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Article: Neuronal MHC-I complex is destabilized by amyloid-β and its implications in Alzheimer's disease.

Kim, Min-Seok / Cho, Kwangmin / Cho, Mi-Hyang / Kim, Na-Young / Kim, Kyunggon / Kim, Dong-Hou / Yoon, Seung-Yong

2023 Volume 13, Issue 1, Page(s) 181

Abstract: Backgrounds: The expression of major histocompatibility complex I (MHC-I) in neurons has recently been shown to regulate neurite outgrowth and synaptic plasticity. However, its contribution to neurodegenerative diseases such as Alzheimer's disease (AD) ... ...

Abstract	Backgrounds: The expression of major histocompatibility complex I (MHC-I) in neurons has recently been shown to regulate neurite outgrowth and synaptic plasticity. However, its contribution to neurodegenerative diseases such as Alzheimer's disease (AD) remains largely unknown. Methods: In this study, we investigated the relationship between impaired MHC-I-β2M complex and AD in vitro and human AD samples. Interaction between protein was identified by liquid chromatography-tandem mass spectrometry and confirmed by immunoprecipitation. Single-chain trimer of MHC-I-β2M was generated to study the effect of stabilization of MHC-I-β2M complex on NCAM1 signaling. Results: MHC-I is destabilized in the brains of AD patients and neuronal cells treated with oligomeric β-amyloid (Aβ). Specifically, Aβ oligomers disassemble the MHC-I-β2-microglobulin (β2M) complex, leading to reduced interactions with neural cell adhesion molecule 1 (NCAM1), a novel interactor of neuronal MHC-I, and decreased signaling. Inhibition of MHC-I-β2M complex destabilization by non-dissociable MHC-I-β2M-peptide complex restored MHC-I-NCAM1 signaling in neuronal cells. Conclusions: The current study demonstrated that disruption of MHC-1-NCAM1 signaling by Aβ induced disassembly of MHC-I-β2M complex is involved in the pathophysiology of AD. Moreover, our findings suggest modulation of MHC-I stability may be a potential therapeutic target for restoring synaptic function in AD.
Language	English
Publishing date	2023-09-29
Publishing country	England
Document type	Journal Article
ZDB-ID	2593367-X
ISSN	2045-3701
ISSN	2045-3701
DOI	10.1186/s13578-023-01132-1
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Article ; Online: Alzheimer's disease genes and autophagy.

Yoon, Seung-Yong / Kim, Dong-Hou

Brain research

2016 Volume 1649, Issue Pt B, Page(s) 201–209

Abstract: Autophagy is a process to degrade and recycle cellular constituents via the lysosome for regulating cellular homeostasis. Its dysfunction is now considered to be involved in many diseases, including neurodegenerative diseases. Many features reflecting ... ...

Abstract	Autophagy is a process to degrade and recycle cellular constituents via the lysosome for regulating cellular homeostasis. Its dysfunction is now considered to be involved in many diseases, including neurodegenerative diseases. Many features reflecting autophagy impairment, such as autophagosome accumulation and lysosomal dysfunction, have been also revealed to be involved in Alzheimer's disease (AD). Recent genetic studies such as genome-wide association studies in AD have identified a number of novel genes associated with AD. Some of the identified genes have demonstrated dysfunction in autophagic processes in AD, while others remain under investigation. Since autophagy is strongly regarded to be one of the major pathogenic mechanisms of AD, it is necessary to review how the AD-associated genes are related to autophagy. We anticipate our current review to be a starting point for future studies regarding AD-associated genes and autophagy. This article is part of a Special Issue entitled SI:Autophagy.
MeSH term(s)	Alzheimer Disease/genetics ; Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Animals ; Autophagy ; Brain/metabolism ; Brain/pathology ; Humans ; Membrane Proteins/genetics ; Membrane Proteins/metabolism
Chemical Substances	Membrane Proteins
Language	English
Publishing date	2016-10-15
Publishing country	Netherlands
Document type	Journal Article ; Review
ZDB-ID	1200-2
ISSN	1872-6240 ; 0006-8993
ISSN (online)	1872-6240
ISSN	0006-8993
DOI	10.1016/j.brainres.2016.03.018
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Article ; Online: Tau acetylation at K280 regulates tau phosphorylation.

