Добірка наукової літератури з теми "APP-CTFs"
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Статті в журналах з теми "APP-CTFs":
Vaillant-Beuchot, Loan, Arnaud Mary, Raphaëlle Pardossi-Piquard, Alexandre Bourgeois, Inger Lauritzen, Fanny Eysert, Paula Fernanda Kinoshita, et al. "Accumulation of amyloid precursor protein C-terminal fragments triggers mitochondrial structure, function, and mitophagy defects in Alzheimer’s disease models and human brains." Acta Neuropathologica 141, no. 1 (October 20, 2020): 39–65. http://dx.doi.org/10.1007/s00401-020-02234-7.
Marttinen, Mikael, Catarina B. Ferreira, Kaisa M. A. Paldanius, Mari Takalo, Teemu Natunen, Petra Mäkinen, Luukas Leppänen та ін. "Presynaptic Vesicle Protein SEPTIN5 Regulates the Degradation of APP C-Terminal Fragments and the Levels of Aβ". Cells 9, № 11 (15 листопада 2020): 2482. http://dx.doi.org/10.3390/cells9112482.
Hao, Candy Yan, Michael S. Perkinton, William Wai-Lun Chan, Ho Yin Edwin Chan, Christopher C. J. Miller, and Kwok-Fai Lau. "GULP1 is a novel APP-interacting protein that alters APP processing." Biochemical Journal 436, no. 3 (May 27, 2011): 631–39. http://dx.doi.org/10.1042/bj20110145.
Sivanesan, Senthilkumar, Ravi Mundugaru, and Jayakumar Rajadas. "Possible Clues for Brain Energy Translation via Endolysosomal Trafficking of APP-CTFs in Alzheimer’s Disease." Oxidative Medicine and Cellular Longevity 2018 (October 21, 2018): 1–11. http://dx.doi.org/10.1155/2018/2764831.
Lauritzen, I., R. Pardossi-Piquard, A. Bourgeois, A. Bécot, and F. Checler. "Does Intraneuronal Accumulation of Carboxyl-terminal Fragments of the Amyloid Precursor Protein Trigger Early Neurotoxicity in Alzheimer’s Disease?" Current Alzheimer Research 16, no. 5 (May 21, 2019): 453–57. http://dx.doi.org/10.2174/1567205016666190325092841.
Wang, Bo-Jeng, Guor Mour Her, Ming-Kuan Hu, Yun-Wen Chen, Ying-Tsen Tung, Pei-Yi Wu, Wen-Ming Hsu, et al. "ErbB2 regulates autophagic flux to modulate the proteostasis of APP-CTFs in Alzheimer’s disease." Proceedings of the National Academy of Sciences 114, no. 15 (March 28, 2017): E3129—E3138. http://dx.doi.org/10.1073/pnas.1618804114.
Shinohara, Mitsuru, Naoyuki Sato, Hitomi Kurinami, Daisuke Takeuchi, Shuko Takeda, Motoko Noma, Hiromi Rakugi та Ryuichi Morishita. "Fluvastatin reduces Aβ levels in brain by upregulating APP-CTFs degradation and Aβ clearance". Neuroscience Research 65 (січень 2009): S64. http://dx.doi.org/10.1016/j.neures.2009.09.194.
Xie, Zhongcong, Yuanlin Dong, Uta Maeda, Weiming Xia та Rudolph E. Tanzi. "RNA Interference Silencing of the Adaptor Molecules ShcC and Fe65 Differentially Affect Amyloid Precursor Protein Processing and Aβ Generation". Journal of Biological Chemistry 282, № 7 (14 грудня 2006): 4318–25. http://dx.doi.org/10.1074/jbc.m609293200.
Yang, Chuanbin, Cui-Zan Cai, Ju-Xian Song, Jie-Qiong Tan, Siva Sundara Kumar Durairajan, Ashok Iyaswamy, Ming-Yue Wu, et al. "NRBF2 is involved in the autophagic degradation process of APP-CTFs in Alzheimer disease models." Autophagy 13, no. 12 (December 2, 2017): 2028–40. http://dx.doi.org/10.1080/15548627.2017.1379633.
