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Article ; Online: Autophagy and protein aggregation as a mechanism of dopaminergic degeneration in a primary human dopaminergic neuronal model

Cuevas, Elvis / Guzman, Aida / Burks, Susan M. / Ramirez-Lee, Alejandro / Ali, Syed F. / Imam, Syed Z.

Toxicology Reports. 2022, v. 9 p.806-813

2022

Abstract: The pathophysiology underlying the loss of dopaminergic neurons in Parkinson's disease (PD) is unclear. A gap of knowledge in the molecular and cellular events leading to degeneration of the nigrostriatal DA system is a major barrier to the development ... ...

Abstract	The pathophysiology underlying the loss of dopaminergic neurons in Parkinson's disease (PD) is unclear. A gap of knowledge in the molecular and cellular events leading to degeneration of the nigrostriatal DA system is a major barrier to the development of effective therapies for PD. 1-methyl-4-phenylpyridinium (MPP⁺) is used as a reliable in vitro model of PD in dopaminergic neurons; however, the molecular mechanisms that lead to cell death with this model are not fully understood. Additionally, there is a lack of translational in vitro models to fully understand progressive dopaminergic neurotoxicity. Here, we propose cultures of primary human dopaminergic neuronal precursor cells (HDNPCs) as a model to study progressive dopaminergic toxicity and neuronal damage in PD. We evaluated the concentration-response of MPP⁺ (0-10 mM) at 24 h, using cell viability and mitochondrial activity assays (LDH, XTT, Live/Dead staining, and MitoTracker). Based on concentration-response data, we chose two concentrations (1.0 and 2.5 mM) of MPP⁺ to evaluate markers of autophagy and dopaminergic status [tyrosine hydroxylase (TH)] after a 24-h exposure. Exposure to MPP⁺ induced cytotoxicity, reduced cell viability, and decreased mitochondrial activity. MPP⁺ at 1.0 and 2.5 mM also induced expression of lysosome-associated membrane protein 1 (LAMP-1) and increased the ratio of light chain 3 (LC3), LC3BII/LC3BI. The expression of TH also decreased. Furthermore, α-synuclein (α-SYN) and parkin were evaluated by immunofluorescence (IF) at 1.0 and 2.5 mM MPP⁺ after 24 h. A qualitative analysis revealed decreased parkin expression while α-SYN aggregation was observed in the cytoplasm and the nucleus. These data suggest that in HDNPCs MPP⁺ can cause cytotoxicity and neuronal damage. This damage may be mediated by autophagy, dopamine synthesis, and protein aggregation. The combination of HDNPCs and MPP⁺ may serve as valuable in vitro model of progressive dopaminergic neurotoxicity for research into potential treatments for PD.
Keywords	autophagy ; cell viability ; cytotoxicity ; dopamine ; fluorescent antibody technique ; humans ; membrane proteins ; mitochondria ; models ; neurons ; neurotoxicity ; pathophysiology ; qualitative analysis ; toxicology ; tyrosine 3-monooxygenase ; MPP+ ; Parkinson's disease ; In vitro model ; Protein aggregation
Language	English
Size	p. 806-813.
Publishing place	Elsevier B.V.
Document type	Article ; Online
Note	Use and reproduction
ZDB-ID	2805786-7
ISSN	2214-7500
ISSN	2214-7500
DOI	10.1016/j.toxrep.2022.03.047
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Can SARS-CoV-2 infect the central nervous system via the olfactory bulb or the blood-brain barrier?

Burks, Susan M / Rosas-Hernandez, Hector / Alejandro Ramirez-Lee, Manuel / Cuevas, Elvis / Talpos, John C

Brain, behavior, and immunity

2021 Volume 95, Page(s) 7–14

Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) emerged in Wuhan, China in December 2019. On February 11, the World Health Organization (WHO) announced the name for the new illness caused by SARS-CoV-2: COVID-19. By March 11, the outbreak of ...

