Relevant bibliographies by topics / Synaptic proteins loss

Academic literature on the topic 'Synaptic proteins loss'

Author: Grafiati
Published: 10 December 2022
Last updated: 29 January 2023

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Journal articles on the topic "Synaptic proteins loss"

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Reddy, P. Hemachandra, Geethalakshmi Mani, Byung S. Park, Joline Jacques, Geoffrey Murdoch, William Whetsell, Jeffrey Kaye, and Maria Manczak. "Differential loss of synaptic proteins in Alzheimer's disease: Implications for synaptic dysfunction." Journal of Alzheimer's Disease 7, no. 2 (April 18, 2005): 103–17. http://dx.doi.org/10.3233/jad-2005-7203.

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Camporesi, Elena, Johanna Nilsson, Ann Brinkmalm, Bruno Becker, Nicholas J. Ashton, Kaj Blennow, and Henrik Zetterberg. "Fluid Biomarkers for Synaptic Dysfunction and Loss." Biomarker Insights 15 (January 2020): 117727192095031. http://dx.doi.org/10.1177/1177271920950319.

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Synapses are the site for brain communication where information is transmitted between neurons and stored for memory formation. Synaptic degeneration is a global and early pathogenic event in neurodegenerative disorders with reduced levels of pre- and postsynaptic proteins being recognized as a core feature of Alzheimer’s disease (AD) pathophysiology. Together with AD, other neurodegenerative and neurodevelopmental disorders show altered synaptic homeostasis as an important pathogenic event, and due to that, they are commonly referred to as synaptopathies. The exact mechanisms of synapse dysfunction in the different diseases are not well understood and their study would help understanding the pathogenic role of synaptic degeneration, as well as differences and commonalities among them and highlight candidate synaptic biomarkers for specific disorders. The assessment of synaptic proteins in cerebrospinal fluid (CSF), which can reflect synaptic dysfunction in patients with cognitive disorders, is a keen area of interest. Substantial research efforts are now directed toward the investigation of CSF synaptic pathology to improve the diagnosis of neurodegenerative disorders at an early stage as well as to monitor clinical progression. In this review, we will first summarize the pathological events that lead to synapse loss and then discuss the available data on established (eg, neurogranin, SNAP-25, synaptotagmin-1, GAP-43, and α-syn) and emerging (eg, synaptic vesicle glycoprotein 2A and neuronal pentraxins) CSF biomarkers for synapse dysfunction, while highlighting possible utilities, disease specificity, and technical challenges for their detection.
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Xu, Lingyan, Zhiyun Ren, Frances E. Chow, Richard Tsai, Tongzheng Liu, Flavio Rizzolio, Silvia Boffo, et al. "Pathological Role of Peptidyl-Prolyl Isomerase Pin1 in the Disruption of Synaptic Plasticity in Alzheimer’s Disease." Neural Plasticity 2017 (2017): 1–12. http://dx.doi.org/10.1155/2017/3270725.

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Synaptic loss is the structural basis for memory impairment in Alzheimer’s disease (AD). While the underlying pathological mechanism remains elusive, it is known that misfolded proteins accumulate as β-amyloid (Aβ) plaques and hyperphosphorylated Tau tangles decades before the onset of clinical disease. The loss of Pin1 facilitates the formation of these misfolded proteins in AD. Pin1 protein controls cell-cycle progression and determines the fate of proteins by the ubiquitin proteasome system. The activity of the ubiquitin proteasome system directly affects the functional and structural plasticity of the synapse. We localized Pin1 to dendritic rafts and postsynaptic density (PSD) and found the pathological loss of Pin1 within the synapses of AD brain cortical tissues. The loss of Pin1 activity may alter the ubiquitin-regulated modification of PSD proteins and decrease levels of Shank protein, resulting in aberrant synaptic structure. The loss of Pin1 activity, induced by oxidative stress, may also render neurons more susceptible to the toxicity of oligomers of Aβ and to excitation, thereby inhibiting NMDA receptor-mediated synaptic plasticity and exacerbating NMDA receptor-mediated synaptic degeneration. These results suggest that loss of Pin1 activity could lead to the loss of synaptic plasticity in the development of AD.
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Uytterhoeven, Valerie, Sabine Kuenen, Jaroslaw Kasprowicz, Katarzyna Miskiewicz, and Patrik Verstreken. "Loss of Skywalker Reveals Synaptic Endosomes as Sorting Stations for Synaptic Vesicle Proteins." Cell 145, no. 1 (April 2011): 117–32. http://dx.doi.org/10.1016/j.cell.2011.02.039.