Kim, Min-Seok / Mun, Yeon-Seon / Lee, Seung-Eun / Cho, Woo-Young / Han, Seung-Hwan / Kim, Dong-Hou / Yoon, Seung-Yong

The International journal of neuroscience

2022 Volume 133, Issue 12, Page(s) 1394–1398

Abstract: Purpose/aim of the study: Accumulation of hyperphosphorylated tau is a key pathological finding of Alzheimer's disease. Recently, acetylation of tau is emerging as another key pathogenic modification, especially regarding the acetylation of tau at K280 ... ...

Abstract	Purpose/aim of the study: Accumulation of hyperphosphorylated tau is a key pathological finding of Alzheimer's disease. Recently, acetylation of tau is emerging as another key pathogenic modification, especially regarding the acetylation of tau at K280 of the hexapeptide Materials and methods: The human neuroblastoma cell line, SH-SY5Y, was transfected with p300 acetyltransferase and tau to induce acetylation of tau. Phosphorylation profile after acetylation was evaluated on western blot. K280A-mutant tau was transfected to investigate the effect of acetylation of tau at K280 on tau phosphorylation profile. Results: Overexpression of p300 acetyltransferase in tau-transfected SH-SY5Y human neuroblastoma cells increased acetylation of tau. Meanwhile, tau and its phosphorylation also increased at various sites such as S199/202, S202/T205, T231, and S422, but not at S396. However, blocking acetylation only at K280 with K280A-mutant tau reversed the increased phosphorylation of tau at S202/T205, T231, and S422, but not at S199/202 or S396. Conclusion: Here we identified tau phosphorylation profile in the context of p300-induced acetylation and K280A-mutant tau, demonstrating that tau acetylation affects phosphorylation differently by residues and that acetylation at K280 is a determinant of phosphorylation at some residues in the context of pathologic acetyltransferase activity. Yet, our results suggest there is a complex interplay yet to be explored between tau acetylation with tau phosphorylation.
MeSH term(s)	Humans ; Phosphorylation ; tau Proteins/metabolism ; Acetylation ; Neuroblastoma ; Protein Processing, Post-Translational ; Alzheimer Disease/metabolism
Chemical Substances	tau Proteins
Language	English
Publishing date	2022-06-28
Publishing country	England
Document type	Journal Article
ZDB-ID	3061-2
ISSN	1563-5279 ; 1543-5245 ; 0020-7454
ISSN (online)	1563-5279 ; 1543-5245
ISSN	0020-7454
DOI	10.1080/00207454.2022.2081165
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Zs.A 657: Show issues

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Article ; Online: Amphiregulin normalizes altered circuit connectivity for social dominance of the CRTC3 knockout mouse.

Park, Ji-Seon / Heo, Hwon / Kim, Min-Seok / Lee, Seung-Eun / Park, Sukyoung / Kim, Ki-Hyun / Kang, Young-Ho / Kim, Je Seong / Sung, Young Hoon / Shim, Woo Hyun / Kim, Dong-Hou / Song, Youngsup / Yoon, Seung-Yong

Molecular psychiatry

2023 Volume 28, Issue 11, Page(s) 4655–4665

Abstract: Social hierarchy has a profound impact on social behavior, reward processing, and mental health. Moreover, lower social rank can lead to chronic stress and often more serious problems such as bullying victims of abuse, suicide, or attack to society. ... ...