Abstract	Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) emerged in Wuhan, China in December 2019. On February 11, the World Health Organization (WHO) announced the name for the new illness caused by SARS-CoV-2: COVID-19. By March 11, the outbreak of COVID-19 was declared a pandemic by the WHO. This virus has extensively altered daily life for many across the globe, while claiming hundreds of thousands of lives. While fundamentally a respiratory illness, many infected individuals experience symptoms that involve the central nervous system (CNS). It is likely that many of these symptoms are the result of the virus residing outside of the CNS. However, the current evidence does indicate that the SARS-CoV-2 virus can use olfactory neurons (or other nerve tracts) to travel from the periphery into the CNS, and that the virus may also enter the brain through the blood-brain barrier (BBB). We discuss how the virus may use established infection mechanisms (ACE2, NRP1, TMPRSS2, furin and Cathepsin L), as well mechanisms still under consideration (BASIGIN) to infect and spread throughout the CNS. Confirming the impact of the virus on the CNS will be crucial in dealing with the long-term consequences of the epidemic.
MeSH term(s)	Blood-Brain Barrier ; COVID-19 ; Central Nervous System ; China ; Humans ; Olfactory Bulb ; SARS-CoV-2
Language	English
Publishing date	2021-01-04
Publishing country	Netherlands
Document type	Journal Article ; Review
ZDB-ID	639219-2
ISSN	1090-2139 ; 0889-1591
ISSN (online)	1090-2139
ISSN	0889-1591
DOI	10.1016/j.bbi.2020.12.031
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Zs.A 2276: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Autophagy and protein aggregation as a mechanism of dopaminergic degeneration in a primary human dopaminergic neuronal model.

Cuevas, Elvis / Guzman, Aida / Burks, Susan M / Ramirez-Lee, Alejandro / Ali, Syed F / Imam, Syed Z

Toxicology reports

2022 Volume 9, Page(s) 806–813

Abstract	The pathophysiology underlying the loss of dopaminergic neurons in Parkinson's disease (PD) is unclear. A gap of knowledge in the molecular and cellular events leading to degeneration of the nigrostriatal DA system is a major barrier to the development of effective therapies for PD. 1-methyl-4-phenylpyridinium (MPP
Language	English
Publishing date	2022-04-01
Publishing country	Ireland
Document type	Journal Article
ZDB-ID	2805786-7
ISSN	2214-7500 ; 2214-7500
ISSN (online)	2214-7500
ISSN	2214-7500
DOI	10.1016/j.toxrep.2022.03.047
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Article ; Online: Downregulation of 14-3-3 Proteins in Alzheimer's Disease.

Gu, Qiang / Cuevas, Elvis / Raymick, James / Kanungo, Jyotshna / Sarkar, Sumit

Molecular neurobiology

2019 Volume 57, Issue 1, Page(s) 32–40

Abstract: One of the most abundant proteins expressed in the brain, 14-3-3 comprises about 1% of the brain's total soluble proteins. The 14-3-3 isoforms bind to specific phosphoserine- and phosphothreonine-containing motifs found on a variety of signaling proteins ...

Abstract	One of the most abundant proteins expressed in the brain, 14-3-3 comprises about 1% of the brain's total soluble proteins. The 14-3-3 isoforms bind to specific phosphoserine- and phosphothreonine-containing motifs found on a variety of signaling proteins (kinases and transcription factors, among others) to regulate a wide array of cellular processes including cell cycling, apoptosis, and autophagy. Previously, we described the expression of different 14-3-3 isoforms in the rat frontal cortex and reported their downregulation in a rodent model of neurodegeneration. To further investigate possible roles of 14-3-3 proteins in neurodegeneration, the present study examined different 14-3-3 isoforms in the frontal cortex of postmortem Alzheimer's disease (AD) patients and control subjects. Among the different 14-3-3 isoforms in the human frontal cortex, the relative abundance of expression is in the following order: 14-3-3-eta > tau > sigma > gamma > epsilon > zeta/delta > beta/alpha. These relative abundance levels of different 14-3-3 isoforms in human frontal cortex closely resemble those in rat frontal cortex, suggesting a conserved expression pattern of different 14-3-3 isoforms in mammalian species. In the AD samples, there was a significant decrease in total 14-3-3 levels and the 14-3-3-eta and 14-3-3-gamma isoforms, while no significant difference in the expression level of other 14-3-3 isoforms between AD and control brains was detected. Together, these results demonstrate an abundance of several 14-3-3 isoforms in the frontal cortex and that a downregulation of total 14-3-3 protein levels and specific 14-3-3 isoforms is associated with neurodegeneration. Given the known function of 14-3-3 proteins as inhibitors of apoptosis, the present results suggest that 14-3-3 proteins may play an important role in neurodegeneration and deserve further investigations into AD and other neurodegenerative disorders.
MeSH term(s)	14-3-3 Proteins/metabolism ; Aged ; Aged, 80 and over ; Alzheimer Disease/metabolism ; Brain/metabolism ; Down-Regulation/physiology ; Female ; Frontal Lobe/metabolism ; Humans ; Male ; Middle Aged ; Protein Isoforms/metabolism ; tau Proteins/metabolism
Chemical Substances	14-3-3 Proteins ; Protein Isoforms ; tau Proteins
Language	English
Publishing date	2019-09-05
Publishing country	United States
Document type	Journal Article
ZDB-ID	645020-9
ISSN	1559-1182 ; 0893-7648
ISSN (online)	1559-1182
ISSN	0893-7648
DOI	10.1007/s12035-019-01754-y
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Zs.A 2411: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

