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https://www.readbyqxmd.com/read/27738871/targeting-sumo-1ylation-contrasts-synaptic-dysfunction-in-a-mouse-model-of-alzheimer-s-disease
#1
Serena Marcelli, Elena Ficulle, Filomena Iannuzzi, Enikö Kövari, Robert Nisticò, Marco Feligioni
Synaptic dysfunction has been recognized as an early feature occurring at the onset of Alzheimer's disease (AD). Compromised neurotransmission leads over time to synaptic loss and these events correlate with the cognitive decline that progressively affects AD patients.Protein SUMOylation (Small Ubiquitin-like MOdifier) is a post-translational modification (PTM) involved in several cellular processes including synaptic transmission.We here demonstrate that cortical synaptosomes prepared from Tg2576 mice of 6 months of age show an increased SUMO-1ylation, which returns back to normal levels at 20 months although synaptic SUMOylation, at this age, resulted more sensible to KCl stimulus...
October 13, 2016: Molecular Neurobiology
https://www.readbyqxmd.com/read/27435506/a-comprehensive-compilation-of-sumo-proteomics
#2
Ivo A Hendriks, Alfred C O Vertegaal
Small ubiquitin-like modifiers (SUMOs) are essential for the regulation of several cellular processes and are potential therapeutic targets owing to their involvement in diseases such as cancer and Alzheimer disease. In the past decade, we have witnessed a rapid expansion of proteomic approaches for identifying sumoylated proteins, with recent advances in detecting site-specific sumoylation. In this Analysis, we combined all human SUMO proteomics data currently available into one cohesive database. We provide proteomic evidence for sumoylation of 3,617 proteins at 7,327 sumoylation sites, and insight into SUMO group modification by clustering the sumoylated proteins into functional networks...
September 2016: Nature Reviews. Molecular Cell Biology
https://www.readbyqxmd.com/read/27354696/psumo-cd-predicting-sumoylation-sites-in-proteins-with-covariance-discriminant-algorithm-by-incorporating-sequence-coupled-effects-into-general-pseaac
#3
Jianhua Jia, Liuxia Zhang, Zi Liu, Xuan Xiao, Kuo-Chen Chou
MOTIVATION: Sumoylation is a posttranslational modification (PTM) process, in which small ubiquitin-related modifier (SUMO) is attaching by covalent bonds to substrate protein. It is critical to many different biological processes such as replicating genome, expressing gene, localizing and stabilizing proteins; unfortunately, it is also involved with many major disorders including Alzheimer's and Parkinson's diseases. Therefore, for both basic research and drug development, it is important to identify the sumoylation sites in proteins...
June 26, 2016: Bioinformatics
https://www.readbyqxmd.com/read/27335169/ubiquitin-dependent-and-independent-roles-of-sumo-in-proteostasis
#4
Frauke Liebelt, Alfred C O Vertegaal
Cellular proteomes are continuously undergoing alterations as a result of new production of proteins, protein folding, and degradation of proteins. The proper equilibrium of these processes is known as proteostasis, implying that proteomes are in homeostasis. Stress conditions can affect proteostasis due to the accumulation of misfolded proteins as a result of overloading the degradation machinery. Proteostasis is affected in neurodegenerative diseases like Alzheimer's disease, Parkinson's disease, and multiple polyglutamine disorders including Huntington's disease...
August 1, 2016: American Journal of Physiology. Cell Physiology
https://www.readbyqxmd.com/read/27084229/polymorphisms-of-small-ubiquitin-related-modifier-genes-are-associated-with-risk-of-alzheimer-s-disease-in-korean-a-case-control-study
#5
Myung-Jin Mun, Jin-Ho Kim, Ji-Young Choi, Min-Seon Kim, Won-Cheoul Jang, Jung Jae Lee, Young Lee Eun, Shang-June Kwak, Ki Woong Kim, Seok Bum Lee
Sumoylation regulates transcription factor transactivation, protein-protein interactions, and appropriate subcellular localization of certain proteins. Previous studies have shown that sumoylation of amyloid precursor protein (APP) is associated with decreased levels of amyloid beta (Aβ) proteins, suggesting that sumoylation may play a role in the pathogenesis of Alzheimer's disease (AD). We investigated the association between polymorphisms of the SUMO genes and the risk of AD. Our study subjects consisted of 144 AD patients and 335 healthy controls without dementia...
