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Kurti, Aishe

Mayo Clinic

Mayo Clinic

Citations 19

Author response: APOE2 is associated with longevity independent of Alzheimer’s disease
Shinohara, Mitsuru , Kanekiyo, Takahisa , Kurti, Aishe, Shinohara, Motoko, Sullivan, Patrick M. , Fryer, John Denis , Tachibana, Masaya, Fu, Yuan , Zhao, Jing , Han, Xianlin , Rebeck, G. William , Heckman, Michael G. , Bu, Guojun

No container title available | October 26, 2020 | Volume: No volume available | Issue: No issue available | Pages: No page available

10.7554/elife.62199.sa2 Get It

APOE2 is associated with longevity independent of Alzheimer’s disease
Shinohara, Mitsuru , Kanekiyo, Takahisa , Kurti, Aishe, Shinohara, Motoko, Fu, Yuan , Sullivan, Patrick M. , Rebeck, G. William , Fryer, John Denis , Bu, Guojun , Tachibana, Masaya , Fryer, John D , Bu, Guojun , Tachibana, Masaya, Zhao, Jing , Han, Xianlin , Heckman, Michael G.

eLife | October 19, 2020 | Volume: 9 | Issue: No issue available | Pages: No page available

10.7554/elife.62199 Get It

Although the ε2 allele of apolipoprotein E ( APOE2 ) benefits longevity, its mechanism is not understood. The protective effects of the APOE 2 on Alzheimer’s disease (AD) risk, particularly through their effects on amyloid or tau accumulation, may confound APOE2 effects on longevity. Herein, we showed that the association between APOE2 and longer lifespan persisted irrespective of AD status, including its neuropathology, by analyzing clinical datasets as well as animal models. Notably, APOE2 was associated with preserved activity during aging, which also associated with lifespan. In animal models, distinct apoE isoform levels, where APOE2 has the highest, were correlated with activity levels, while some forms of cholesterol and triglycerides were associated with apoE and activity levels. These results indicate that APOE2 can contribute to longevity independent of AD. Preserved activity would be an early-observable feature of APOE2 -mediated longevity, where higher levels of apoE2 and its-associated lipid metabolism might be involved.
APOE4 exacerbates α-synuclein pathology and related toxicity independent of amyloid
Zhao, Na , Attrebi, Olivia N., Ren, Yingxue , Qiao, Wenhui , Sonustun, Berkiye , Martens, Yuka A. , Meneses, Axel , Li, Fuyao , Shue, Francis , Zheng, Jiaying , Ingelgom, Alexandra J. Van, Davis, Mary Dabney , Kurti, Aishe, Linares, Cynthia , Chen, Yixing , Delenclos, Marion , Liu, Chia‐Chen , Fryer, John Denis , Asmann, Yan W. , McLean, Pamela J. , Ross, Owen A. , Bu, Guojun , Meneses, Axel D , Van Ingelgom, Alexandra J, Davis, Mary D , Knight, Joshua A. , McLean, Pamela J , Liu, Chia-Chen , Dickson, Dennis W , Ross, Owen A , Bu, Guojun , Shue, Francis , Zhao, Na , Chen, Yixing , Sonustun, Berkiye , Li, Fuyao , McLean, Pamela J , Zheng, Jiaying , Dickson, Dennis W.

Science Translational Medicine | February 6, 2020 | Volume: 12 | Issue: 529 | Pages: No page available

10.1126/scitranslmed.aay1809 Get It

APOE4 exacerbates α-synuclein pathology in a synucleinopathy mouse model, and APOE4 genotype associates with increased α-synuclein pathology in humans.
Heterochromatin anomalies and double-stranded RNA accumulation underlie C9orf72 poly(PR) toxicity
Zhang, Yong‐Jie , Guo, Lin , Gonzales, Patrick , Gendron, Tania F. , Wu, Yanwei , Jansen‐West, Karen , O’Raw, Aliesha D. , Pickles, Sarah , Prudencio, Mercedes , Carlomagno, Yari , Gachechiladze, Mariam A. , Tian, Ruilin , Chew, Jeannie , DeTure, Michael , Lin, Wen-Lang, Tong, Jimei, Daughrity, Lillian M. , Yue, Mei, Song, Yuping , Andersen, Jonathan W. , Castanedes‐Casey, Monica , Kurti, Aishe, Antognetti, Giovanna, McCampbell, Alexander , Rademakers, Rosa , Oskarsson, Björn , Kampmann, Martin , Ward, Michael E. , Fryer, John Denis , Link, Christopher D. , Shorter, James , Petrucelli, Leonard , Gonzales, Patrick K , Pickles, Sarah R , Chew, Jeannie , DeTure, Michael , Daughrity, Lillian M , Castanedes-Casey, Monica , McCampbell, Alexander , Rademakers, Rosa , Oskarsson, Björn , Dickson, Dennis W , Kampmann, Martin , Ward, Michael E , Shorter, James , Petrucelli, Leonard , Zhang, Yong-Jie , Prudencio, Mercedes , O'Raw, Aliesha , Gendron, Tania F , Guo, Lin , Ludwig, Connor , Datta, Abhishek, Dickson, Dennis W.

