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Article ; Online: BAG2 prevents Tau hyperphosphorylation and increases p62/SQSTM1 in cell models of neurodegeneration.

Lima, Raquel S / Carrettiero, Daniel C / Ferrari, Merari F R

2022 Volume 49, Issue 8, Page(s) 7623–7635

Abstract: Background: Protein aggregates are pathological hallmarks of many neurodegenerative diseases, however the physiopathological role of these aggregates is not fully understood. Protein quality control has a pivotal role for protein homeostasis and depends ...

Abstract	Background: Protein aggregates are pathological hallmarks of many neurodegenerative diseases, however the physiopathological role of these aggregates is not fully understood. Protein quality control has a pivotal role for protein homeostasis and depends on specific chaperones. The co-chaperone BAG2 can target phosphorylated Tau for degradation by an ubiquitin-independent pathway, although its possible role in autophagy was not yet elucidated. In view of this, the aim of the present study was to investigate the association among protein aggregation, autophagy and BAG2 levels in cultured cells from hippocampus and locus coeruleus as well as in SH-SY5Y cell line upon different protein aggregation scenarios induced by rotenone, which is a flavonoid used as pesticide and triggers neurodegeneration. Methods and results: The present study showed that rotenone exposure at 0.3 nM for 48 h impaired autophagy prior to Tau phosphorylation at Ser199/202 in hippocampus but not in locus coeruleus cells, suggesting that distinct neuron cells respond differently to rotenone toxicity. Rotenone induced Tau phosphorylation at Ser199/202, together with a decrease in the endogenous BAG2 protein levels in SH-SY5Y and hippocampus cell culture, which indicates that rotenone and Tau hyperphosphorylation can affect this co-chaperone. Finally, it has been shown that BAG2 overexpression, increased p62/SQSTM1 levels in cells from hippocampus and locus coeruleus, stimulated LC3II recycling as well as prevented the raise of phosphorylated Tau at Ser199/202 in hippocampus. Conclusions: Results demonstrate a possible role for BAG2 in degradation pathways of specific substrates and its importance for the study of cellular aspects of neurodegenerative diseases.
MeSH term(s)	Humans ; Molecular Chaperones/metabolism ; Neuroblastoma ; Protein Aggregates ; Rotenone/pharmacology ; Sequestosome-1 Protein/genetics ; Sequestosome-1 Protein/metabolism ; tau Proteins/metabolism
Chemical Substances	BAG2 protein, human ; Molecular Chaperones ; Protein Aggregates ; SQSTM1 protein, human ; Sequestosome-1 Protein ; tau Proteins ; Rotenone (03L9OT429T)
Language	English
Publishing date	2022-05-25
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	186544-4
ISSN	1573-4978 ; 0301-4851
ISSN (online)	1573-4978
ISSN	0301-4851
DOI	10.1007/s11033-022-07577-w
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Article ; Online: Mitochondria-ER Tethering in Neurodegenerative Diseases.

Raeisossadati, Reza / Ferrari, Merari F R

Cellular and molecular neurobiology

2020 Volume 42, Issue 4, Page(s) 917–930

Abstract: Organelles juxtaposition has been detected for decades, although only recently gained importance due to a pivotal role in the regulation of cellular processes dependent on membrane contact sites. Endoplasmic reticulum (ER) and mitochondria interaction is ...

Abstract	Organelles juxtaposition has been detected for decades, although only recently gained importance due to a pivotal role in the regulation of cellular processes dependent on membrane contact sites. Endoplasmic reticulum (ER) and mitochondria interaction is a prime example of organelles contact sites. Mitochondria-associated membranes (MAM) are proposed to harbor ER-mitochondria tether complexes, mainly when these organelles are less than 30 nm apart. Dysfunctions of proteins located at the MAM are associated with neurodegenerative diseases such as Parkinson's, Alzheimer's and amyotrophic lateral sclerosis, as well as neurodevelopmental disorders; hence any malfunction in MAM can potentially trigger cell death. This review will focus on the role of ER-mitochondria contact sites, regarding calcium homeostasis, lipid metabolism, autophagy, morphology and dynamics of mitochondria, mainly in the context of neurodegenerative diseases. Approaches that have been employed so far to study organelles contact sites, as well as methods that were not used in neurosciences yet, but are promising and accurate ways to unveil the functions of MAM during neurodegeneration, is also discussed in the present review.
MeSH term(s)	Cell Death ; Endoplasmic Reticulum/metabolism ; Humans ; Mitochondria/metabolism ; Mitochondrial Membranes ; Neurodegenerative Diseases/metabolism
Language	English
Publishing date	2020-11-16
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	283404-2
ISSN	1573-6830 ; 0272-4340
ISSN (online)	1573-6830
ISSN	0272-4340
DOI	10.1007/s10571-020-01008-9
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Article ; Online: Parkin is downregulated among autophagy-related proteins prior to hyperphosphorylation of Tau in TS65DN mice.