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Gulyássy, Péter, Katalin Todorov-Völgyi, Vilmos Tóth, Balázs A. Györffy, Gina Puska, Attila Simor, Gábor Juhász, László Drahos, and Katalin Adrienna Kékesi. "The Effect of Sleep Deprivation and Subsequent Recovery Period on the Synaptic Proteome of Rat Cerebral Cortex." Molecular Neurobiology 59, no. 2 (January 5, 2022): 1301–19. http://dx.doi.org/10.1007/s12035-021-02699-x.

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AbstractSleep deprivation (SD) is commonplace in the modern way of life and has a substantial social, medical, and human cost. Sleep deprivation induces cognitive impairment such as loss of executive attention, working memory decline, poor emotion regulation, increased reaction times, and higher cognitive functions are particularly vulnerable to sleep loss. Furthermore, SD is associated with obesity, diabetes, cardiovascular diseases, cancer, and a vast majority of psychiatric and neurodegenerative disorders are accompanied by sleep disturbances. Despite the widespread scientific interest in the effect of sleep loss on synaptic function, there is a lack of investigation focusing on synaptic transmission on the proteome level. In the present study, we report the effects of SD and recovery period (RP) on the cortical synaptic proteome in rats. Synaptosomes were isolated after 8 h of SD performed by gentle handling and after 16 h of RP. The purity of synaptosome fraction was validated with western blot and electron microscopy, and the protein abundance alterations were analyzed by mass spectrometry. We observed that SD and RP have a wide impact on neurotransmitter-related proteins at both the presynaptic and postsynaptic membranes. The abundance of synaptic proteins has changed to a greater extent in consequence of SD than during RP: we identified 78 proteins with altered abundance after SD and 39 proteins after the course of RP. Levels of most of the altered proteins were upregulated during SD, while RP showed the opposite tendency, and three proteins (Gabbr1, Anks1b, and Decr1) showed abundance changes with opposite direction after SD and RP. The functional cluster analysis revealed that a majority of the altered proteins is related to signal transduction and regulation, synaptic transmission and synaptic assembly, protein and ion transport, and lipid and fatty acid metabolism, while the interaction network analysis revealed several connections between the significantly altered proteins and the molecular processes of synaptic plasticity or sleep. Our proteomic data implies suppression of SNARE-mediated synaptic vesicle exocytosis and impaired endocytic processes after sleep deprivation. Both SD and RP altered GABA neurotransmission and affected protein synthesis, several regulatory processes and signaling pathways, energy homeostatic processes, and metabolic pathways.
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Jadhav, Santosh, Veronika Cubinkova, Ivana Zimova, Veronika Brezovakova, Aladar Madari, Viera Cigankova, and Norbert Zilka. "Tau-mediated synaptic damage in Alzheimer’s disease." Translational Neuroscience 6, no. 1 (January 1, 2015): 214–26. http://dx.doi.org/10.1515/tnsci-2015-0023.

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AbstractSynapses are the principal sites for chemical communication between neurons and are essential for performing the dynamic functions of the brain. In Alzheimer’s disease and related tauopathies, synapses are exposed to disease modified protein tau, which may cause the loss of synaptic contacts that culminate in dementia. In recent decades, structural, transcriptomic and proteomic studies suggest that Alzheimer’s disease represents a synaptic disorder. Tau neurofibrillary pathology and synaptic loss correlate well with cognitive impairment in these disorders. Moreover, regional distribution and the load of neurofibrillary lesions parallel the distribution of the synaptic loss. Several transgenic models of tauopathy expressing various forms of tau protein exhibit structural synaptic deficits. The pathological tau proteins cause the dysregulation of synaptic proteome and lead to the functional abnormalities of synaptic transmission. A large body of evidence suggests that tau protein plays a key role in the synaptic impairment of human tauopathies.
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Bellucci, Arianna, Francesca Longhena, and Maria Grazia Spillantini. "The Role of Rab Proteins in Parkinson’s Disease Synaptopathy." Biomedicines 10, no. 8 (August 10, 2022): 1941. http://dx.doi.org/10.3390/biomedicines10081941.

