Relevant bibliographies by topics / Neuroprotective proteins

Academic literature on the topic 'Neuroprotective proteins'

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Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Neuroprotective proteins"

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Zhang, Jianmin, Jia Yang, Huaishan Wang, Omar Sherbini, Matthew J. Keuss, George KE Umanah, Emily Ling-Lin Pai, et al. "The AAA + ATPase Thorase is neuroprotective against ischemic injury." Journal of Cerebral Blood Flow & Metabolism 39, no. 9 (April 16, 2018): 1836–48. http://dx.doi.org/10.1177/0271678x18769770.

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Neuronal preconditioning in vitro or in vivo with a stressful but non-lethal stimulus leads to new protein expression that mediates a profound neuroprotection against glutamate excitotoxicity and experimental stroke. The proteins that mediate neuroprotection are relatively unknown and under discovery. Here we find that the expression of the AAA + ATPase Thorase is induced by preconditioning stimulation both in vitro and in vivo. Thorase provides neuroprotection in an ATP-dependent manner against oxygen–glucose deprivation (OGD) neurotoxicity or glutamate N-Methyl-D-aspartate (NMDA) receptor-mediated excitotoxicity in vitro. Knock-down of Thorase prevents the establishment of preconditioning induced neuroprotection against OGD or NMDA neurotoxicity. Transgenic overexpression of Thorase provides neuroprotection in vivo against middle cerebral artery occlusion (MCAO)-induced stroke in mice, while genetic deletion of Thorase results in increased injury in vivo following stroke. These results define Thorase as a neuroprotective protein and understanding Thorase signaling could offer a new therapeutic strategy for the treatment of neurologic disorders.
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Puchowicz, Michelle A., Jennifer L. Zechel, Jose Valerio, Douglas S. Emancipator, Kui Xu, Svetlana Pundik, Joseph C. LaManna, and W. David Lust. "Neuroprotection in Diet-Induced Ketotic Rat Brain after Focal Ischemia." Journal of Cerebral Blood Flow & Metabolism 28, no. 12 (July 23, 2008): 1907–16. http://dx.doi.org/10.1038/jcbfm.2008.79.

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Neuroprotective properties of ketosis may be related to the upregulation of hypoxia inducible factor (HIF)-1α, a primary constituent associated with hypoxic angiogenesis and a regulator of neuroprotective responses. The rationale that the utilization of ketones by the brain results in elevation of intracellular succinate, a known inhibitor of prolyl hydroxylase (the enzyme responsible for the degradation of HIF-1α) was deemed as a potential mechanism of ketosis on the upregulation of HIF-1α. The neuroprotective effect of diet-induced ketosis (3 weeks of feeding a ketogenic diet), as pretreatment, on infarct volume, after reversible middle cerebral artery occlusion (MCAO), and the upregulation of HIF-1α were investigated. The effect of β-hydroxybutyrate (BHB), as a pretreatment, via intraventricular infusion (4 days of infusion before stroke) was also investigated following MCAO. Levels of HIF-1α and Bcl-2 (anti-apoptotic protein) proteins and succinate content were measured. A 55% or 70% reduction in infarct volume was observed with BHB infusion or diet-induced ketosis, respectively. The levels of HIF-1α and Bcl-2 proteins increased threefold with diet-induced ketosis; BHB infusions also resulted in increases in these proteins. As hypothesized, succinate content increased by 55% with diet-induced ketosis and fourfold with BHB infusion. In conclusion, the biochemical link between ketosis and the stabilization of HIF-1α is through the elevation of succinate, and both HIF-1α stabilization and Bcl-2 upregulation play a role in ketone-induced neuroprotection in the brain.
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Shen, Shichen, Ming Zhang, Min Ma, Sailee Rasam, David Poulsen, and Jun Qu. "Potential Neuroprotective Mechanisms of Methamphetamine Treatment in Traumatic Brain Injury Defined by Large-Scale IonStar-Based Quantitative Proteomics." International Journal of Molecular Sciences 22, no. 5 (February 24, 2021): 2246. http://dx.doi.org/10.3390/ijms22052246.