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Article ; Online: Stretch-Induced Deformation as a Model to Study Dopaminergic Dysfunction in Traumatic Brain Injury.

Rosas-Hernandez, Hector / Burks, Susan M / Cuevas, Elvis / Ali, Syed F

Neurochemical research

2019 Volume 44, Issue 11, Page(s) 2546–2555

Abstract: Traumatic brain injury (TBI) is defined as damage to the brain that consequently disrupts normal function. Neuronal death, a hallmark of TBI, has been related to the development of neurodegenerative disorders like Parkinson's disease (PD), where loss of ... ...

Abstract	Traumatic brain injury (TBI) is defined as damage to the brain that consequently disrupts normal function. Neuronal death, a hallmark of TBI, has been related to the development of neurodegenerative disorders like Parkinson's disease (PD), where loss of dopaminergic neurons and dopaminergic dysfunction are observed. To date, no in vitro model exists in which the dopaminergic damage observed in TBI is replicated. In this study, we evaluated the effects of in vitro simulated TBI on human dopaminergic neurons. To simulate TBI, neurons were subjected to 0%, 5%, 10%, 15%, 25% and 50% deformation. 24 h after injury, cell viability and apoptosis were determined by lactate dehydrogenase (LDH) release and DNA fragmentation, as well as ethidium homodimer and caspase 3/7 staining. Dopamine (DA) levels were determined by ELISA. Levels of tyrosine hydroxylase (TH) and DA transporter (DAT) were determined by western blot. Only 50% stretch increased LDH release and ethidium homodimer staining, suggesting the induction of necrosis. On the contrary, 25% and 50% stretch increased DNA fragmentation while 15%, 25% and 50% increased caspase 3/7 staining, suggesting that moderate and severe TBI promote apoptosis. Levels of intracellular DA decreased in a stretch-dependent manner with 15%, 25% and 50% stretch, which were related with a decrease in TH expression. Extracellular DA levels increased only at 50%. Levels of DAT remained unchanged regardless of treatment. These data support the use of stretch as a model to simulate TBI in vitro in human dopaminergic neurons, replicating the acute effects of TBI in the dopaminergic system.
MeSH term(s)	Apoptosis/physiology ; Brain Injuries, Traumatic/pathology ; Caspase 3/metabolism ; Caspase 7/metabolism ; DNA/metabolism ; DNA Fragmentation ; Dopamine/metabolism ; Dopaminergic Neurons/metabolism ; Dopaminergic Neurons/pathology ; Humans ; L-Lactate Dehydrogenase/metabolism ; Models, Biological ; Necrosis/physiopathology ; Trauma, Nervous System/metabolism ; Tyrosine 3-Monooxygenase/metabolism
Chemical Substances	DNA (9007-49-2) ; L-Lactate Dehydrogenase (EC 1.1.1.27) ; Tyrosine 3-Monooxygenase (EC 1.14.16.2) ; CASP3 protein, human (EC 3.4.22.-) ; CASP7 protein, human (EC 3.4.22.-) ; Caspase 3 (EC 3.4.22.-) ; Caspase 7 (EC 3.4.22.-) ; Dopamine (VTD58H1Z2X)
Language	English
Publishing date	2019-09-16
Publishing country	United States
Document type	Journal Article
ZDB-ID	199335-5
ISSN	1573-6903 ; 0364-3190
ISSN (online)	1573-6903
ISSN	0364-3190
DOI	10.1007/s11064-019-02872-8
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Zs.A 1368: 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)

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Article ; Online: Modification of methods to use Congo-red stain to simultaneously visualize amyloid plaques and tangles in human and rodent brain tissue sections.