May 15, 2016: Journal of the Neurological Sciences
https://www.readbyqxmd.com/read/26227998/battling-alzheimer-s-disease-targeting-sumoylation-mediated-pathways
#6
REVIEW
Wagner Carbolin Martins, Carla Inês Tasca, Helena Cimarosti
SUMO (small ubiquitin-like modifier) conjugation is a critically important control process in all eukaryotic cells, because it acts as a biochemical switch and regulates the function of hundreds of proteins in many different pathways. Although the diverse functional consequences and molecular targets of SUMOylation remain largely unknown, SUMOylation is becoming increasingly implicated in the pathophysiology of Alzheimer's disease (AD). Apart from the central SUMO-modified disease-associated proteins, such as amyloid precursor protein, amyloid β, and tau, SUMOylation also regulates several other processes underlying AD...
March 2016: Neurochemical Research
https://www.readbyqxmd.com/read/26149080/corrigendum-regulation-of-synaptic-plasticity-and-cognition-by-sumo-in-normal-physiology-and-alzheimer-s-disease
#7
Linda Lee, Elena Dale, Agnes Staniszewski, Hong Zhang, Faisal Saeed, Mikako Sakurai, Mauro Fa', Ian Orozco, Francesco Michelassi, Nsikan Akpan, Helaina Lehrer, Ottavio Arancio
No abstract text is available yet for this article.
2015: Scientific Reports
https://www.readbyqxmd.com/read/25448527/regulation-of-synaptic-plasticity-and-cognition-by-sumo-in-normal-physiology-and-alzheimer-s-disease
#8
Linda Lee, Elena Dale, Agnes Staniszewski, Hong Zhang, Faisal Saeed, Mikako Sakurai, Mauro Fa', Ian Orozco, Francesco Michelassi, Nsikan Akpan, Helena Lehrer, Ottavio Arancio
Learning and memory and the underlying cellular correlate, long-term synaptic plasticity, involve regulation by posttranslational modifications (PTMs). Here we demonstrate that conjugation with the small ubiquitin-like modifier (SUMO) is a novel PTM required for normal synaptic and cognitive functioning. Acute inhibition of SUMOylation impairs long-term potentiation (LTP) and hippocampal-dependent learning. Since Alzheimer's disease (AD) prominently features both synaptic and PTM dysregulation, we investigated SUMOylation under pathology induced by amyloid-β (Aβ), a primary neurotoxic molecule implicated in AD...
2014: Scientific Reports
https://www.readbyqxmd.com/read/25378699/sumoylation-at-k340-inhibits-tau-degradation-through-deregulating-its-phosphorylation-and-ubiquitination
#9
Hong-Bin Luo, Yi-Yuan Xia, Xi-Ji Shu, Zan-Chao Liu, Ye Feng, Xing-Hua Liu, Guang Yu, Gang Yin, Yan-Si Xiong, Kuan Zeng, Jun Jiang, Keqiang Ye, Xiao-Chuan Wang, Jian-Zhi Wang
Intracellular accumulation of the abnormally modified tau is hallmark pathology of Alzheimer's disease (AD), but the mechanism leading to tau aggregation is not fully characterized. Here, we studied the effects of tau SUMOylation on its phosphorylation, ubiquitination, and degradation. We show that tau SUMOylation induces tau hyperphosphorylation at multiple AD-associated sites, whereas site-specific mutagenesis of tau at K340R (the SUMOylation site) or simultaneous inhibition of tau SUMOylation by ginkgolic acid abolishes the effect of small ubiquitin-like modifier protein 1 (SUMO-1)...
November 18, 2014: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/24778618/age-related-changes-of-protein-sumoylation-balance-in-the-a%C3%AE-pp-tg2576-mouse-model-of-alzheimer-s-disease
#10
Robert Nisticò, Caterina Ferraina, Veronica Marconi, Fabio Blandini, Lucia Negri, Jan Egebjerg, Marco Feligioni
Alzheimer's disease (AD) is a complex disorder that affects the central nervous system causing a severe neurodegeneration. This pathology affects an increasing number of people worldwide due to the overall aging of the human population. In recent years SUMO protein modification has emerged as a possible cellular mechanism involved in AD. Some of the proteins engaged in the physiopathological process of AD, like BACE1, GSK3-β tau, AβPP, and JNK, are in fact subject to protein SUMO modifications or interactions...