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Although traumatic brain injury (TBI) causes hospitalizations and mortality worldwide, there are no approved neuroprotective treatments, partly due to a poor understanding of the molecular mechanisms underlying TBI neuropathology and neuroprotection. We previously reported that the administration of low-dose methamphetamine (MA) induced significant functional/cognitive improvements following severe TBI in rats. We further demonstrated that MA mediates neuroprotection in part, via dopamine-dependent activation of the PI3K-AKT pathway. Here, we further investigated the proteomic changes within the rat cortex and hippocampus following mild TBI (TM), severe TBI (TS), or severe TBI plus MA treatment (TSm) compared to sham operated controls. We identified 402 and 801 altered proteins (APs) with high confidence in cortical and hippocampal tissues, respectively. The overall profile of APs observed in TSm rats more closely resembled those seen in TM rather than TS rats. Pathway analysis suggested beneficial roles for acute signaling through IL-6, TGFβ, and IL-1β. Moreover, changes in fibrinogen levels observed in TSm rats suggested a potential role for these proteins in reducing/preventing TBI-induced coagulopathies. These data facilitate further investigations to identify specific pathways and proteins that may serve as key targets for the development of neuroprotective therapies.
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Chan, Elaine W. L., Emilia T. Y. Yeo, Kelly W. L. Wong, Mun L. See, Ka Y. Wong, Jeremy K. Y. Yap, and Sook Y. Gan. "Piper sarmentosum Roxb. Attenuates Beta Amyloid (Aβ)-Induced Neurotoxicity Via the Inhibition of Amyloidogenesis and Tau Hyperphosphorylation in SH-SY5Y Cells." Current Alzheimer Research 18, no. 1 (April 28, 2021): 80–87. http://dx.doi.org/10.2174/1567205018666210324124239.

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Background: In Alzheimer’s disease, accumulation of beta amyloid (Aβ) triggers amyloidogenesis and hyperphosphorylation of tau protein leading to neuronal cell death. Piper sarmentosum Roxb. (PS) is a traditional medicinal herb used by Malay to treat rheumatism, headache and boost memory. It possesses various biological effects, such as anti-cholinergic, anti-inflammatory, anti-oxidant and anti-depressant-like effects. Objective: The present study aimed to investigate neuroprotective properties of PS against Aβ-induced neurotoxicity and to evaluate its potential mechanism of action. Methods: Neuroprotective effects of hexane (HXN), dichloromethane (DCM), ethyl acetate (EA) and methanol (MEOH) extracts from leaves (L) and roots (R) of PS against Aβ-induced neurotoxicity were investigated in SH-SY5Y human neuroblastoma cells. Cells were pre-treated with PS for 24 h followed by 24 h of induction with Aβ. The neuroprotective effects of PS were studied using cell viability and cellular reactive oxygen species (ROS) assays. The levels of extracellular Aβ and tau proteins phosphorylated at threonine 231 (pT231) were determined. Gene and protein expressions were assessed using qRT-PCR analyses and western blot analyses, respectively. Results: Hexane extracts of PS (LHXN and RHXN) protected SH-SY5Y cells against Aβ-induced neurotoxicity, and decreased levels of extracellular Aβ and phosphorylated tau (pT231). Although extracts of PS inhibited Aβ-induced ROS production, it was unlikely that neuroprotective effects were simply due to the anti-oxidant capacity of PS. Further, mechanistic study suggested that the neuroprotective effects of PS might be due to its capability to regulate amyloidogenesis through the downregulation of BACE and APP. Conclusion: These findings suggest that hexane extracts of PS confer neuroprotection against Aβ- induced neurotoxicity in SH-SY5Y cells by attenuating amyloidogenesis and tau hyperphosphorylation. Due to its neuroprotective properties, PS might be a potential therapeutic agent for Alzheimer’s disease.
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Kim, Jong Youl, Sumit Barua, Mei Ying Huang, Joohyun Park, Midori A. Yenari, and Jong Eun Lee. "Heat Shock Protein 70 (HSP70) Induction: Chaperonotherapy for Neuroprotection after Brain Injury." Cells 9, no. 9 (September 2, 2020): 2020. http://dx.doi.org/10.3390/cells9092020.

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The 70 kDa heat shock protein (HSP70) is a stress-inducible protein that has been shown to protect the brain from various nervous system injuries. It allows cells to withstand potentially lethal insults through its chaperone functions. Its chaperone properties can assist in protein folding and prevent protein aggregation following several of these insults. Although its neuroprotective properties have been largely attributed to its chaperone functions, HSP70 may interact directly with proteins involved in cell death and inflammatory pathways following injury. Through the use of mutant animal models, gene transfer, or heat stress, a number of studies have now reported positive outcomes of HSP70 induction. However, these approaches are not practical for clinical translation. Thus, pharmaceutical compounds that can induce HSP70, mostly by inhibiting HSP90, have been investigated as potential therapies to mitigate neurological disease and lead to neuroprotection. This review summarizes the neuroprotective mechanisms of HSP70 and discusses potential ways in which this endogenous therapeutic molecule could be practically induced by pharmacological means to ultimately improve neurological outcomes in acute neurological disease.
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Hawkins, Liam J., Hanane Hadj-Moussa, Vu C. Nguyen, Matthew E. Pamenter, and Kenneth B. Storey. "Naked mole rats activate neuroprotective proteins during hypoxia." Journal of Experimental Zoology Part A: Ecological and Integrative Physiology 331, no. 10 (September 23, 2019): 571–76. http://dx.doi.org/10.1002/jez.2321.

