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Article ; Online: Bezafibrate confers neuroprotection in the 5xFAD mouse model of Alzheimer's disease.

Lu, Yubing / Fujioka, Hisashi / Wang, Wenzhang / Zhu, Xiongwei

Biochimica et biophysica acta. Molecular basis of disease

2023 Volume 1869, Issue 8, Page(s) 166841

Abstract: Mitochondrial dysfunction plays an important role in the pathogenesis of Alzheimer's disease (AD), the most common neurodegenerative disease. Prior studies suggested impaired mitochondrial biogenesis likely contributes to mitochondrial dysfunction in AD. ...

Abstract	Mitochondrial dysfunction plays an important role in the pathogenesis of Alzheimer's disease (AD), the most common neurodegenerative disease. Prior studies suggested impaired mitochondrial biogenesis likely contributes to mitochondrial dysfunction in AD. Bezafibrate, a peroxisome proliferator-activated receptor (PPAR) pan-agonist, has been shown to enhance mitochondrial biogenesis and increase oxidative phosphorylation capacity. In the present study, we investigated whether bezafibrate could rescue mitochondrial dysfunction and other AD-related deficits in 5xFAD mice. Bezafibrate was well tolerated by 5xFAD mice. Indeed, it rescued the expression of key mitochondrial proteins as well as mitochondrial dynamics and function in the brain of 5xFAD mice. Importantly, bezafibrate treatment led to significant improvement of cognitive/memory function in 5xFAD mice accompanied by alleviation of amyloid pathology and neuronal loss as well as reduced oxidative stress and neuroinflammation. Overall, this study suggests that bezafibrate improves mitochondrial function, mitigates neuroinflammation and improves cognitive functions in 5xFAD mice, thus supporting the notion that enhancing mitochondrial biogenesis/function is a promising therapeutic strategy for AD.
MeSH term(s)	Mice ; Animals ; Alzheimer Disease/drug therapy ; Alzheimer Disease/genetics ; Alzheimer Disease/metabolism ; Bezafibrate/pharmacology ; Bezafibrate/therapeutic use ; Neurodegenerative Diseases ; Neuroprotection ; Neuroinflammatory Diseases
Chemical Substances	Bezafibrate (Y9449Q51XH)
Language	English
Publishing date	2023-08-07
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	60-7
ISSN	1879-260X ; 1879-2596 ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-260X ; 1879-2596 ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbadis.2023.166841
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Article: Ultrastructure of Myzocytosis and Cyst Formation, and the Role of Actin in Tubular Tether Formation in

Sam-Yellowe, Tobili Y / Fujioka, Hisashi / Peterson, John W

Pathogens (Basel, Switzerland)

2022 Volume 11, Issue 4

Abstract: Free-living relatives of the Apicomplexa such ... ...

Abstract	Free-living relatives of the Apicomplexa such as
Language	English
Publishing date	2022-04-11
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2695572-6
ISSN	2076-0817
ISSN	2076-0817
DOI	10.3390/pathogens11040455
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Article: Fluorescent Nanoparticle Uptake by Myzocytosis and Endocytosis in

Sam-Yellowe, Tobili Y / Asraf, Mary M / Peterson, John W / Fujioka, Hisashi

Microorganisms

2023 Volume 11, Issue 8

Abstract: ... ...

Abstract	Colpodella
Language	English
Publishing date	2023-07-29
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2720891-6
ISSN	2076-2607
ISSN	2076-2607
DOI	10.3390/microorganisms11081945
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Article ; Online: Author Correction: FAM222A encodes a protein which accumulates in plaques in Alzheimer's disease.

Yan, Tingxiang / Liang, Jingjing / Gao, Ju / Wang, Luwen / Fujioka, Hisashi / Zhu, Xiaofeng / Wang, Xinglong

Nature communications

2022 Volume 13, Issue 1, Page(s) 4006

Language	English
Publishing date	2022-07-11
Publishing country	England
Document type	Published Erratum
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-022-31711-8
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Article ; Online: Intermittent Ex Vivo Lung Perfusion in a Porcine Model for Prolonged Lung Preservation.

Sakanoue, Ichiro / Okamoto, Toshihiro / Ayyat, Kamal S / Yun, James J / Farver, Carol F / Fujioka, Hisashi / Date, Hiroshi / McCurry, Kenneth R

Transplantation

2023 Volume 108, Issue 3, Page(s) 669–678

Abstract: Background: Ex vivo lung perfusion expands the lung transplant donor pool and extends preservation time beyond cold static preservation. We hypothesized that repeated regular ex vivo lung perfusion would better maintain lung grafts.: Methods: Ten pig ...