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In patients affected by Parkinson’s disease (PD), the most common neurodegenerative movement disorder, the brain is characterized by the loss of dopaminergic neurons in the nigrostriatal system, leading to dyshomeostasis of the basal ganglia network activity that is linked to motility dysfunction. PD mostly arises as an age-associated sporadic disease, but several genetic forms also exist. Compelling evidence supports that synaptic damage and dysfunction characterize the very early phases of either sporadic or genetic forms of PD and that this early PD synaptopathy drives retrograde terminal-to-cell body degeneration, culminating in neuronal loss. The Ras-associated binding protein (Rab) family of small GTPases, which is involved in the maintenance of neuronal vesicular trafficking, synaptic architecture and function in the central nervous system, has recently emerged among the major players in PD synaptopathy. In this manuscript, we provide an overview of the main findings supporting the involvement of Rabs in either sporadic or genetic PD pathophysiology, and we highlight how Rab alterations participate in the onset of early synaptic damage and dysfunction.
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Royero, Pedro Xavier, Guilherme Shigueto Vilar Higa, Daiane Soares Kostecki, Bianca Araújo dos Santos, Cayo Almeida, Kézia Accioly Andrade, Erika Reime Kinjo, and Alexandre Hiroaki Kihara. "Ryanodine receptors drive neuronal loss and regulate synaptic proteins during epileptogenesis." Experimental Neurology 327 (May 2020): 113213. http://dx.doi.org/10.1016/j.expneurol.2020.113213.

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Desnos, C., L. Clift-O'Grady, and R. B. Kelly. "Biogenesis of synaptic vesicles in vitro." Journal of Cell Biology 130, no. 5 (September 1, 1995): 1041–49. http://dx.doi.org/10.1083/jcb.130.5.1041.

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Synaptic vesicles are synthesized at a rapid rate in nerve terminals to compensate for their rapid loss during neurotransmitter release. Their biogenesis involves endocytosis of synaptic vesicle membrane proteins from the plasma membrane and requires two steps, the segregation of synaptic vesicle membrane proteins from other cellular proteins, and the packaging of those unique proteins into vesicles of the correct size. By labeling an epitope-tagged variant of a synaptic vesicle protein, VAMP (synaptobrevin), at the cell surface of the neuroendocrine cell line PC12, synaptic vesicle biogenesis could be followed with considerable precision, quantitatively and kinetically. Epitope-tagged VAMP was recovered in synaptic vesicles within a few minutes of leaving the cell surface. More efficient targeting was obtained by using the VAMP mutant, del 61-70. Synaptic vesicles did not form at 15 degrees C although endocytosis still occurred. Synaptic vesicles could be generated in vitro from a homogenate of cells labeled at 15 degrees C. The newly formed vesicles are identical to those formed in vivo in their sedimentation characteristics, the presence of the synaptic vesicle protein synaptophysin, and the absence of detectable transferrin receptor. Brain, but not fibroblast cytosol, allows vesicles of the correct size to form. Vesicle formation is time and temperature-dependent, requires ATP, is calcium independent, and is inhibited by GTP-gamma S. Thus, two key steps in synaptic vesicle biogenesis have been reconstituted in vitro, allowing direct analysis of the proteins involved.
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Ahmad-Annuar, Azlina, Lorenza Ciani, Iordanis Simeonidis, Judit Herreros, Naila Ben Fredj, Silvana B. Rosso, Anita Hall, Stephen Brickley, and Patricia C. Salinas. "Signaling across the synapse: a role for Wnt and Dishevelled in presynaptic assembly and neurotransmitter release." Journal of Cell Biology 174, no. 1 (July 3, 2006): 127–39. http://dx.doi.org/10.1083/jcb.200511054.