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Gozes, Illana. "The cytoskeleton as a drug target for neuroprotection: the case of the autism- mutated ADNP." Biological Chemistry 397, no. 3 (March 1, 2016): 177–84. http://dx.doi.org/10.1515/hsz-2015-0152.

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Abstract Fifteen years ago we discovered activity-dependent neuroprotective protein (ADNP), and showed that it is essential for brain formation/function. Our protein interaction studies identified ADNP as a member of the chromatin remodeling complex, SWI/SNF also associated with alternative splicing of tau and prediction of tauopathy. Recently, we have identified cytoplasmic ADNP interactions with the autophagy regulating microtubule-associated protein 1 light chain 3 (LC3) and with microtubule end-binding (EB) proteins. The ADNP-EB-binding SIP domain is shared with the ADNP snippet drug candidate, NAPVSIPQ termed NAP (davunetide). Thus, we identified a precise target for ADNP/NAP (davunetide) neuroprotection toward improved drug development.
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Bayliss, Jacqueline A., and Zane B. Andrews. "Ghrelin is neuroprotective in Parkinson’s disease: molecular mechanisms of metabolic neuroprotection." Therapeutic Advances in Endocrinology and Metabolism 4, no. 1 (February 2013): 25–36. http://dx.doi.org/10.1177/2042018813479645.

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Ghrelin is a circulating orexigenic signal that rises with prolonged fasting and falls postprandially. Ghrelin regulates energy homeostasis by stimulating appetite and body weight; however, it also has many nonmetabolic functions including enhanced learning and memory, anxiolytic effects as well as being neuroprotective. In Parkinson’s disease, ghrelin enhances dopaminergic survival via reduced microglial and caspase activation and improved mitochondrial function. As mitochondrial dysfunction contributes to Parkinson’s disease, any agent that enhances mitochondrial function could be a potential therapeutic target. We propose that ghrelin provides neuroprotective effects via AMPK (5′ adenosine monophosphate-activated protein kinase) activation and enhanced mitophagy (removal of damaged mitochondria) to ultimately enhance mitochondrial bioenergetics. AMPK activation shifts energy balance from a negative to a neutral state and has a role in regulating mitochondrial biogenesis and reducing reactive oxygen species production. Mitophagy is important in Parkinson’s disease because damaged mitochondria produce reactive oxygen species resulting in damage to intracellular proteins, lipids and DNA predisposing them to neurodegeneration. Many genetic mutations linked to Parkinson’s disease are due to abnormal mitochondrial function and mitophagy, for example LRRK2, PINK1 and Parkin. An interaction between ghrelin and these classic Parkinson’s disease markers has not been observed, however by enhancing mitochondrial function, ghrelin or AMPK is a potential therapeutic target for slowing the progression of Parkinson’s disease symptoms, both motor and nonmotor.
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Logsdon, Aric F., Michelle A. Erickson, Xiaodi Chen, Joseph Qiu, Yow-Pin Lim, Barbara S. Stonestreet, and William A. Banks. "Inter-alpha inhibitor proteins attenuate lipopolysaccharide-induced blood–brain barrier disruption and downregulate circulating interleukin 6 in mice." Journal of Cerebral Blood Flow & Metabolism 40, no. 5 (June 24, 2019): 1090–102. http://dx.doi.org/10.1177/0271678x19859465.

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Circulating levels of inter-alpha inhibitor proteins change dramatically in acute inflammatory disorders, which suggest an important contribution to the immunomodulatory system. Human blood-derived inter-alpha inhibitor proteins are neuroprotective and improve survival of neonatal mice exposed to lipopolysaccharide. Lipopolysaccharide augments inflammatory conditions and disrupts the blood–brain barrier. There is a paucity of therapeutic strategies to treat blood–brain barrier dysfunction, and the neuroprotective effects of human blood-derived inter-alpha inhibitor proteins are not fully understood. To examine the therapeutic potential of inter-alpha inhibitor proteins, we administered human blood-derived inter-alpha inhibitor proteins to male and female CD-1 mice after lipopolysaccharide exposure and quantified blood–brain barrier permeability of intravenously injected14C-sucrose and99mTc-albumin. We hypothesized that human blood-derived inter-alpha inhibitor protein treatment would attenuate lipopolysaccharide-induced blood–brain barrier disruption and associated inflammation. Lipopolysaccharide increased blood–brain barrier permeability to both14C-sucrose and99mTc-albumin, but human blood-derived inter-alpha inhibitor protein treatment only attenuated increases in14C-sucrose blood–brain barrier permeability in male mice. Lipopolysaccharide stimulated a more robust elevation of male serum inter-alpha inhibitor protein concentration compared to the elevation measured in female serum. Lipopolysaccharide administration also increased multiple inflammatory factors in serum and brain tissue, including interleukin 6. Human blood-derived inter-alpha inhibitor protein treatment downregulated serum interleukin 6 levels, which were inversely correlated with serum inter-alpha inhibitor protein concentration. We conclude that inter-alpha inhibitor proteins may be neuroprotective through mechanisms of blood–brain barrier disruption associated with systemic inflammation.
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Snider, B. Joy. "Neuroprotective Mechanisms of Heat Shock Gene Expression." Neuroscientist 4, no. 4 (July 1998): 236–39. http://dx.doi.org/10.1177/107385849800400412.

