. We first examined the functional intactness or normalcy of endothelial cells adherent to the nanofeatured ensemble surface utilizing standard immunostaining and flow cytometry methods. We found β1-integrin expression dominated quiescent adherent endothelial cells while αVβ3-integrins expression was more common in migratory cells. Endothelial cells were noted to express high levels of PECAM-1 over time when exposed to nanofeatured surface and RGD peptides. For understanding the contribution of the nanofeatured surface (entrapped RGD conjugated nanoparticles) to cell adhesion, cytochalasin B was used to alter cell spreading. Confocal microscopy illustrated the uptake of nanoparticles in endothelial cells on composite surfaces, as well as the inhibition of this endocytosis by cytochalasin B. After prohibiting the cells from engulfing nanoparticles, we found an 80% reduction in cell adhesion; suggesting that an endocytic mechanism might play a role in maintaining cell adhesion. Nanofeatured ensemble surfaces appear to be good substrates for achieving a high level of EC adhesion, with maintained growth and stability.
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