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Proper dialogue between presynaptic neurons and their targets is essential for correct synaptic assembly and function. At central synapses, Wnt proteins function as retrograde signals to regulate axon remodeling and the accumulation of presynaptic proteins. Loss of Wnt7a function leads to defects in the localization of presynaptic markers and in the morphology of the presynaptic axons. We show that loss of function of Dishevelled-1 (Dvl1) mimics and enhances the Wnt7a phenotype in the cerebellum. Although active zones appear normal, electrophysiological recordings in cerebellar slices from Wnt7a/Dvl1 double mutant mice reveal a defect in neurotransmitter release at mossy fiber–granule cell synapses. Deficiency in Dvl1 decreases, whereas exposure to Wnt increases, synaptic vesicle recycling in mossy fibers. Dvl increases the number of Bassoon clusters, and like other components of the Wnt pathway, it localizes to synaptic sites. These findings demonstrate that Wnts signal across the synapse on Dvl-expressing presynaptic terminals to regulate synaptic assembly and suggest a potential novel function for Wnts in neurotransmitter release.
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Dissertations / Theses on the topic "Synaptic proteins loss"

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VanGuilder, Heather D. "Depletion of retinal synaptic proteins in experimental diabetes implications for vision loss in diabetic retinopathy /." 2008. http://etda.libraries.psu.edu/theses/approved/WorldWideIndex/ETD-2462/index.html.

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Books on the topic "Synaptic proteins loss"

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Nakamura, Tomohiro, and Stuart A. Lipton. Neurodegenerative Diseases as Protein Misfolding Disorders. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780190233563.003.0002.

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Neurodegenerative diseases (NDDs) often represent disorders of protein folding. Rather than large aggregates, recent evidence suggests that soluble oligomers of misfolded proteins are the most neurotoxic species. Emerging evidence points to small, soluble oligomers of misfolded proteins as the cause of synaptic dysfunction and loss, the major pathological correlate to disease progression in many NDDs including Alzheimer’s disease. The protein quality control machinery of the cell, which includes molecular chaperones as found in the endoplasmic reticulum (ER), the ubiquitin-proteasome system (UPS), and various forms of autophagy, can counterbalance the accumulation of misfolded proteins to some extent. Their ability to eliminate the neurotoxic effects of misfolded proteins, however, declines with age. A plausible explanation for the age-dependent deterioration of the quality control machinery involves compromise of these systems by excessive generation of reactive oxygen species (ROS), such as superoxide anion (O2-), and reactive nitrogen species (RNS), such as nitric oxide (NO). The resulting redox stress contributes to the accumulation of misfolded proteins. Here, we focus on aberrantly increased generation of NO-related species since this process appears to accelerate the manifestation of key neuropathological features, including protein misfolding. We review the chemical mechanisms of posttranslational modification by RNS such as protein S-nitrosylation of critical cysteine thiol groups and nitration of tyrosine residues, showing how they contribute to the pathogenesis of NDDs.
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Book chapters on the topic "Synaptic proteins loss"

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Callahan, Linda, and Paul D. Coleman. "Neurofibrillary Tangles are Associated with the Differential Loss of Message Expression for Synaptic Proteins in Alzheimer’s Disease." In Connections, Cognition and Alzheimer’s Disease, 53–57. Berlin, Heidelberg: Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/978-3-642-60680-9_5.

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Nakamura, Tomohiro, and Stuart A. Lipton. "Redox Regulation of Protein Misfolding, Synaptic Damage, and Neuronal Loss in Neurodegenerative Diseases." In Protein Chaperones and Protection from Neurodegenerative Diseases, 65–99. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2011. http://dx.doi.org/10.1002/9781118063903.ch2.