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Heat shock proteins were initially described as the predominant proteins expressed immediately after a thermal stress. These ubiquitously expressed proteins function as molecular chaperones; they aid in the folding, subcellular translocation, and assembly of other proteins. Although most of these proteins are expressed constitutively, enhanced expression, induced by stress or genetic manipulations, can reduce subsequent cellular injury in many cell types, including neurons and glia. Further understanding of how the expression of these proteins is controlled in the nervous system, and how they can be manipulated to attenuate injury, could provide therapeutic targets for cerebral ischemia and neurodegenerative disorders.
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Dissertations / Theses on the topic "Neuroprotective proteins"

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Wagstaff, Marcus James Dermot. "The neuroprotective effect of the heat shock proteins." Thesis, University College London (University of London), 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.267150.

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Aron, Badin Romina. "Neuroprotective effects of heat shock proteins in experimental ischaemia : an MRI study." Thesis, University College London (University of London), 2006. http://discovery.ucl.ac.uk/1444501/.

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Heat shock proteins (HSPs) are molecular chaperones with essential roles in cellular function such as modulating the proteolytic machinery and accelerating cell repair. HSP overexpression has been observed in vitro and in vivo under stresses including heat, nutrient deprivation and ischaemia. Experiments in in vivo models of stroke indicate that transgenically overexpressed or virally delivered HSPs can enhance cell survival but cannot always reduce lesion size. This study aims to assess the protective effects of HSPs in a rat model of reversible focal cerebral ischaemia using magnetic resonance imaging (MRI) techniques to measure cerebral blood flow and lesion size. The experiments described used three different herpes simplex virus (HSV) constructs: two potentially therapeutic vectors, HSV-HSP27 and HSV-HSP70, and an HSV-LacZ control vector. Initially, the localization and duration of expression from the viral vector used to deliver the HSP genes into the rat brain was assessed. Subsequently, the effect of pre-ischaemic intra-striatal microinjections of HSV-HSP27 and HSV-HSP70 was evaluated in a middle cerebral artery occlusion (MCAO) model of stroke. Finally, the effect of delivering the same HSPs 30 minutes after ischaemia was assessed. Behavioural tests were carried out in the latter study up to a month after MCAO in order to determine whether HSP treatment induced functional recovery as well as reduction in lesion size. Results suggest that intracerebral microinjections with HSV-HSP27 have a neuroprotective effect pre- and [?] ischaemia. Multislice T2-weighted images show that HSP27 treatment results in a significant reduction in lesion size after MCAO, whereas HSP70 treatment does not affect lesion size compared to controls. Western blots confirm that virally-induced overexpression of both HSP27 and HSP70 is achieved in treated animals. For the first time, non-invasive MRI techniques were used to demonstrate the neuroprotective effect of HSP27 and not HSP70 in a rat model of reversible focal cerebral ischaemia.
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Avery, Michelle A. "Axon Death Prevented: Wlds and Other Neuroprotective Molecules: A Dissertation." eScholarship@UMMS, 2010. https://escholarship.umassmed.edu/gsbs_diss/520.