Sarkar, Sumit / Raymick, James / Cuevas, Elvis / Rosas-Hernandez, Hector / Hanig, Joseph

Metabolic brain disease

2020 Volume 35, Issue 8, Page(s) 1371–1383

Abstract: Although there are multiple histochemical tracers available to label plaques and tangles in the brain to evaluate neuropathology in Alzheimer disease (AD), few of them are versatile in nature and compatible with immunohistochemical procedures. Congo Red ( ...

Abstract	Although there are multiple histochemical tracers available to label plaques and tangles in the brain to evaluate neuropathology in Alzheimer disease (AD), few of them are versatile in nature and compatible with immunohistochemical procedures. Congo Red (CR) is an anisotropic organic stain discovered to label amyloid beta (Aβ) plaques in the brain. Unfortunately, its use is underappreciated due to its low resolution and brightness as stated in previous studies using bright field microscopy. Here, we modified a previous method to localize both plaques and tangles in brains from humans and a transgenic rodent model of AD for fluorescence microscopic visualization. The plaque staining affinities displayed by CR were compared with fibrillar pattern labeling seen with Thioflavin S. This study summarizes the optimization of protocols in which various parameters have been finetuned. To determine the target CR potentially binds, we have performed double labeling with different antibodies against Aβ as well as phosphorylated Tau. The plaque staining affinities exhibited by CR are compared with those associated with the diffuse pattern of labeling seen with antibodies directed against different epitopes of Aβ. Neither CP13, TNT2 or TOC1 binds all the neurofibrillary tangles as revealed by CR labeling in the human brain. Additionally, we also evaluated double labeling with AT8, AT180, and PHF1. Interestingly, PHF-1 shows 40% colocalization and AT8 shows 15% colocalization with NFT. Thus, CR is a much better marker to detect AD pathologies in human and rodent brains with higher fluorescence intensity relative to other conventional fluorescence markers.
MeSH term(s)	Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Animals ; Brain/metabolism ; Brain/pathology ; Brain Chemistry/physiology ; Coloring Agents/analysis ; Coloring Agents/metabolism ; Congo Red/analysis ; Congo Red/metabolism ; Humans ; Mice ; Mice, Transgenic ; Neurofibrillary Tangles/chemistry ; Neurofibrillary Tangles/metabolism ; Neurofibrillary Tangles/pathology ; Optical Imaging/methods ; Plaque, Amyloid/chemistry ; Plaque, Amyloid/metabolism ; Plaque, Amyloid/pathology ; Rats ; Rodentia ; Staining and Labeling/methods
Chemical Substances	Coloring Agents ; Congo Red (3U05FHG59S)
Language	English
Publishing date	2020-08-27
Publishing country	United States
Document type	Journal Article
ZDB-ID	632824-6
ISSN	1573-7365 ; 0885-7490
ISSN (online)	1573-7365
ISSN	0885-7490
DOI	10.1007/s11011-020-00608-0
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Zs.A 2155: Show issues

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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)

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Article ; Online: Impaired Amyloid Beta Clearance and Brain Microvascular Dysfunction are Present in the Tg-SwDI Mouse Model of Alzheimer's Disease.

Rosas-Hernandez, Hector / Cuevas, Elvis / Raymick, James B / Robinson, Bonnie L / Sarkar, Sumit

Neuroscience

2020 Volume 440, Page(s) 48–55

Abstract: Alzheimer's disease (AD) pathology is characterized by amyloid plaques containing amyloid beta (Aβ) peptides, neurofibrillary tangles containing hyperphosphorylated tau protein, and neuronal loss. In addition, Aβ deposition in brain microvessels, known ... ...