Abstract	Social hierarchy has a profound impact on social behavior, reward processing, and mental health. Moreover, lower social rank can lead to chronic stress and often more serious problems such as bullying victims of abuse, suicide, or attack to society. However, its underlying mechanisms, particularly their association with glial factors, are largely unknown. In this study, we report that astrocyte-derived amphiregulin plays a critical role in the determination of hierarchical ranks. We found that astrocytes-secreted amphiregulin is directly regulated by cAMP response element-binding (CREB)-regulated transcription coactivator 3 (CRTC3) and CREB. Mice with systemic and astrocyte-specific CRTC3 deficiency exhibited a lower social rank with reduced functional connectivity between the prefrontal cortex, a major social hierarchy center, and the parietal cortex. However, this effect was reversed by astrocyte-specific induction of amphiregulin expression, and the epidermal growth factor domain was critical for this action of amphiregulin. These results provide evidence of the involvement of novel glial factors in the regulation of social dominance and may shed light on the clinical application of amphiregulin in the treatment of various psychiatric disorders.
MeSH term(s)	Animals ; Mice ; Amphiregulin/genetics ; Mice, Knockout ; Signal Transduction ; Social Dominance ; Transcription Factors/metabolism
Chemical Substances	Amphiregulin ; CRTC3 protein, mouse ; Transcription Factors ; Areg protein, mouse
Language	English
Publishing date	2023-09-20
Publishing country	England
Document type	Journal Article
ZDB-ID	1330655-8
ISSN	1476-5578 ; 1359-4184
ISSN (online)	1476-5578
ISSN	1359-4184
DOI	10.1038/s41380-023-02258-x
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Article ; Online: Regulation of amyloid precursor protein processing by its KFERQ motif.

Park, Ji-Seon / Kim, Dong-Hou / Yoon, Seung-Yong

BMB reports

2016 Volume 49, Issue 6, Page(s) 337–342

Abstract: Understanding of trafficking, processing, and degradation mechanisms of amyloid precursor protein (APP) is important because APP can be processed to produce β-amyloid (Aβ), a key pathogenic molecule in Alzheimer's disease (AD). Here, we found that APP ... ...

Abstract	Understanding of trafficking, processing, and degradation mechanisms of amyloid precursor protein (APP) is important because APP can be processed to produce β-amyloid (Aβ), a key pathogenic molecule in Alzheimer's disease (AD). Here, we found that APP contains KFERQ motif at its C-terminus, a consensus sequence for chaperone-mediated autophagy (CMA) or microautophagy which are another types of autophagy for degradation of pathogenic molecules in neurodegenerative diseases. Deletion of KFERQ in APP increased C-terminal fragments (CTFs) and secreted N-terminal fragments of APP and kept it away from lysosomes. KFERQ deletion did not abolish the interaction of APP or its cleaved products with heat shock cognate protein 70 (Hsc70), a protein necessary for CMA or microautophagy. These findings suggest that KFERQ motif is important for normal processing and degradation of APP to preclude the accumulation of APP-CTFs although it may not be important for CMA or microautophagy. [BMB Reports 2016; 49(6): 337-342].
MeSH term(s)	Amino Acid Motifs ; Amino Acid Sequence ; Amyloid beta-Protein Precursor/chemistry ; Amyloid beta-Protein Precursor/metabolism ; Cell Line, Tumor ; HSC70 Heat-Shock Proteins/metabolism ; Humans ; Lysosomes/metabolism ; Phosphorylation ; Protein Binding ; Protein Processing, Post-Translational ; Structure-Activity Relationship ; tau Proteins/metabolism
Chemical Substances	Amyloid beta-Protein Precursor ; HSC70 Heat-Shock Proteins ; tau Proteins
Language	English
Publishing date	2016-01-15
Publishing country	Korea (South)
Document type	News
ZDB-ID	2410389-5
ISSN	1976-670X ; 1976-6696
ISSN (online)	1976-670X
ISSN	1976-6696
DOI	10.5483/bmbrep.2016.49.6.212
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Article ; Online: Ouabain activates transcription factor EB and exerts neuroprotection in models of Alzheimer's disease.

Song, Ha-Lim / Demirev, Atanas Vladimirov / Kim, Na-Young / Kim, Dong-Hou / Yoon, Seung-Yong

Molecular and cellular neurosciences

2018 Volume 95, Page(s) 13–24

Abstract: The number of neurofibrillary tangles containing abnormal hyperphosphorylated tau protein correlates with the degree of dementia in Alzheimer's disease (AD). In addition, autophagosome accumulation and disturbance of autophagy, the process by which toxic ...