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A common feature of many neuropathies is axon degeneration. While the reasons for degeneration differ greatly, the process of degeneration itself is similar in most cases. Axon degeneration after axotomy is termed ‘Wallerian degeneration,’ whereby injured axons rapidly fragment and disappear after a short period of latency (Waller, 1850). Wallerian degeneration was thought to be a passive process until the discovery of the Wallerian degeneration slow (Wlds) mouse mutant. In these mice, axons survive and function for weeks after nerve transection. Furthermore, when the full-length protein is inserted into mouse models of disease with an axon degeneration phenotype (such as progressive motor neuronopathy), Wlds is able to delay disease onset (for a review, see Coleman, 2005). Wlds has been cloned and was found to be a fusion event of two neighboring genes: Ube4b, which encodes an ubiquitinating enzyme, and NMNAT-1 (nicotinamide mononucleotide adenylyltransferase-1), which encodes a key factor in NAD (nicotinamide adenine dinucleotide) biosynthesis, joined by a 54 nucleotide linker span (Mack et al., 2001). To address the role of Wlds domains in axon protection and to characterize the subcellular localization of Wlds in neurons, our lab developed a novel method to study Wallerian degeneration in Drosophila in vivo (MacDonald et al., 2006). Using this method, we have discovered that mouse Wlds can also protect Drosophila axons for weeks after acute injury, indicating that the molecular mechanisms of Wallerian degeneration are well conserved between mouse and Drosophila. This observation allows us to use an easily manipulated genetic model to move the Wlds field forward; we can readily identify what Wlds domains give the greatest protection after injury and where in the neuron protection occurs. In chapter two of this thesis, I identify the minimal domains of Wlds that are needed for protection of severed Drosophila axons: the first 16 amino acids of Ube4b fused to Nmnat1. Although Nmnat1 and Wlds are nuclear proteins, we find evidence of a non-nuclear role in axonal protection in that a mitochondrial protein, Nmnat3, protects axons as well as Wlds. In chapter 3, I further explore a role for mitochondria in Wlds-mediated severed axon protection and find the first cell biological changes seen in a Wlds-expressing neuron. The mitochondria of Wlds- and Nmnat3-expressing neurons are more motile before injury. We find this motility is necessary for protection as suppressing the motility with miro heterozygous alleles suppresses Wldsmediated axon protection. We also find that Wlds- and Nmnat3- expressing neurons show a decrease in calcium fluorescent reporter, gCaMP3, signal after axotomy. We propose a model whereby Wlds, through production of NAD in the mitochondria, leads to an increase in calcium buffering capacity, which would decrease the amount of calcium in the cytosol, allowing for more motile mitochondria. In the case of injury, the high calcium signal is buffered more quickly and so cannot signal for the axon to die. Finally, in chapter 4 of my thesis, I identify a gene in an EMS-based forward genetic screen which can suppress Wallerian degeneration. This mutant is a loss of function, which, for the first time, definitively demonstrates that Wallerian degeneration is an active process. The mammalian homologue of the gene encodes a mitochondrial protein, which in light of the rest of the work in this thesis, highlights the importance of mitochondria in neuronal health and disease. In conclusion, the work presented in this thesis highlights a role for mitochondria in both Wlds-mediated axon protection and Wallerian degeneration itself. I identified the first cell biological changes seen in Wlds-expressing neurons and show that at least one of these is necessary for its protection of severed axons. I also helped find the first Wallerian degeneration loss-of-function mutant, showing Wallerian degeneration is an active process, mediated by a molecularly distinct axonal degeneration pathway. The future of the axon degeneration field should focus on the mitochondria as a potential therapeutic target.
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Boulos, Sherif. "Identification and characterisation of potential neuroprotective proteins induced by erythropoietin (EPO) preconditioning of cortical neuronal cultures." University of Western Australia. School of Biomedical and Chemical Sciences, 2008. http://theses.library.uwa.edu.au/adt-WU2008.0128.

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[Truncated abstract] Clinical therapeutic agents to directly inhibit ischaemic neuronal death are presently unavailable. One approach to developing therapeutics is based upon the identification of proteins up-regulated by 'preconditioning', a natural adaptive response utilised by the neural cells to counter damaging insults, such as ischaemia. Thus, my project aimed to firstly identify proteins differentially expressed following erythropoietin (EPO) mediated neuronal preconditioning and secondly to assess whether any of these proteins possessed neuroprotective activity using in vitro ischaemia like models. To achieve the first aim, it was shown that in vitro neuronal EPO preconditioning could: (i) induce cell signal changes in neuronal cultures, (ii) protect neurons against in vitro ischaemia and (iii) induce differential protein expression. Overall, 40 differentially expressed proteins were identified in cortical neuronal cultures following EPO preconditioning. In order to investigate the neuroprotective or neurodamaging activity of proteins induced by EPO preconditioning I developed an adenoviral expression system for use in neuronal cultures. To this end, I assessed the suitability of four promoters (cytomegalovirus [CMV], rous sarcoma virus [RSV], human synapsin 1 [hSYN1], rat synapsin 1 [rSYN1]) previously used to express proteins in neuronal cultures and demonstrated the superiority of the RSV promoter for this purpose. ... Finally, in order to validate this adenoviral expression system, I over-expressed the anti-apoptotic protein Bcl-XL in neuronal cultures and subsequently confirmed its neuroprotective activity in the in vitro ischaemia and oxidative stress models used in my project. Using this adenoviral vector system and the in vitro oxidative stress model I assessed a number of proteins up-regulated by EPO preconditioning. The results of this preliminary study indicated that cyclophilin A (CyPA), peroxiredoxin 2 (PRDX2) and superoxide dismutase 1 (SOD1) over-expression were neuroprotective. It was subsequently verified that adenoviral mediated over-expression of CyPA and PRDX2, v but not SOD1 in cortical neuronal cultures could protect neurons from in vitro ischaemia. I also confirmed that CyPA mRNA increased in the rat hippocampus in response to 3 minutes of global cerebral ischaemia. Interestingly, an increase in CyPA, PRDX2 or SOD1 protein was not observed in the same experimental paradigm. To investigate CyPA's mode of action I confirmed that cultured neurons, but not astrocytes, express the CyPA receptor, CD147. It was also demonstrated that administration of exogenous CyPA protein to neuronal cultures could protect neurons against oxidative and ischaemic injury. I further demonstrated that exogenous administration of CyPA induces a rapid and transient activation of the extracellular signal-regulated kinase (ERK) 1/2 pathway in neuronal cultures. From this observation, I have proposed that the extracellular mediated neuroprotective activity of CyPA occurs via CD147 receptor signalling and activation of ERK1/2 pro-survival pathways. Based on the findings reported in this thesis, the neuroprotective activities of PRDX2 and CyPA warrant further investigation as targets for the development of new therapies to treat cerebral ischaemia.
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Lee, Christopher James. "Neuroprotective effects of overexpression of the inhibitor of apoptosis proteins in the quinolinic acid model of excitotoxic injury." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2000. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape4/PQDD_0020/MQ48164.pdf.