Science | February 15, 2019 | Volume: 363 | Issue: 6428 | Pages: No page available

10.1126/science.aav2606 Get It

How dipeptide repeats cause pathology A repeat expansion in the chromosome 9 open reading frame 72 ( C9orf72 ) gene is the most common known cause of two neurodegenerative diseases: frontotemporal dementia and amyotrophic lateral sclerosis. This expansion leads to the abnormal production of proteins of repeating dipeptides, but their contribution to disease pathogenesis remains unclear. Zhang et al. engineered a mouse model to study the consequences of one of these dipeptides—prolinearginine dipeptide repeat protein, poly(PR)—in the brain. They found that poly(PR) caused neuron loss as well as motor and memory impairments. These detrimental effects resulted from poly(PR)-induced perturbation of heterochromatin function, a tightly packed form of DNA that represses gene expression. Science , this issue p. eaav2606
P4‐065: APOE4 CONDITIONALLY EXPRESSED IN CEREBROVASCULATURE IMPAIRS ENDOTHELIAL FUNCTIONS AND INDUCES COGNITIVE DEFICITS
Kurti, Aishe, Yamazaki, Akari, Fryer, John Denis , Kanekiyo, Takahisa , Yamazaki, Yu , Liu, Chia‐Chen , Oue, Hiroshi , Bu, Guojun

Alzheimer's & Dementia | October 22, 2018 | Volume: 14 | Issue: 7S_Part_27 | Pages: No page available

10.1016/j.jalz.2018.06.2468 Get It

[P4–125]: THE MOLECULAR CHAPERONE BRICHOS INHIBITS Aβ AGGREGATION AND OTHER NEUROPATHOLOGICAL PHENOTYPES IN A MOUSE MODEL OF Aβ AMYLOIDOSIS
Kim, Chaeyoung, Dolfe, Lisa, Belmonte, Krystal Courtney D. , Kurti, Aishe, Fryer, John Denis , Kim, Jungsu , Flores, Luis Emilio , Presto, Jenny , Johansson, Jan

Alzheimer's & Dementia | October 20, 2017 | Volume: 13 | Issue: 7S_Part_27 | Pages: No page available

10.1016/j.jalz.2017.06.1991 Get It

Behavioral and transcriptomic analysis of Trem2-null mice: not all knockout mice are created equal
Kang, Silvia S. , Kurti, Aishe, Baker, Kelsey E., Liu, Chia‐Chen , Ulrich, Jason D. , Bu, Guojun , Fryer, John Denis , Fryer, John D., Liu, Chia-Chen , Bu, Guojun , Colonna, Marco , Holtzman, David M.

Human Molecular Genetics | October 10, 2017 | Volume: 27 | Issue: 2 | Pages: 211-223

10.1093/hmg/ddx366 Get It

Loss of clusterin shifts amyloid deposition to the cerebrovasculature via disruption of perivascular drainage pathways
Wojtas, Aleksandra, Kang, Silvia S. , Olley, Benjamin M., Gatherer, Maureen, Shinohara, Mitsuru , Lozano, Patricia A., Liu, Chia‐Chen , Kurti, Aishe, Baker, Kelsey E., Yue, Mei, Petrucelli, Leonard , Bu, Guojun , Fryer, John Denis , Wojtas, Aleksandra M, Fryer, John D., Dickson, Dennis W. , Carare, Roxana Octavia , Liu, Chia-Chen , Bu, Guojun

Proceedings of the National Academy of Sciences | July 12, 2017 | Volume: 114 | Issue: 33 | Pages: No page available

10.1073/pnas.1701137114 Get It

Significance Deposition of amyloid-β (Aβ) peptide in the form of parenchymal plaques and Aβ accumulation in the walls of cerebral vessels as cerebral amyloid angiopathy (CAA) are pathological hallmarks of Alzheimer’s disease (AD). The clusterin ( CLU ) gene, which confers AD risk, is associated with amyloid deposition. Here we show that loss of CLU promotes cerebrovascular CAA, yet significantly reduces the amount of parenchymal plaques by altering perivascular drainage of Aβ in the APP/PS1 mouse model of AD. The absence of CLU in these mice is associated with a lower number of hemorrhages and a decrease in inflammation. These results suggest that CLU functions as a major Aβ chaperone to maintain Aβ solubility along interstitial fluid drainage pathways and prevent CAA formation.
C9ORF72 repeat expansions in mice cause TDP-43 pathology, neuronal loss, and behavioral deficits
Chew, Jeannie , Prudencio, Mercedes , Sasaguri, Hiroki , Zhang, Yong‐Jie , Castanedes‐Casey, Monica , Lee, Chris W. , Jansen‐West, Karen , Kurti, Aishe, Murray, Melissa E. , Bieniek, Kevin F. , Bauer, Peter , Whitelaw, Ena C., Rousseau, Linda , Stankowski, Jeannette N. , Stetler, Caroline, Daughrity, Lillian M. , Perkerson, Emilie A., Desaro, Pamela , Johnston, Amelia, Overstreet, Karen, Edbauer, Dieter , Rademakers, Rosa , Fryer, John Denis , Petrucelli, Leonard , Gendron, Tania F. , Castanedes-Casey, Monica, Jansen-West, Karen, Bauer, Peter O, Boylan, Kevin B, Fryer, John D., Boylan, Khrista , Dickson, Dennis W. , Zhang, Yong-Jie , Prudencio, Mercedes , Murray, Melissa E

Science | May 14, 2015 | Volume: 348 | Issue: 6239 | Pages: 1151-1154

10.1126/science.aaa9344 Get It

A mouse model for ALS A G4C2 repeat expansion in C9ORF72 is known to be the major genetic cause of frontotemporal dementia and amyotrophic lateral sclerosis (c9FTD/ALS). However, a lack of animal models recapitulating key disease features has hindered efforts to understand and prevent c9FTD/ALS-related neurodegeneration. Until now. Chew et al. describe a mouse model that mimics both neuropathological and clinical phenotypes of c9FTD/ALS. Science , this issue p. 1151