2014: Frontiers in Pharmacology
https://www.readbyqxmd.com/read/24602872/expression-and-purification-of-the-aortic-amyloid-polypeptide-medin
#11
Hannah A Davies, Mark C Wilkinson, Robert P Gibson, David A Middleton
The 50-amino acid protein medin is the main fibrillar component of human aortic medial amyloid (AMA), the most common form of localised amyloid which affects 97% of Caucasians over the age of 50. Structural models for several amyloid assemblies, including the Alzheimer's amyloid-β peptides, have been defined from solid-state nuclear magnetic resonance (SSNMR) measurements on (13)C- and (15)N-labelled protein fibrils. SSNMR-derived structural information on fibrillar medin is scant, however, because studies to date have been restricted to limited measurements on site-specifically labelled protein prepared by solid-phase synthesis...
June 2014: Protein Expression and Purification
https://www.readbyqxmd.com/read/23979993/sumo-and-alzheimer-s-disease
#12
REVIEW
Linda Lee, Mikako Sakurai, Shinsuke Matsuzaki, Ottavio Arancio, Paul Fraser
Alzheimer's disease (AD) is a neurodegenerative disorder characterized by progressive cognitive decline and is the most common cause of dementia in the elderly. Histopathologically, AD features insoluble aggregates of two proteins in the brain, amyloid-β (Aβ) and the microtubule-associated protein tau, both of which have been linked to the small ubiquitin-like modifier (SUMO). A large body of research has elucidated many of the molecular and cellular pathways that underlie AD, including those involving the abnormal Aβ and tau aggregates...
December 2013: Neuromolecular Medicine
https://www.readbyqxmd.com/read/23788181/-potential-involvement-of-abnormal-increased-sumo-1-in-modulation-of-the-formation-of-alzheimer-s-disease-senile-plaques-and-neuritic-dystrophy-in-app-ps1-transgenic-mice
#13
Xiao-Yan Zhao, Dan-Dan Wang, Ye Shan, Cui-Qing Zhu
Small ubiquitin-related modifiers (SUMOs) belong to an important class of ubiquitin like proteins. SUMOylation is a post-translational modification process that regulates the functional properties of many proteins, among which are several proteins implicated in neurodegenerative diseases. This study was aimed to investigate the changes of SUMO-1 expression and modification, and the relationship between SUMO-1 and Alzheimer's disease (AD) pathology in APP/PS1 transgenic AD mice. Using Western blot, co-immunoprecipitation and immunofluorescent staining methods, the SUMO-1 expression and modification and its relation to tau, amyloid precursor protein (APP) and β-amyloid protein (Aβ) in the 12-month-old APP/PS1 transgenic AD mice were analyzed...
June 25, 2013: Sheng Li Xue Bao: [Acta Physiologica Sinica]
https://www.readbyqxmd.com/read/23651519/sumo-1-conjugation-blocks-beta-amyloid-induced-astrocyte-reactivity
#14
Juliana B Hoppe, Marcus Rattray, Henry Tu, Christianne G Salbego, Helena Cimarosti
Astrocyte reactivity is implicated in the neuronal loss underlying Alzheimer's disease. Curcumin has been shown to reduce astrocyte reactivity, though the exact pathways underlying these effects are incompletely understood. Here we investigated the role of the small ubiquitin-like modifier (SUMO) conjugation in mediating this effect of curcumin. In beta-amyloid (Aβ)-treated astrocytes, morphological changes and increased glial fibrillary acidic protein (GFAP) confirmed reactivity, which was accompanied by c-jun N-terminal kinase activation...
June 24, 2013: Neuroscience Letters
https://www.readbyqxmd.com/read/23339020/the-ubiquitin-proteasome-system-in-retinal-health-and-disease
#15
REVIEW
Laura Campello, Julián Esteve-Rudd, Nicolás Cuenca, José Martín-Nieto
The ubiquitin-proteasome system (UPS) is the main intracellular pathway for modulated protein turnover, playing an important role in the maintenance of cellular homeostasis. It also exerts a protein quality control through degradation of oxidized, mutant, denatured, or misfolded proteins and is involved in many biological processes where protein level regulation is necessary. This system allows the cell to modulate its protein expression pattern in response to changing physiological conditions and provides a critical protective role in health and disease...