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Aboonq, Moutasem Salih. "Activity dependent neuroprotective protein (ADNP) expression and functions." Thesis, University of Liverpool, 2010. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.540017.

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Lin, Tse-Shen. "Prion protein topologies and the effect on its neuroprotective function." Thesis, McGill University, 2008. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=18773.

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The normal prion protein (PrP) is ubiquitously expressed and is especially abundant in the brain. However, the major physiological function of PrP has remained elusive. Recently, it was demonstrated that PrP prevents Bcl-2 associated protein X (Bax)-mediated cell death by inhibiting the initial Bax conformational change that converts cytosolic Bax into a pro-apoptotic protein (Roucou et al., 2005). To further determine the form and subcellular location of PrP with anti-Bax function, we co-expressed various Syrian hamster PrP (SHaPrP) mutants that favor specific PrP topologies and subcellular localization with N-terminally green fluorescent protein tagged pro-apoptotic Bax (EGFP-Bax) in MCF-7 cells and primary human neurons. The PrP mutants that synthesize transmembrane PrP lose their anti-Bax function, whereas those that exclusively synthesize secreted or cytosolic PrP (CyPrP) retain protection comparable to that of wild type PrP in both cell types. Furthermore, co-expression of CyPrP with these mutants rescues the anti-Bax function. Addition of extracellular PrP supports only minimally the anti-Bax function. Therefore, the results indicate that the CyPrP is the predominant form of PrP with anti-Bax function. We have previously excluded the need for other Bcl-2 family members in the anti-Bax function of PrP. Here, we also fail to co-immunoprecipitate PrP and Bax indicating that PrP's anti-Bax function is not through a direct PrP-Bax interaction in the cytosol. We conclude that there must exist a cytosolic Bax interactor through which PrP exerts its effect.
La forme normale du prion (PrP) est exprimée de façon omniprésente mais elle est particulièrement abondante dans le cerveau. Cependant, la fonction physiologique principale du PrP reste indéfinie. Récemment, il a été démontré que PrP empêche la mort cellulaire causée par Bax (Bcl-2-associated protein X) en inhibant le changement de conformation initial de Bax, à partir duquel le Bax cytosolique est converti en protéine pro-apoptotique (Roucou et al., 2005). Afin de mieux déterminer la forme et la localisation sous-cellulaire de PrP ayant une fonction anti-Bax, nous avons co-exprimé divers mutants de PrP du hamster syrien (SHaPrP), lesquels favorisent des topologies et des localisations sous-cellulaires spécifiques de PrP, avec la construction pro-apoptotique Bax marquée à son bout N-terminal par la protéine fluorescente verte (EGFP-Bax), et ce, dans la lignée cellulaire MCF-7 et dans les neurones humaines primaires. Les mutants PrP qui favorisent les formes transmembranaire de PrP perdent leur fonction anti-Bax, tandis que ceux qui produisent exclusivement du PrP sécrété ou cytosolique (CyPrP) retiennent une protection comparable à celle du PrP sauvage retrouvée dans les deux types de cellules. De plus, la co-expression de CyPrP avec ces mutants récupère la fonction anti-Bax. L'ajout du PrP extracellulaire ne soutient que de façon minimale la fonction anti-Bax. Par conséquent, ces résultats indiquent que le CyPrP est la forme prédominante de PrP possédant une fonction anti-Bax. Nous avons exclut précédemment la nécessité de présence de d'autres membres de la famille Bcl-2 dans la fonction anti-Bax. Ici, nous n'avons pas pu co-immunoprécipiter PrP et Bax, ce qui indique que la fonction anti-Bax du PrP ne peut être pas attribuée à une interaction directe entre PrP et Bax, dans le cytosol. Nous concluons donc que PrP exercerait son effet sur Bax via un interagisseur cytosolique.
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Johnson, Erik Andrew. "Survivin expression after traumatic brain injury potential roles in neuroprotection /." [Gainesville, Fla.] : University of Florida, 2004. http://purl.fcla.edu/fcla/etd/UFE0008337.