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Roseman, Graham P., Li Fu, and Stephen M. Strittmatter. "Prion Protein Complex with mGluR5 Mediates Amyloid-ß Synaptic Loss in Alzheimer’s Disease." In Prions and Diseases, 467–81. Cham: Springer International Publishing, 2023. http://dx.doi.org/10.1007/978-3-031-20565-1_22.

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Chaudhary, Rishabh, Mujeeba Rehman, Vipul Agarwal, Arjun Singh Kaushik, and Vikas Mishra. "Protein Aggregation in Neurodegenerative Diseases." In Neurodegenerative Diseases - Multifactorial Degenerative Processes, Biomarkers and Therapeutic Approaches (First Edition), 26–58. BENTHAM SCIENCE PUBLISHERS, 2022. http://dx.doi.org/10.2174/9789815040913122010005.

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Protein aggregation-related diseases primarily affect the central nervous system and are involved in the pathogenesis of multiple neurodegenerative diseases as well as several rare hereditary disorders that involve the deposition of protein aggregates in the brain. These diseases include Alzheimer's, Parkinson, Huntington's disease, Prion diseases, amyotrophic lateral sclerosis, familial amyloid polyneuropathy, etc. The aggregates usually consist of fibers containing misfolded protein with a betasheet conformation. As a result, proteins’ secondary structures change from α-helix to β-sheet, leading to the accumulation of harmful misfolded protein aggregates in the CNS. The misfolding, subsequent aggregation and accumulation of proteins in neurodegenerative diseases lead to cellular dysfunction, loss of synaptic connections and brain damage. This chapter discusses some of the important neurodegenerative diseases resulting from protein misfolding and explains the pathological mechanisms behind brain damage.
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Kaur, Ramneek, Harleen Kaur, Rashi Rajput, Sachin Kumar, Rachana R., and Manisha Singh. "Neurodegenerative Disorders Progression." In Advances in Medical Diagnosis, Treatment, and Care, 129–52. IGI Global, 2019. http://dx.doi.org/10.4018/978-1-5225-5282-6.ch006.

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Neurodegenerative disorders (NDs) are a diverse group of disorders characterized by selective and progressive loss of neural systems that cause dysfunction of the central nervous system (CNS). The examples of NDs include Alzheimer's disease (AD), amyotrophic lateral sclerosis (ALS), Parkinson's disease (PD), and Huntington's disease (HD). The aggregated proteins block or disrupt the normal proteosomal turnover, autophagy, and become abnormally modified with time, generating toxicity via pathways thereby resulting in neurodegeneration and neuron death. The chapter highlights the understanding in the areas of AD, PD, HD as illustrative of major research so as to define the key factors and events in the improvement of NDs. It defines the physiological functioning of neural transmission (presynaptic, postsynaptic activity) at neural signaling pathway, then the dynamics of neuronal dysfunctioning and its molecular mechanism. Further, it also discusses the progression from synaptic dysfunction to transmission failure followed by NDs.
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Bragin, Valentin, and Ilya Bragin. "An Innovative Framework for Integrative Rehabilitation in Dementia." In Alzheimer's Disease [Working Title]. IntechOpen, 2022. http://dx.doi.org/10.5772/intechopen.101863.

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Alzheimer’s disease (AD) is a progressive neurodegenerative disorder with multiple pathophysiological mechanisms affecting every organ and system in the body. Cerebral hypoperfusion, hypoxia, mitochondrial failure, abnormal protein deposition, multiple neurotransmitters and synaptic failures, white matter lesions, and inflammation, along with sensory-motor system dysfunctions, hypodynamia, sarcopenia, muscle spasticity, muscle hypoxia, digestive problems, weight loss, and immune system alterations. Rehabilitation of AD patients is an emerging concept aimed at achieving optimum levels of physical and psychological functioning in the presence of aging, neurodegenerative processes, and progression of chronic medical illnesses. We hypothesize that the simultaneous implementation of multiple rehabilitation modalities can delay the progression of mild into moderate dementia. This chapter highlights recent research related to a novel treatment model aimed at modifying the natural course of AD and delaying cognitive decline for medically ill community-dwelling patients with dementia. For practical implementation of rehabilitation in AD, the standardized treatment protocols are warranted.
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