Abstract	Background: Ex vivo lung perfusion expands the lung transplant donor pool and extends preservation time beyond cold static preservation. We hypothesized that repeated regular ex vivo lung perfusion would better maintain lung grafts. Methods: Ten pig lungs were randomized into 2 groups. The control underwent 16 h of cold ischemic time and 2 h of cellular ex vivo lung perfusion. The intermittent ex vivo lung perfusion group underwent cold ischemic time for 4 h, ex vivo lung perfusion (first) for 2 h, cold ischemic time for 10 h, and 2 h of ex vivo lung perfusion (second). Lungs were assessed, and transplant suitability was determined after 2 h of ex vivo lung perfusion. Results: The second ex vivo lung perfusion was significantly associated with better oxygenation, limited extravascular water, higher adenosine triphosphate, reduced intraalveolar edema, and well-preserved mitochondria compared with the control, despite proinflammatory cytokine elevation. No significant difference was observed in the first and second perfusion regarding oxygenation and adenosine triphosphate, whereas the second was associated with lower dynamic compliance and higher extravascular lung water than the first. Transplant suitability was 100% for the first and 60% for the second ex vivo lung perfusion, and 0% for the control. Conclusions: The second ex vivo lung perfusion had a slight deterioration in graft function compared to the first. Intermittent ex vivo lung perfusion created a better condition for lung grafts than cold static preservation, despite cytokine elevation. These results suggested that intermittent ex vivo lung perfusion may help prolong lung preservation.
MeSH term(s)	Swine ; Animals ; Organ Preservation/methods ; Lung ; Perfusion/adverse effects ; Perfusion/methods ; Lung Transplantation/adverse effects ; Lung Transplantation/methods ; Cytokines ; Adenosine Triphosphate
Chemical Substances	Cytokines ; Adenosine Triphosphate (8L70Q75FXE)
Language	English
Publishing date	2023-09-20
Publishing country	United States
Document type	Journal Article
ZDB-ID	208424-7
ISSN	1534-6080 ; 0041-1337
ISSN (online)	1534-6080
ISSN	0041-1337
DOI	10.1097/TP.0000000000004802
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Zs.A 488: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MO 509: Show issues

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Article ; Online: Intraneuronal β-amyloid impaired mitochondrial proteostasis through the impact on LONP1.

Wang, Wenzhang / Ma, Xiaopin / Bhatta, Sabina / Shao, Changjuan / Zhao, Fanpeng / Fujioka, Hisashi / Torres, Sandy / Wu, Fengqin / Zhu, Xiongwei

Proceedings of the National Academy of Sciences of the United States of America

2023 Volume 120, Issue 51, Page(s) e2316823120

Abstract: Mitochondrial dysfunction plays a critical role in the pathogenesis of Alzheimer's disease (AD). Mitochondrial proteostasis regulated by chaperones and proteases in each compartment of mitochondria is critical for mitochondrial function, and it is ... ...

Abstract	Mitochondrial dysfunction plays a critical role in the pathogenesis of Alzheimer's disease (AD). Mitochondrial proteostasis regulated by chaperones and proteases in each compartment of mitochondria is critical for mitochondrial function, and it is suspected that mitochondrial proteostasis deficits may be involved in mitochondrial dysfunction in AD. In this study, we identified LONP1, an ATP-dependent protease in the matrix, as a top Aβ42 interacting mitochondrial protein through an unbiased screening and found significantly decreased LONP1 expression and extensive mitochondrial proteostasis deficits in AD experimental models both in vitro and in vivo, as well as in the brain of AD patients. Impaired METTL3-m
MeSH term(s)	Mice ; Animals ; Humans ; Proteostasis ; Amyloid beta-Peptides/genetics ; Amyloid beta-Peptides/metabolism ; Alzheimer Disease/metabolism ; Mitochondria/metabolism ; Mice, Transgenic ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Mitochondrial Diseases/metabolism ; Methyltransferases/metabolism ; ATP-Dependent Proteases/metabolism
Chemical Substances	Amyloid beta-Peptides ; Mitochondrial Proteins ; METTL3 protein, human (EC 2.1.1.62) ; Methyltransferases (EC 2.1.1.-) ; LONP1 protein, human (EC 3.4.21.-) ; ATP-Dependent Proteases (EC 3.4.21.-)
Language	English
Publishing date	2023-12-13
Publishing country	United States
Document type	Journal Article
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2316823120
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Zs.A 1148: Show issues

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Article ; Online: Damaged mitochondria coincide with presynaptic vesicle loss and abnormalities in alzheimer's disease brain.