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Thesis (Ph.D.)--University of Florida, 2004.
Typescript. Title from title page of source document. Document formatted into pages; contains 87 pages. Includes Vita. Includes bibliographical references.
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Gustafsson, Helena. "Uncoupling Proteins : Regulation by IGF-1 and Neuroprotection during Hyperglycemia in Vitro." Doctoral thesis, Stockholm : Institutionen för neurokemi och neurotoxikologi, Univ, 2004. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-121.

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Sakthivelu, Vignesh. "Functional characterization of Shadoo, a PrP-like protein with neuroprotective activity." Diss., lmu, 2012. http://nbn-resolving.de/urn:nbn:de:bvb:19-144326.

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Books on the topic "Neuroprotective proteins"

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Glaucoma: An open window to neurodegeneration and neuroprotection. New York: Elsevier, 2008.

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Asea, Alexzander A. A., and Ian R. Brown, eds. Heat Shock Proteins and the Brain: Implications for Neurodegenerative Diseases and Neuroprotection. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-8231-3.

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A, Asea Alexzander A., and Brown Ian R, eds. Heat shocks and the brain: Implications for neurodegenrative diseases and neuroprotection. New York: Springer, 2008.

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Bagetta, Giacinto, and Carlo Nucci. Glaucoma: A Pancitopatia of the Retina and Beyond. Elsevier, 2020.

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Bagetta, Giacinto, and Carlo Nucci. Glaucoma: A Pancitopatia of the Retina and Beyond. Elsevier, 2020.

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Hartman, Adam L. Amino Acids in the Treatment of Neurological Disorders. Edited by Dominic P. D’Agostino. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780190497996.003.0035.

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Studies of metabolism- and diet-based therapies in epilepsy and neuroprotection have focused primarily on the quality and quantity of fat supplementation or carbohydrate restriction. However, protein is another key dietary component that has not been as thoroughly studied. A number of amino acids have been shown to stop, terminate, or prevent seizures. In addition, some have been shown to exert neuroprotective effects in other neurological disorders. Amino acids (and their metabolites) may exert their effects by acting at membrane or cytoplasmic receptors, serving as substrates for membrane transporters and as modulators of signaling pathway activity. This chapter highlights examples of each of these mechanisms of action in select nervous system disorders.
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Streijger, Femke, Ward T. Plunet, and Wolfram Tetzlaff. Ketogenic Diet and Ketones for the Treatment of Traumatic Brain and Spinal Cord Injury. Edited by Jong M. Rho. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780190497996.003.0016.

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Ketogenic diets (KD)—high in fat, adequate in protein, and very low in carbohydrates—were developed almost a century ago and are still used clinically for drug-resistant epilepsy and some rare metabolic disorders. Possible new indications for cancers, diabetes, obesity, and neurodegenerative disorders are being trialed in humans based on a growing body of preclinical data showing efficacy. However the underlying mechanisms of KD remain incompletely understood. This chapter focuses on the neuroprotective effects of KD after spinal cord injury (SCI) and traumatic brain injury (TBI), and discusses possible mechanisms of action. It considers the possible role of ketone bodies as alternative fuels for mitochondrial energy utilization and the actions of ketones outside the mitochondria as agonists of antioxidant and anti-inflammatory pathways. It places these into context with the known pathophysiology of SCI and TBI, and discusses possible roles of KD and ketone bodies for their treatment.
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Book chapters on the topic "Neuroprotective proteins"

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Howarth, Joanna, Do-Young Lee, and James B. Uney. "Use of Viral Gene Delivery Systems to Investigate the Neuroprotective Roles of Hsp70 and Hsp40 Proteins." In Heat Shock Proteins and the Brain: Implications for Neurodegenerative Diseases and Neuroprotection, 223–37. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-8231-3_11.

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Kwiecien, Jacek M., Jordan R. Yaron, Kathleen H. Delaney, and Alexandra R. Lucas. "Neurologic and Histologic Tests Used to Measure Neuroprotective Effectiveness of Virus-Derived Immune-Modulating Proteins." In Methods in Molecular Biology, 227–39. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-1012-1_13.

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Russelakis-Carneiro, Milene, Claudio Hetz, Joaquin Castilla, and Claudio Soto. "Protein Misfolding." In Neuroprotection, 213–27. Weinheim, FRG: Wiley-VCH Verlag GmbH & Co. KGaA, 2005. http://dx.doi.org/10.1002/3527603867.ch11.