Henrique, Alan M / Gianetti, Nathália G / Ferrari, Merari F R

Biochemical and biophysical research communications

2021 Volume 561, Page(s) 59–64

Abstract: Autophagy is a pathway through which cells execute a plethora of functions, such as macromolecules and organelles quality control, recycling of building blocks and apoptosis. Numerous studies have shown in the past that autophagy is an important ... ...

Abstract	Autophagy is a pathway through which cells execute a plethora of functions, such as macromolecules and organelles quality control, recycling of building blocks and apoptosis. Numerous studies have shown in the past that autophagy is an important mechanism associated with the pathology of various neurodegenerative diseases, whose impairment may lead to several disease-characteristic phenotypes (e.g. misfolded protein and defective organelles accumulation). With this in mind, we aimed to investigate whether alterations in expression of autophagy-related proteins would show before hyperphosphorylation of Tau, a hallmark of Alzheimer's disease (AD). After analyzing 7 different proteins, we observed that, while Pink1 and p62 show an age-related reduction in the Ts65Dn mice respectively in the locus coeruleus and hippocampus, Parkin shows an age-genotype interaction-associated reduction in both brain areas. This suggests potential outcomes in pathways associated with Parkin that could relate to later stages of the disease development.
MeSH term(s)	Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Animals ; Autophagy-Related Proteins/metabolism ; Disease Models, Animal ; Down Syndrome/metabolism ; Down Syndrome/pathology ; Down-Regulation ; Female ; Male ; Mice ; Mice, Transgenic ; Phosphorylation ; Ubiquitin-Protein Ligases/metabolism ; tau Proteins/metabolism
Chemical Substances	Autophagy-Related Proteins ; tau Proteins ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; parkin protein (EC 2.3.2.27)
Language	English
Publishing date	2021-05-18
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	205723-2
ISSN	1090-2104 ; 0006-291X ; 0006-291X
ISSN (online)	1090-2104 ; 0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2021.05.016
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Article: BAG2 prevents Tau hyperphosphorylation and increases p62/SQSTM1 in cell models of neurodegeneration

Lima, Raquel S. / Carrettiero, Daniel C. / Ferrari, Merari F. R.

Molecular biology reports. 2022 Aug., v. 49, no. 8

2022

Abstract: BACKGROUND: Protein aggregates are pathological hallmarks of many neurodegenerative diseases, however the physiopathological role of these aggregates is not fully understood. Protein quality control has a pivotal role for protein homeostasis and depends ... ...

Abstract	BACKGROUND: Protein aggregates are pathological hallmarks of many neurodegenerative diseases, however the physiopathological role of these aggregates is not fully understood. Protein quality control has a pivotal role for protein homeostasis and depends on specific chaperones. The co-chaperone BAG2 can target phosphorylated Tau for degradation by an ubiquitin-independent pathway, although its possible role in autophagy was not yet elucidated. In view of this, the aim of the present study was to investigate the association among protein aggregation, autophagy and BAG2 levels in cultured cells from hippocampus and locus coeruleus as well as in SH-SY5Y cell line upon different protein aggregation scenarios induced by rotenone, which is a flavonoid used as pesticide and triggers neurodegeneration. METHODS AND RESULTS: The present study showed that rotenone exposure at 0.3 nM for 48 h impaired autophagy prior to Tau phosphorylation at Ser199/202 in hippocampus but not in locus coeruleus cells, suggesting that distinct neuron cells respond differently to rotenone toxicity. Rotenone induced Tau phosphorylation at Ser199/202, together with a decrease in the endogenous BAG2 protein levels in SH-SY5Y and hippocampus cell culture, which indicates that rotenone and Tau hyperphosphorylation can affect this co-chaperone. Finally, it has been shown that BAG2 overexpression, increased p62/SQSTM1 levels in cells from hippocampus and locus coeruleus, stimulated LC3II recycling as well as prevented the raise of phosphorylated Tau at Ser199/202 in hippocampus. CONCLUSIONS: Results demonstrate a possible role for BAG2 in degradation pathways of specific substrates and its importance for the study of cellular aspects of neurodegenerative diseases.
Keywords	autophagy ; brain stem ; cell culture ; cell lines ; hippocampus ; homeostasis ; molecular biology ; neurodegenerative diseases ; neurons ; pesticides ; phosphorylation ; protein value ; quality control ; rotenone ; toxicity
Language	English
Dates of publication	2022-08
Size	p. 7623-7635.
Publishing place	Springer Netherlands
Document type	Article
ZDB-ID	186544-4
ISSN	1573-4978 ; 0301-4851
ISSN (online)	1573-4978
ISSN	0301-4851
DOI	10.1007/s11033-022-07577-w
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Article ; Online: Absence of Gem1 (mammalian Miro/Rhot) mitigates alpha-synuclein toxicity in a yeast model of Parkinson's disease.