Abstract	The number of neurofibrillary tangles containing abnormal hyperphosphorylated tau protein correlates with the degree of dementia in Alzheimer's disease (AD). In addition, autophagosome accumulation and disturbance of autophagy, the process by which toxic aggregate proteins are degraded in the cytosol, are also found in AD models. These indicate that regulation of the autophagy-lysosome system may be a potential therapeutic target for AD. Activation of transcription factor EB (TFEB), a master regulator of autophagy-lysosome system gene transcription, reduces the amount of tau in APP mice. Here, to identify potential therapeutic compounds for AD, we performed two types of screening to determine pharmacologically active compounds that increase 1) neuronal viability in okadaic acid-induced tau hyperphosphorylation-related neurodegeneration models and 2) nuclear localization of TFEB in high-contents screening. Ouabain, a cardiac glycoside, was discovered as a common hit compound in both screenings. It also exhibited a significant protective effect in tau transgenic fly and mouse models in vivo. This work demonstrates that ouabain enhances activation of TFEB through inhibition of the mTOR pathway and induces downstream autophagy-lysosomal gene expression and cellular restorative properties. Therefore, therapeutic approaches using ouabain reduce the accumulation of abnormal toxic tau in vitro and in vivo.
MeSH term(s)	Alzheimer Disease/metabolism ; Animals ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors/metabolism ; Cells, Cultured ; Drosophila melanogaster ; HeLa Cells ; Humans ; Mice ; Mice, Inbred C57BL ; Neurons/drug effects ; Neurons/metabolism ; Neuroprotective Agents/pharmacology ; Ouabain/pharmacology ; TOR Serine-Threonine Kinases/metabolism ; tau Proteins/genetics ; tau Proteins/metabolism
Chemical Substances	Basic Helix-Loop-Helix Leucine Zipper Transcription Factors ; Neuroprotective Agents ; Tcfeb protein, mouse ; tau Proteins ; Ouabain (5ACL011P69) ; TOR Serine-Threonine Kinases (EC 2.7.1.1)
Language	English
Publishing date	2018-12-28
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1046640-x
ISSN	1095-9327 ; 1044-7431
ISSN (online)	1095-9327
ISSN	1044-7431
DOI	10.1016/j.mcn.2018.12.007
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Article: TLQP-21 mediated activation of microglial BV2 cells promotes clearance of extracellular fibril amyloid-β

Cho, Kwangmin / Jang, You-Jin / Lee, Se-Jong / Jeon, Yu-Na / Shim, Young-Lim / Lee, Ji-Yong / Lim, Da-Som / Kim, Dong-Hou / Yoon, Seung-Yong

Biochemical and biophysical research communications. 2020 Apr. 09, v. 524, no. 3

2020

Abstract: β-Amyloid (Aβ) plaque in the brains of patients with Alzheimer’s disease (AD) is mainly caused by impaired clearance of Aβ by glial cells, including microglia and astrocytes. Because microglia play an important protective role in the central nervous ... ...

Abstract	β-Amyloid (Aβ) plaque in the brains of patients with Alzheimer’s disease (AD) is mainly caused by impaired clearance of Aβ by glial cells, including microglia and astrocytes. Because microglia play an important protective role in the central nervous system, many efforts have been made to identify agents that effectively improve microglial Aβ phagocytosis. This study found that TLQP-21, which is cleaved from VGF (VGF nerve growth factor inducible) precursor protein, enhanced Aβ phagocytosis and degradation by microglial BV2 cells. TLQP-21 also improved microglial phagocytic activity and promoted fibrillar amyloid-β (fAβ) uptake by microglial BV2 cells via a C3AR1-dependent mechanism. Moreover, TLQP-21 stimulated Aβ degradation by enhancing lysosome activity, thereby enhancing fAβ clearance. These results suggest that treatment with TLQP-21 may be a novel therapeutic strategy to efficiently enhance microglial Aβ clearance in AD.
Keywords	astrocytes ; lysosomes ; nerve growth factor ; phagocytosis ; protective effect ; research ; therapeutics
Language	English
Dates of publication	2020-0409
Size	p. 764-771.
Publishing place	Elsevier Inc.
Document type	Article
Note	NAL-AP-2-clean
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2020.01.111
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Article ; Online: Inhibition of REV-ERBs stimulates microglial amyloid-beta clearance and reduces amyloid plaque deposition in the 5XFAD mouse model of Alzheimer's disease.