Wang, Wenzhang / Zhao, Fanpeng / Lu, Yubing / Siedlak, Sandra L / Fujioka, Hisashi / Feng, Hao / Perry, George / Zhu, Xiongwei

Acta neuropathologica communications

2023 Volume 11, Issue 1, Page(s) 54

Abstract: Loss of synapses is the most robust pathological correlate of Alzheimer's disease (AD)-associated cognitive deficits, although the underlying mechanism remains incompletely understood. Synaptic terminals have abundant mitochondria which play an ... ...

Abstract	Loss of synapses is the most robust pathological correlate of Alzheimer's disease (AD)-associated cognitive deficits, although the underlying mechanism remains incompletely understood. Synaptic terminals have abundant mitochondria which play an indispensable role in synaptic function through ATP provision and calcium buffering. Mitochondrial dysfunction is an early and prominent feature in AD which could contribute to synaptic deficits. Here, using electron microscopy, we examined synapses with a focus on mitochondrial deficits in presynaptic axonal terminals and dendritic spines in cortical biopsy samples from clinically diagnosed AD and age-matched non-AD control patients. Synaptic vesicle density within the presynaptic axon terminals was significantly decreased in AD cases which appeared largely due to significantly decreased reserve pool, but there were significantly more presynaptic axons containing enlarged synaptic vesicles or dense core vesicles in AD. Importantly, there was reduced number of mitochondria along with significantly increased damaged mitochondria in the presynapse of AD which correlated with changes in SV density. Mitochondria in the post-synaptic dendritic spines were also enlarged and damaged in the AD biopsy samples. This study provided evidence of presynaptic vesicle loss as synaptic deficits in AD and suggested that mitochondrial dysfunction in both pre- and post-synaptic compartments contribute to synaptic deficits in AD.
MeSH term(s)	Humans ; Alzheimer Disease/pathology ; Synapses/metabolism ; Presynaptic Terminals/metabolism ; Mitochondria/pathology ; Brain/pathology
Language	English
Publishing date	2023-03-31
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2715589-4
ISSN	2051-5960 ; 2051-5960
ISSN (online)	2051-5960
ISSN	2051-5960
DOI	10.1186/s40478-023-01552-7
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Article ; Online: Colpodella

Getty, Troy A / Peterson, John W / Fujioka, Hisashi / Walsh, Aidan M / Sam-Yellowe, Tobili Y

Tropical medicine and infectious disease

2021 Volume 6, Issue 3

Abstract: ... ...

Abstract	Colpodella
Language	English
Publishing date	2021-07-11
Publishing country	Switzerland
Document type	Journal Article
ISSN	2414-6366
ISSN (online)	2414-6366
DOI	10.3390/tropicalmed6030127
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Article ; Online: FAM222A encodes a protein which accumulates in plaques in Alzheimer's disease.

Yan, Tingxiang / Liang, Jingjing / Gao, Ju / Wang, Luwen / Fujioka, Hisashi / Zhu, Xiaofeng / Wang, Xinglong

Nature communications

2020 Volume 11, Issue 1, Page(s) 411

Abstract: Alzheimer's disease (AD) is characterized by amyloid plaques and progressive cerebral atrophy. Here, we report FAM222A as a putative brain atrophy susceptibility gene. Our cross-phenotype association analysis of imaging genetics indicates a potential ... ...