Melo, Thaiany Q / Palma, Flavio R / Gomes, Fernando / Netto, Luis E S / Ferrari, Merari F R

Molecular and cellular neurosciences

2022 Volume 122, Page(s) 103757

Abstract: Alpha-synuclein aggregation is a hallmark of Parkinson's disease (PD). Mutants A30P and A53T alpha-synuclein are known to exacerbate the toxicity of alpha-synuclein, which includes oxidative stress, mitochondrial and endoplasmic reticulum (ER) ... ...

Abstract	Alpha-synuclein aggregation is a hallmark of Parkinson's disease (PD). Mutants A30P and A53T alpha-synuclein are known to exacerbate the toxicity of alpha-synuclein, which includes oxidative stress, mitochondrial and endoplasmic reticulum (ER) dysfunction. Saccharomyces cerevisiae (budding yeast) is a cellular model widely used to investigate mechanisms underlying neurodegenerative disorders, such as PD. In yeast, Gem1 (Miro/Rhot mammalian orthologue) coordinates mitochondrial dynamics and ER homeostasis, which is impaired in the presence of mutant alpha-synuclein and can lead to cell death. In this study, A30P or A53T alpha-synuclein were expressed in wild type or ΔGem (deletion of Gem1 gene) yeast strains. ΔGem cells presented decreased viability and increased mitochondrial H2O2 production and ER stress compared to wild type cells. However, in the presence of mutant alpha-synuclein, ΔGem cells showed increased growth compared to cells that do not express mutant alpha-synuclein. ΔGem cells expressing A53T alpha-synuclein also presented reduced ER stress and increased ability to deal with oxidative stress. Together, our results suggest that deletion of Gem1 activates pathways that strengthen cells against other stressful agents such as the presence of mutant alpha-synuclein.
MeSH term(s)	Animals ; Endoplasmic Reticulum/metabolism ; Hydrogen Peroxide ; Parkinson Disease/genetics ; Parkinson Disease/metabolism ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; alpha-Synuclein/genetics ; alpha-Synuclein/metabolism
Chemical Substances	GEM1 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; alpha-Synuclein ; Hydrogen Peroxide (BBX060AN9V)
Language	English
Publishing date	2022-07-16
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.2022.103757
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Zs.A 3035: Show issues

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Article: Parkin is downregulated among autophagy-related proteins prior to hyperphosphorylation of Tau in TS65DN mice

Henrique, Alan M / Gianetti, Nathália G / Ferrari, Merari F.R

Biochemical and biophysical research communications. 2021 July 05, v. 561

2021

Abstract	Autophagy is a pathway through which cells execute a plethora of functions, such as macromolecules and organelles quality control, recycling of building blocks and apoptosis. Numerous studies have shown in the past that autophagy is an important mechanism associated with the pathology of various neurodegenerative diseases, whose impairment may lead to several disease-characteristic phenotypes (e.g. misfolded protein and defective organelles accumulation). With this in mind, we aimed to investigate whether alterations in expression of autophagy-related proteins would show before hyperphosphorylation of Tau, a hallmark of Alzheimer's disease (AD). After analyzing 7 different proteins, we observed that, while Pink1 and p62 show an age-related reduction in the Ts65Dn mice respectively in the locus coeruleus and hippocampus, Parkin shows an age-genotype interaction-associated reduction in both brain areas. This suggests potential outcomes in pathways associated with Parkin that could relate to later stages of the disease development.
Keywords	Alzheimer disease ; apoptosis ; autophagy ; brain stem ; hippocampus ; organelles ; quality control ; research
Language	English
Dates of publication	2021-0705
Size	p. 59-64.
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.2021.05.016
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Article ; Online: Epigenetic regulation of retinal development.

Raeisossadati, Reza / Ferrari, Merari F R / Kihara, Alexandre Hiroaki / AlDiri, Issam / Gross, Jeffrey M

Epigenetics & chromatin

2021 Volume 14, Issue 1, Page(s) 11

Abstract: In the developing vertebrate retina, retinal progenitor cells (RPCs) proliferate and give rise to terminally differentiated neurons with exquisite spatio-temporal precision. Lineage commitment, fate determination and terminal differentiation are ... ...