Lee, Jiyeon / Kim, Do Eon / Griffin, Percy / Sheehan, Patrick W / Kim, Dong-Hou / Musiek, Erik S / Yoon, Seung-Yong

Aging cell

2019 Volume 19, Issue 2, Page(s) e13078

Abstract: A promising new therapeutic target for the treatment of Alzheimer's disease (AD) is the circadian system. Although patients with AD are known to have abnormal circadian rhythms and suffer sleep disturbances, the role of the molecular clock in regulating ... ...

Abstract	A promising new therapeutic target for the treatment of Alzheimer's disease (AD) is the circadian system. Although patients with AD are known to have abnormal circadian rhythms and suffer sleep disturbances, the role of the molecular clock in regulating amyloid-beta (Aβ) pathology is still poorly understood. Here, we explored how the circadian repressors REV-ERBα and β affected Aβ clearance in mouse microglia. We discovered that, at Circadian time 4 (CT4), microglia expressed higher levels of the master clock protein BMAL1 and more rapidly phagocytosed fibrillary Aβ
MeSH term(s)	ARNTL Transcription Factors/metabolism ; Alzheimer Disease/pathology ; Amyloid beta-Peptides/chemical synthesis ; Amyloid beta-Peptides/metabolism ; Animals ; CLOCK Proteins/metabolism ; Cell Line ; Circadian Clocks/genetics ; Disease Models, Animal ; Isoquinolines/pharmacology ; Macrophages/metabolism ; Mice ; Mice, Knockout ; Microglia/metabolism ; Nuclear Receptor Subfamily 1, Group D, Member 1/antagonists & inhibitors ; Nuclear Receptor Subfamily 1, Group D, Member 1/metabolism ; Plaque, Amyloid/genetics ; Plaque, Amyloid/metabolism ; Plaque, Amyloid/pathology ; RNA, Small Interfering ; Receptors, Cytoplasmic and Nuclear/antagonists & inhibitors ; Receptors, Cytoplasmic and Nuclear/genetics ; Receptors, Cytoplasmic and Nuclear/metabolism ; Receptors, Purinergic P2Y12/drug effects ; Receptors, Purinergic P2Y12/metabolism ; Repressor Proteins/antagonists & inhibitors ; Repressor Proteins/genetics ; Repressor Proteins/metabolism ; Synapses/genetics ; Synapses/metabolism ; Thiophenes/pharmacology
Chemical Substances	ARNTL Transcription Factors ; Amyloid beta-Peptides ; Bmal1 protein, mouse ; Isoquinolines ; Nr1d1 protein, mouse ; Nr1d2 protein, mouse ; Nuclear Receptor Subfamily 1, Group D, Member 1 ; P2ry12 protein, mouse ; RNA, Small Interfering ; Receptors, Cytoplasmic and Nuclear ; Receptors, Purinergic P2Y12 ; Repressor Proteins ; SR 8278 ; Thiophenes ; CLOCK Proteins (EC 2.3.1.48)
Language	English
Publishing date	2019-12-04
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; 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.13078
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Article ; Online: Small-molecule drug screening identifies drug Ro 31-8220 that reduces toxic phosphorylated tau in Drosophila melanogaster.

Shim, Kyu-Ho / Kim, Soo-Hwan / Hur, Joon / Kim, Dong-Hou / Demirev, Atanas Vladimirov / Yoon, Seung-Yong

Neurobiology of disease

2019 Volume 130, Page(s) 104519

Abstract: The intraneuronal aggregates of hyperphosphorylated and misfolded tau (neurofibrillary tangles, NFTs) cause a stereotypical spatiotemporal Alzheimer's disease (AD) progression that correlates with the severity of the associated cognitive decline. Kinase ... ...