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Furukawa, Katsutoshi. "Signaling by β-Amyloid Precursor Protein." In Neuroprotective Signal Transduction, 197–220. Totowa, NJ: Humana Press, 1998. http://dx.doi.org/10.1007/978-1-59259-475-7_11.

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Yenari, Midori A. "Heat Shock Proteins and Neuroprotection." In Advances in Experimental Medicine and Biology, 281–99. Boston, MA: Springer US, 2003. http://dx.doi.org/10.1007/978-1-4615-0123-7_10.

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Magrané, Jordi, and Henry W. Querfurth. "Heat Shock Proteins, Unfolded Protein Response Chaperones and Alzheimer’s Disease." In Heat Shock Proteins and the Brain: Implications for Neurodegenerative Diseases and Neuroprotection, 25–50. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-8231-3_2.

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Banerjee, Rona. "Effect of Polyphenols on Protein Misfolding." In Neuroprotective Effects of Phytochemicals in Neurological Disorders, 501–13. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2017. http://dx.doi.org/10.1002/9781119155195.ch26.

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Tóth, Melinda E., Miklós Sántha, Botond Penke, and László Vígh. "How to Stabilize Both the Proteins and the Membranes: Diverse Effects of sHsps in Neuroprotection." In Heat Shock Proteins, 527–62. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-16077-1_23.

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Kim, Jong Youl, Meiying Huang, Jong Eun Lee, and Midori A. Yenari. "Role of Heat Shock Proteins (HSP) in Neuroprotection for Ischemic Stroke." In Heat Shock Proteins in Neuroscience, 69–82. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-24285-5_6.

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Resenberger, Ulrike K., Konstanze F. Winklhofer, and Jörg Tatzelt. "Neuroprotective and Neurotoxic Signaling by the Prion Protein." In Topics in Current Chemistry, 101–19. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/128_2011_160.

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Conference papers on the topic "Neuroprotective proteins"

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Šulák, Ondřej, Miroslava Spanilá, Dagmar Gajdošová, Jiří Pazourek, and Josef Havel. "Minimization of adsorption in capillary zone electrophoresis of proteins and neuroprotective peptides." In IXth Conference Biologically Active Peptides. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2005. http://dx.doi.org/10.1135/css200508087.

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Abdul Quadir, Mohammed, Probir Das, Shoyeb khan, Mahmoud Thaher, and Hareb Al Jabri. "Production of Phycocyanin from Marine Cyanobacteria in Open Raceway Pond." In Qatar University Annual Research Forum & Exhibition. Qatar University Press, 2020. http://dx.doi.org/10.29117/quarfe.2020.0029.

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Phycocyanin is one of the major light harvesting accessory pigment present in microalgae and cyanobacteria. This water-soluble pigment protein exhibits antioxidant, anti-inflammatory, and neuroprotective effects. Application of this pigment has also been used in dietary nutritional supplements in many food, nutraceutical, cosmetic, and biotechnology industries. In the present study phycocyanin was extracted from locally isolated marine cyanobacteria Geitlerinema sp. Geitlerinema sp. showed a higher growth during the summer perioed of 0.75 g/L and 0.54 g/L. Similarly, the maximum Phycocyanin obtained was up to 7.1% during summer period.
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Bernick, Kristin B., and Simona Socrate. "Substrate Dependence of Mechanical Response of Neurons and Astrocytes." In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53538.

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The response of neural cells to mechanical cues is a critical component of the innate neuroprotective cascade aimed at minimizing the consequences of traumatic brain injury (TBI). Reactive gliosis and the formation of glial scars around the lesion site are among the processes triggered by TBI where mechanical stimuli play a central role. It is well established that the mechanical properties of the microenvironment influence phenotype and morphology in most cell types. It has been shown that astrocytes change morphology [1] and cytoskeletal content [2] when grown on substrates of varying stiffness, and that mechanically injured astrocyte cultures show alterations in cell stiffness [3]. Accurate estimates of the mechanical properties of central nervous system (CNS) cells in their in-vivo conditions are needed to develop multiscale models of TBI. Lu et al found astrocytes to be softer than neurons under small deformations [4]. In recent studies, we investigated the response of neurons to large strains and at different loading rates in order to develop single cell models capable of simulating cell deformations in regimes relevant for TBI conditions [5]. However, these studies have been conducted on cells cultured on hard substrates, and the measured cell properties might differ from their in-vivo counterparts due to the aforementioned effects. Here, in order to investigate the effects of substrate stiffness on the cell mechanical properties, we used atomic force microscopy (AFM) and confocal imaging techniques to characterize the response of primary neurons and astrocytes cultured on polyacrylamide (PAA) gels of varying composition. The use of artificial gels minimizes confounding effects associated with biopolymer gels (both protein-based and polysaccharide-based) where specific receptor bindings may trigger additional biochemical responses [1].
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