April 2013: Molecular Neurobiology
https://www.readbyqxmd.com/read/23185553/the-proteome-response-to-amyloid-protein-expression-in-vivo
#16
Ricardo A Gomes, Catarina Franco, Gonçalo Da Costa, Sébastien Planchon, Jenny Renaut, Raquel M Ribeiro, Francisco Pinto, Marta Sousa Silva, Ana Varela Coelho, Ana Ponces Freire, Carlos Cordeiro
Protein misfolding disorders such as Alzheimer, Parkinson and transthyretin amyloidosis are characterized by the formation of protein amyloid deposits. Although the nature and location of the aggregated proteins varies between different diseases, they all share similar molecular pathways of protein unfolding, aggregation and amyloid deposition. Most effects of these proteins are likely to occur at the proteome level, a virtually unexplored reality. To investigate the effects of an amyloid protein expression on the cellular proteome, we created a yeast expression system using human transthyretin (TTR) as a model amyloidogenic protein...
2012: PloS One
https://www.readbyqxmd.com/read/23022145/withdrawn-protein-sumoylation-and-human-diseases
#17
Kevin D Sarge, Ok-Kyong Park-Sarge
This review has been withdrawn at the request of the author(s) and/or editor. The Publisher apologizes for any inconvenience this may cause. The full Elsevier Policy on Article Withdrawal can be found at http://www.elsevier.com/locate/withdrawalpolicy.
September 26, 2012: Biochimie
https://www.readbyqxmd.com/read/22975420/sumo1-modulates-a%C3%AE-generation-via-bace1-accumulation
#18
Sang-Moon Yun, Sun-Jung Cho, Jae Chun Song, Sung Yeon Song, Sangmee Ahn Jo, Chulman Jo, Keejung Yoon, Rudolph E Tanzi, Eui-Ju Choi, Young Ho Koh
Accumulation of disease-related proteins is a characteristic event observed in the pathogenesis of neurodegenerative diseases. β-secretase (BACE)-1, which initiates generation of β-amyloid (Aβ), is increased in the Alzheimer's diseased brain. However, the mechanisms of BACE1 accumulation in Alzheimer's disease are largely unknown. In this report, we found that small ubiquitin-like modifier (SUMO)-1 interacts with the dileucine motif of BACE1 and regulates the level of BACE1 protein. This was proved by the coimmunoprecipitation, and gain or loss of function experiments...
March 2013: Neurobiology of Aging
https://www.readbyqxmd.com/read/22700804/differential-expression-and-cellular-localization-of-novel-isoforms-of-the-tendon-biomarker-tenomodulin
#19
J Qi, J M Dmochowski, A N Banes, M Tsuzaki, D Bynum, M Patterson, A Creighton, S Gomez, K Tech, A Cederlund, A J Banes
Tenomodulin (Tnmd, also called Tendin) is classified as a type II transmembrane glycoprotein and is highly expressed in developing as well as in mature tendons. Along with scleraxis (scx), Tnmd is a candidate marker gene for tenocytes. Its function is unknown, but it has been reported to have anti-angiogenic properties. Results in a knockout mouse model did not substantiate that claim. It has homology to chondromodulin-I. Single nucleotide polymorphisms of TNMD have been associated with obesity, macular degeneration, and Alzheimer's disease in patients...
September 2012: Journal of Applied Physiology
https://www.readbyqxmd.com/read/22197912/generating-recombinant-c-terminal-prion-protein-fragments-of-exact-native-sequence
#20
V A Johanssen, K J Barnham, C L Masters, A F Hill, S J Collins
Transmissibility and distinctive neuropathology are hallmark features of prion diseases differentiating them from other neurodegenerative disorders, with pathogenesis and transmission appearing closely linked to misfolded conformers (PrP(Sc)) of the ubiquitously expressed cellular form of the prion protein (PrP(C)). Given the apparent pathogenic primacy of misfolded PrP, the utilisation of peptides based on the prion protein has formed an integral approach for providing insights into misfolding pathways and pathogenic mechanisms...
February 2012: Neurochemistry International
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