Abstract	The intraneuronal aggregates of hyperphosphorylated and misfolded tau (neurofibrillary tangles, NFTs) cause a stereotypical spatiotemporal Alzheimer's disease (AD) progression that correlates with the severity of the associated cognitive decline. Kinase activity contributes to the balance between neuron survival and cell death. Hyperactivation of kinases including the conventional protein kinase C (PKC) is a defective molecular event accompanying associative memory loss, tau phosphorylation, and progression of AD or related neurodegenerative diseases. Here, we investigated the ability of small therapeutic compounds (a custom library) to improve tau-induced rough-eye phenotype in a Drosophila melanogaster model of frontotemporal dementia. We also assessed the tau phosphorylation in vivo and selected hit compounds. Among the potential hits, we investigated Ro 31-8220, described earlier as a potent PKCα inhibitor. Ro 31-8220 robustly improved the rough-eye phenotype, reduced phosphorylated tau species in vitro and in vivo, reversed tau-induced memory impairment, and improved the fly motor functions. In a human neuroblastoma cell line, Ro 31-8220 reduced the PKC activity and the tau phosphorylation pattern, but we also have to acknowledge the compound's wide range of biological activity. Nevertheless, Ro 31-8220 is a novel therapeutic mitigator of tau-induced neurotoxocity.
MeSH term(s)	Animals ; Disease Models, Animal ; Drosophila melanogaster ; Drug Evaluation, Preclinical ; Frontotemporal Dementia/metabolism ; Indoles/pharmacology ; Neurofibrillary Tangles/drug effects ; Neurofibrillary Tangles/metabolism ; Neurons/drug effects ; Neurons/metabolism ; Phosphorylation/drug effects ; tau Proteins/metabolism
Chemical Substances	Indoles ; tau Proteins ; Ro 31-8220 (W9A0B5E78O)
Language	English
Publishing date	2019-06-22
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1211786-9
ISSN	1095-953X ; 0969-9961
ISSN (online)	1095-953X
ISSN	0969-9961
DOI	10.1016/j.nbd.2019.104519
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Article ; Online: V232M substitution restricts a distinct O-glycosylation of PLD3 and its neuroprotective function.

Demirev, Atanas Vladimirov / Song, Ha-Lim / Cho, Mi-Hyang / Cho, Kwangmin / Peak, Jong-Jin / Yoo, Hyun Ju / Kim, Dong-Hou / Yoon, Seung-Yong

Neurobiology of disease

2019 Volume 129, Page(s) 182–194

Abstract: The link between Val232Met variant of phospholipase D3 (PLD3) and late-onset Alzheimer's disease (AD) is still obscure. While it may not affect directly the amyloid precursor protein function, PLD3 could be regulating multiple cellular compartments. Here, ...

Abstract	The link between Val232Met variant of phospholipase D3 (PLD3) and late-onset Alzheimer's disease (AD) is still obscure. While it may not affect directly the amyloid precursor protein function, PLD3 could be regulating multiple cellular compartments. Here, we investigated the function of wild-type human PLD3 (PLD3
MeSH term(s)	Alzheimer Disease/genetics ; Alzheimer Disease/metabolism ; Animals ; Animals, Genetically Modified ; Drosophila melanogaster ; Genetic Predisposition to Disease ; Glycosylation ; Humans ; Mutation ; Neurons/metabolism ; Neurons/pathology ; Neuroprotection/physiology ; Phospholipase D/genetics ; Phospholipase D/metabolism ; Protein Transport
Chemical Substances	PLD3 protein, human (EC 3.1.4.4) ; Phospholipase D (EC 3.1.4.4)
Language	English
Publishing date	2019-05-20
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1211786-9
ISSN	1095-953X ; 0969-9961
ISSN (online)	1095-953X
ISSN	0969-9961
DOI	10.1016/j.nbd.2019.05.015
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