Abstract	In the developing vertebrate retina, retinal progenitor cells (RPCs) proliferate and give rise to terminally differentiated neurons with exquisite spatio-temporal precision. Lineage commitment, fate determination and terminal differentiation are controlled by intricate crosstalk between the genome and epigenome. Indeed, epigenetic regulation plays pivotal roles in numerous cell fate specification and differentiation events in the retina. Moreover, aberrant chromatin structure can contribute to developmental disorders and retinal pathologies. In this review, we highlight recent advances in our understanding of epigenetic regulation in the retina. We also provide insight into several aspects of epigenetic-related regulation that should be investigated in future studies of retinal development and disease. Importantly, focusing on these mechanisms could contribute to the development of novel treatment strategies targeting a variety of retinal disorders.
MeSH term(s)	Cell Differentiation ; Epigenesis, Genetic ; Neurons ; Retina ; Stem Cells
Language	English
Publishing date	2021-02-09
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2462129-8
ISSN	1756-8935 ; 1756-8935
ISSN (online)	1756-8935
ISSN	1756-8935
DOI	10.1186/s13072-021-00384-w
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Article ; Online: Alpha-Synuclein Toxicity on Protein Quality Control, Mitochondria and Endoplasmic Reticulum.

Melo, Thaiany Quevedo / Copray, Sjef J C V M / Ferrari, Merari F R

Neurochemical research

2018 Volume 43, Issue 12, Page(s) 2212–2223

Abstract: Parkinson's disease (PD) is characterized by the presence of insoluble protein clusters containing α-synuclein. Impairment of mitochondria, endoplasmic reticulum, autophagy and intracellular trafficking proper function has been suggested to be caused by ... ...

Abstract	Parkinson's disease (PD) is characterized by the presence of insoluble protein clusters containing α-synuclein. Impairment of mitochondria, endoplasmic reticulum, autophagy and intracellular trafficking proper function has been suggested to be caused by α-synuclein toxicity, which is also associated with the higher levels of ROS found in the aged brain and in PD. Oxidative stress leads to protein oligomerization and aggregation that impair autophagy and mitochondrial dynamics leading to a vicious cycle of organelles damage and neurodegeneration. In this review we focused on the role of α-synuclein dysfunction as a cellular stressor that impairs mitochondria, endoplasmic reticulum, autophagy and cellular dynamics culminating with dopaminergic depletion and the pathogenesis of PD.
MeSH term(s)	Amino Acid Sequence ; Animals ; Autophagy/drug effects ; Autophagy/physiology ; Endoplasmic Reticulum/drug effects ; Endoplasmic Reticulum/genetics ; Endoplasmic Reticulum/metabolism ; Humans ; Mitochondria/drug effects ; Mitochondria/genetics ; Mitochondria/metabolism ; Oxidative Stress/drug effects ; Oxidative Stress/physiology ; Parkinson Disease/genetics ; Parkinson Disease/metabolism ; Protein Transport/physiology ; Reactive Oxygen Species/metabolism ; alpha-Synuclein/genetics ; alpha-Synuclein/metabolism ; alpha-Synuclein/toxicity
Chemical Substances	Reactive Oxygen Species ; alpha-Synuclein
Language	English
Publishing date	2018-10-28
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	199335-5
ISSN	1573-6903 ; 0364-3190
ISSN (online)	1573-6903
ISSN	0364-3190
DOI	10.1007/s11064-018-2673-x
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Zs.A 1368: Show issues

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Article ; Online: Restoration of Rab1 Levels Prevents Endoplasmic Reticulum Stress in Hippocampal Cells during Protein Aggregation Triggered by Rotenone.

Lima, Nathan C R / Melo, Thaiany Q / Sakugawa, Andressa Y S / Melo, Karla P / Ferrari, Merari F R

Neuroscience

2019 Volume 419, Page(s) 5–13

Abstract: Disrupted neuronal intracellular trafficking is often related with protein aggregates present in the brain during neurodegenerative diseases such as Alzheimer's. Impairment of intracellular transport may be related to Rab proteins, a class of small ... ...