Matsushima, Takahide, Tadashi Nakaya та Toshiharu Suzuki. "P1-155: Exclusion of phosporylated APP CTFs from membrane region rich in active γ-secretase". Alzheimer's & Dementia 5, № 4S_Part_7 (липень 2009): P223. http://dx.doi.org/10.1016/j.jalz.2009.04.161.
Дисертації з теми "APP-CTFs":
Mary, Arnaud. "Implications de la signalisation de la protéine kinase activée par l’AMP (AMPK) dans les dysfonctions mitochondriales, la pathologie amyloïde et Tau, et la neuroinflammation dans la maladie d’Alzheimer." Thesis, Université Côte d'Azur, 2022. http://theses.univ-cotedazur.fr/2022COAZ6001.
Alzheimer’s disease (AD) is the most common neurodegenerative disease in the world. Failures of candidate treatments targeting the beta amyloid (Aβ), a catabolite originating from the amyloid precursor protein (APP), highlight the multifactorial nature of this pathology. Hence, the early defects of mitochondrial structure and functions, and the neuroinflammation are implicated in AD development. Several studies describe the AMPK (AMP-activated protein kinase) as a master regulator of mitochondrial homeostasis, notably via the elimination of damaged mitochondria by mitophagy, and also of neuroinflammation. The central hypothesis of my thesis postulates that, besides the Aβ peptide, other APP catabolites, the C-terminals fragments (APP-CTFs) can contribute to mitochondrial dysfunctions and that the modulation of the AMPK could hold beneficial effects in AD.My thesis is structured into two specific objectives:Axe 1. Study of the APP-CTFs contribution to the alterations of mitochondria structure, functions, and mitophagy in AD. We have observed an accumulation of APP-CTFs in mitochondria of human neuroblastoma cells stably expressing APP with the double Swedish mutation (SH-SY5Y-APPswe), or the APP-βCTF: C99 (SH-SY5Y-C99), causing an alteration of mitochondria morphology, an increase reactive oxygen species (ROSmit) production, and a blockade of mitophagy. These toxic effects were confirmed in presymptomatic 3xTgAD mice (APPswe, TauP301L, PS1 (M146V)) and in mice expressing the C99 fragment via a lentiviral approach and were exacerbated (in vitro and in vivo) following the inhibition of the γ-secretase, blocking the Aβ production and accumulating APP-CTFs. Finally, we have reported a mitochondrial accumulation of APP-CTFs in the temporal lobes necropsies of sporadic AD patients correlating with a defective mitophagic phenotype. Hence, targeting the early APP-CTFs accumulation and mitochondrial dysfunctions could constitute promising novel therapeutic targets in the AD context.Axe 2. Study of the impact of AMPK signaling cascade modulation in AD. We have observed a defective AMPK-ULK1 cascade in the temporal lobes necropsies of sporadic AD patients, in in vitro AD study models (SH-SY5Y-APPswe and -C99) and in symptomatic 3xTgAD mice. Afterward, we have demonstrated that the pharmacological inhibition of AMPK enhances APP-CTFs accumulation, worsen mitochondria structure alterations, triggers mitochondria membrane hyperpolarization, increases ROSmit production, and inhibits mitophagy in vitro. Pharmacological AMPK blockade also alters the dendritic spine maturation ex vivo (organotypic hippocampal slices lentivirally expressing APPswe). Oppositely, the pharmacological activation of AMPK alleviates mitochondria dysfunctions in vitro and favors the dendritic spine maturation ex vivo. We confirmed these observations using a genetic approach by expressing mutated AMPK constructs (constitutive active and dominant negative forms). Importantly, pharmacological activation of AMPK reduces Aβ and Tau pathologies, as well as neuroinflammation and learning impairments in symptomatic 3xTgAD mice. Overall, the stimulation of AMPK could stand as a new therapeutic avenue to alleviate AD pathogenesis
Bécot, Anaïs. "Les APP-CTFs au cœur du processus pathologique de la maladie d’Alzheimer : contribution du système lysosomal-autophagique et de la sécrétion exosomale." Thesis, Université Côte d'Azur (ComUE), 2019. http://theses.univ-cotedazur.fr/2019AZUR6039.