Abstract	Alzheimer's disease (AD) is characterized by amyloid plaques and progressive cerebral atrophy. Here, we report FAM222A as a putative brain atrophy susceptibility gene. Our cross-phenotype association analysis of imaging genetics indicates a potential link between FAM222A and AD-related regional brain atrophy. The protein encoded by FAM222A is predominantly expressed in the CNS and is increased in brains of patients with AD and in an AD mouse model. It accumulates within amyloid deposits, physically interacts with amyloid-β (Aβ) via its N-terminal Aβ binding domain, and facilitates Aβ aggregation. Intracerebroventricular infusion or forced expression of this protein exacerbates neuroinflammation and cognitive dysfunction in an AD mouse model whereas ablation of this protein suppresses the formation of amyloid deposits, neuroinflammation and cognitive deficits in the AD mouse model. Our data support the pathological relevance of protein encoded by FAM222A in AD.
MeSH term(s)	Aged ; Aged, 80 and over ; Alzheimer Disease/diagnostic imaging ; Alzheimer Disease/genetics ; Alzheimer Disease/pathology ; Amyloid beta-Peptides/metabolism ; Amyloidogenic Proteins/genetics ; Amyloidogenic Proteins/metabolism ; Animals ; Atrophy/diagnostic imaging ; Atrophy/genetics ; Atrophy/pathology ; Brain/diagnostic imaging ; Brain/pathology ; Cognitive Dysfunction/genetics ; Cognitive Dysfunction/pathology ; Datasets as Topic ; Disease Models, Animal ; Female ; Genetic Predisposition to Disease ; Genome-Wide Association Study ; Humans ; Male ; Mice ; Mice, Transgenic ; Middle Aged ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Plaque, Amyloid/genetics ; Plaque, Amyloid/pathology ; Polymorphism, Single Nucleotide ; Protein Aggregation, Pathological/diagnostic imaging ; Protein Aggregation, Pathological/genetics ; Protein Aggregation, Pathological/pathology
Chemical Substances	Amyloid beta-Peptides ; Amyloidogenic Proteins ; FAM222A protein, human ; Fam222a protein, mouse ; Nerve Tissue Proteins
Language	English
Publishing date	2020-01-21
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-019-13962-0
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Article ; Online: VPS35 D620N knockin mice recapitulate cardinal features of Parkinson's disease.

Niu, Mengyue / Zhao, Fanpeng / Bondelid, Karina / Siedlak, Sandra L / Torres, Sandy / Fujioka, Hisashi / Wang, Wenzhang / Liu, Jun / Zhu, Xiongwei

Aging cell

2021 Volume 20, Issue 5, Page(s) e13347

Abstract: D620N mutation in the vacuolar protein sorting 35 ortholog (VPS35) gene causes late-onset, autosomal dominant familial Parkinson's disease (PD) and contributes to idiopathic PD. However, how D620N mutation leads to PD-related deficits in vivo remains ... ...

Abstract	D620N mutation in the vacuolar protein sorting 35 ortholog (VPS35) gene causes late-onset, autosomal dominant familial Parkinson's disease (PD) and contributes to idiopathic PD. However, how D620N mutation leads to PD-related deficits in vivo remains unclear. In the present study, we thoroughly characterized the biochemical, pathological, and behavioral changes of a VPS35 D620N knockin (KI) mouse model with chronic aging. We reported that this VPS35 D620N KI model recapitulated a spectrum of cardinal features of PD at 14 months of age which included age-dependent progressive motor deficits, significant changes in the levels of dopamine (DA) and DA metabolites in the striatum, and robust neurodegeneration of the DA neurons in the SNpc and DA terminals in the striatum, accompanied by increased neuroinflammation, and accumulation and aggregation of α-synuclein in DA neurons. Mechanistically, D620N mutation induced mitochondrial fragmentation and dysfunction in aged mice likely through enhanced VPS35-DLP1 interaction and increased turnover of mitochondrial DLP1 complexes in vivo. Finally, the VPS35 D620N KI mice displayed greater susceptibility to MPTP-mediated degeneration of nigrostriatal pathway, indicating that VPS35 D620N mutation increased vulnerability of DA neurons to environmental toxins. Overall, this VPS35 D620N KI mouse model provides a powerful tool for future disease modeling and pharmacological studies of PD. Our data support the involvement of VPS35 in the development of α-synuclein pathology in vivo and revealed the important role of mitochondrial fragmentation/dysfunction in the pathogenesis of VPS35 D620N mutation-associated PD in vivo.
MeSH term(s)	Animals ; Brain/metabolism ; Brain/pathology ; Disease Models, Animal ; Dopamine/metabolism ; Dopaminergic Neurons/pathology ; Gene Knock-In Techniques ; Mice ; Mitochondria/ultrastructure ; Parkinsonian Disorders/etiology ; Parkinsonian Disorders/genetics ; Parkinsonian Disorders/metabolism ; Parkinsonian Disorders/pathology ; Vesicular Transport Proteins/genetics ; alpha-Synuclein/metabolism
Chemical Substances	Vesicular Transport Proteins ; Vps35 protein, mouse ; alpha-Synuclein ; Dopamine (VTD58H1Z2X)
Language	English
Publishing date	2021-03-21
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2113083-8
ISSN	1474-9726 ; 1474-9718
ISSN (online)	1474-9726
ISSN	1474-9718
DOI	10.1111/acel.13347
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