Abstract	Disrupted neuronal intracellular trafficking is often related with protein aggregates present in the brain during neurodegenerative diseases such as Alzheimer's. Impairment of intracellular transport may be related to Rab proteins, a class of small GTPases responsible for trafficking of organelles and vesicles. Deficit in trafficking between the endoplasmic reticulum (ER) and Golgi apparatus mediated by Rab1 and 6 may lead to increased unfolded protein response (UPR) and ER stress and remodeling. Thus, the objective of this study is to analyze the levels of Rabs 1 and 6 in the hippocampus of aged rats and in vitro during protein aggregation promoted by exposure to rotenone. Levels of Rabs 1 and 6, ATF6 and CHOP were measured by western blotting. PDI immunolabeling and ER-Tracker were employed to study ER morphology. MTT was used to analyze cell metabolism. Rab1 levels and cell viability decreased, whereas Rab6, UPR proteins and ER remodeling increased during protein aggregation, which were restored to normal levels after exogenous expression of Rab1.These results suggest that decrease of Rab1 levels contributes to ER stress and remodeling, while maintaining the elevated expression of Rab1 prevented impairment of cell viability during protein aggregation. In conclusion, Rab1 is a significant player to maintain intracellular homeostasis and its expression may mitigate ER dysfunction in the context of neurodegeneration-related protein inclusions.
MeSH term(s)	Animals ; Cell Line ; Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum Stress/physiology ; Golgi Apparatus/metabolism ; Hippocampus/metabolism ; Neurons/metabolism ; Protein Aggregates ; Protein Transport/physiology ; Rats ; Rotenone/pharmacology ; rab1 GTP-Binding Proteins/metabolism
Chemical Substances	Protein Aggregates ; Rotenone (03L9OT429T) ; rab1 GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2019-09-03
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	196739-3
ISSN	1873-7544 ; 0306-4522
ISSN (online)	1873-7544
ISSN	0306-4522
DOI	10.1016/j.neuroscience.2019.08.050
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Article ; Online: microRNAs expression correlates with levels of APP, DYRK1A, hyperphosphorylated Tau and BDNF in the hippocampus of a mouse model for Down syndrome during ageing.

Chaves, Juliana C S / Machado, Felippe T / Almeida, Michael F / Bacovsky, Tatiana B / Ferrari, Merari F R

Neuroscience letters

2019 Volume 714, Page(s) 134541

Abstract: Down syndrome (DS) patients are more susceptible to Alzheimer's disease (AD) due to the presence of three copies of genes on chromosome 21 such as DYRK1A, which encodes a broad acting kinase, and APP (amyloid precursor protein), leading to formation of ... ...

Abstract	Down syndrome (DS) patients are more susceptible to Alzheimer's disease (AD) due to the presence of three copies of genes on chromosome 21 such as DYRK1A, which encodes a broad acting kinase, and APP (amyloid precursor protein), leading to formation of amyloid beta (Aβ) peptide and hyperphosphorylation of Tau. In this study, we investigated the association among miRNAs miR-17, -20a, -101, -106b, -199b, -26a, 26b and some of their target mRNAs such as APP, DYRK1A and BDNF, as well as the levels of hyperphosphorylated Tau in the hippocampus of a 2 and 5 months old mice model of trisomy 21 (Ts65Dn). Results indicated that increased APP expression in the hippocampus of 5 months old DS mice might be correlated with decrease in miR-17, -20a, -101 and -106b. Whereas at 2 months of age normal levels of APP expression in the hippocampus was correlated with increased levels of miR-17, -101 and -106b in DS mice. DYRK1A mRNA also increased in the hippocampus of 5 months old DS mice and it is associated with decreased levels of miR-199b. Increased levels of DYRK1A in 5-month old mice are associated with increased phosphorylation of Tau at Thr212 residue but not at Ser199-202. Tau pathology is accompanied by decreased expression of BDNF and increased miR-26a/b in mice of 5 months of age. Taken together, data indicate that miR-17, -20a, -26a/b, -101, -106b and -199b might be interesting targets to mitigate Tau and Aβ pathology in DS.
MeSH term(s)	Aging/metabolism ; Amyloid beta-Protein Precursor/biosynthesis ; Animals ; Brain-Derived Neurotrophic Factor/metabolism ; Disease Models, Animal ; Down Syndrome/metabolism ; Hippocampus/metabolism ; Mice ; MicroRNAs/biosynthesis ; Phosphorylation ; Protein Serine-Threonine Kinases/biosynthesis ; Protein-Tyrosine Kinases/biosynthesis ; tau Proteins/metabolism ; Dyrk Kinases
Chemical Substances	APP protein, mouse ; Amyloid beta-Protein Precursor ; Brain-Derived Neurotrophic Factor ; MicroRNAs ; tau Proteins ; Protein-Tyrosine Kinases (EC 2.7.10.1) ; Protein Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2019-10-09
Publishing country	Ireland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	194929-9
ISSN	1872-7972 ; 0304-3940
ISSN (online)	1872-7972
ISSN	0304-3940
DOI	10.1016/j.neulet.2019.134541
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