Alzheimer’s disease (AD) is characterized by the pathological accumulation of extracellular and intracellular aggregates (Aβ and Tau) in the brain. AD is also associated with an early alteration of the major degradation pathway of aggregated proteins, the autophagic-lysosomal pathway. Recent works have suggested that this defectcouldbothbeacauseandaconsequenceofearlyintraneuronalaccumulation of C99 (also named as APP-CTFβ), the direct precursor of Aβ. Due to its toxicity, C99 could be a possible key player of AD etiology. The accumulation of this product occurs mainly within organelles of the endolysosomal network, but our recent observations also indicate an extracellular accumulation of C99 in later stages of the disease, or in conditions where the Aβ-generating enzyme, γ-secretase, is blocked. The first aim of my PhD project was to investigate the possible beneficial effect of restoringlysosomal-autophagicfunctiononC99accumulation. Tothisend, weused a viral strategy to overexpress TFEB, a master regulator of both lysosome biogenesis and autophagy, in a mouse model of AD (3xTg-AD mouse). Two approaches were tested aiming to express TFEB either before or after the beginning of C99 accumulation, by injecting AAV-TFEBs into the ventricles of newborn mice or by stereotaxic injection into 3 month-old mice, respectively. These studies have shown a strong TFEB-mediated reduction of C99 accumulation when using both the preventive and curative approach. The aim of the second part of my PhD work was to understand the reasons of the extracellular accumulation of C99. We postulated that this C99-associated immunostaining could correspond to exosomal-associated C99. Exosomes are nanosizedvesiclesofendocyticoriginthatarereleasedfromcellsandknowntotransport neurotoxic proteins. In our study based on pharmacological, immunocytochemical and genetic approaches, we have confirmed this hypothesis and have shown the presence of C99, and of its direct derived-fragment C83 (APP-CTFα), existing as both monomers and oligomers, in exosomes purified from AD cell and mouse models. Moreover, our data have shown that the levels of these APP-CTFs are strongly increased by γ-secretase inhibition, thus explaining the higher levels of extracellular staining in γ-secretase treated animals. In conclusion, my PhD work shows 1) a new potential therapeutic strategy based on TFEB activation aiming to reduce early C99 accumulation and 2) the presence of monomeric and oligomeric C99 in exosomes in AD models and a link between γ-secretase inhibition and oligomerisation. Future studies are needed to elucidate the exact role of these C99-enriched exosomes in AD
Vingtdeux-Didier, Valérie. "Aspects moléculaires et cellulaires impliqués dans le clivage ou la dégradation des fragments carboxy-terminaux et du domaine intracellulaire du Précurseur du Peptide Amyloïde (APP-CTFs et AICD)." Lille 2, 2006. http://www.theses.fr/2006LIL2S036.
Alzheimer's disease (AD) is characterized by two distinct pathologies: neurofibrillary tangles (NFT) and extracellular amyloid plaques composed of beta-amyloid peptide (Abeta). Abeta derive from the catabolism of the Amyloid Precursor Protein (APP). A relationship between APP metabolism and NFT is observed in AD. This relation is illustrated by a significant decrease of APP-CTFs and AIDD, which correlated with the progression of NFT. APP-CTFs phosphorylation is also modified in AD. The main objectives of this thesis were to identify the degradations pathways of APP-CTFs and AICD. Our results demonstrated that increase in the phosphorylation of APP-CTFs facilitates their processing by the gamma-secretase. Moreover, our data demonstrate for the first time that the endosome/lysosome pathway mediates the degradation of AICD and we describe a novel secretion pathway of APP catabolic derivatives