Abstract	Alzheimer's disease (AD) pathology is characterized by amyloid plaques containing amyloid beta (Aβ) peptides, neurofibrillary tangles containing hyperphosphorylated tau protein, and neuronal loss. In addition, Aβ deposition in brain microvessels, known as cerebral amyloid angiopathy (CAA), increases blood-brain barrier (BBB) permeability and induces vascular dysfunction which aggravates AD pathology. The aim of the present study was to characterize neurovascular dysfunction in the Tg-SwDI mouse model of AD. Isolated brain capillaries from wild type (WT) and Tg-SwDI mice were used to evaluate the expression of monomeric and aggregated forms of Aβ, P-glycoprotein (P-gp), the receptor for advance glycation end-products (RAGE) and the tight junction (TJs) proteins occludin and claudin-5. Cultured brain endothelial cells were used to analyze barrier function via fluorescein flux. Isolated capillaries from Tg-SwDI mice contained increased levels of aggregated and oligomeric Aβ compared to WT animals. Isolated capillaries from Tg-SwDI had decreased levels of P-gp, which transports Aβ from brain to blood, and increased levels of RAGE, which transports Aβ from blood to brain. In addition, the TJ protein occludin was decreased in Tg-SwDI mice relative to WT mice, which correlated with an increase in BBB permeability in cultured brain endothelial cells. These findings demonstrated that Tg-SwDI mice exhibit Aβ aggregation that is due, in part, to impaired Aβ clearance driven by both a decrease in P-gp and increase in RAGE protein levels in brain capillaries. Aβ aggregation promotes a decrease in the expression of the TJ protein occludin, and as consequence an increase in BBB permeability.
MeSH term(s)	Alzheimer Disease ; Amyloid beta-Peptides/metabolism ; Animals ; Blood-Brain Barrier/metabolism ; Brain/metabolism ; Endothelial Cells/metabolism ; Mice ; Mice, Transgenic
Chemical Substances	Amyloid beta-Peptides
Language	English
Publishing date	2020-05-23
Publishing country	United States
Document type	Journal Article
ZDB-ID	196739-3
ISSN	1873-7544 ; 0306-4522
ISSN (online)	1873-7544
ISSN	0306-4522
DOI	10.1016/j.neuroscience.2020.05.024
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Zs.A 1215: Show issues

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ab Jg. 2022: Lesesaal (EG)

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Article ; Online: Characterization of Serum Exosomes from a Transgenic Mouse Model of Alzheimer's Disease.

Rosas-Hernandez, Hector / Cuevas, Elvis / Raymick, James B / Robinson, Bonnie L / Ali, Syed F / Hanig, Joseph / Sarkar, Sumit

Current Alzheimer research

2019 Volume 16, Issue 5, Page(s) 388–395

Abstract: Background: Alzheimer's Disease (AD) is the most common type of dementia characterized by amyloid plaques containing Amyloid Beta (Aβ) peptides and neurofibrillary tangles containing tau protein. In addition to neuronal loss, Cerebral Amyloid Angiopathy ...

Abstract	Background: Alzheimer's Disease (AD) is the most common type of dementia characterized by amyloid plaques containing Amyloid Beta (Aβ) peptides and neurofibrillary tangles containing tau protein. In addition to neuronal loss, Cerebral Amyloid Angiopathy (CAA) commonly occurs in AD. CAA is characterized by Aβ deposition in brain microvessels. Recent studies have suggested that exosomes (cell-derived vesicles containing a diverse cargo) may be involved in the pathogenesis of AD. Objective: Isolate and characterize brain-derived exosomes from a transgenic mouse model of AD that presents CAA. Methods: Exosomes were isolated from serum obtained from 13-month-old wild type and AD transgenic female mice using an exosome precipitation solution. Characterization of exosomal proteins was performed by western blots and dot blots. Results: Serum exosomes were increased in transgenic mice compared to wild types as determined by increased levels of the exosome markers flotillin and alix. High levels of neuronal markers were found in exosomes, without any difference any between the 2 groups. Markers for endothelial-derived exosomes were decreased in the transgenic model, while astrocytic-derived exosomes were increased. Exosome characterization showed increased levels of oligomeric Aβ and oligomeric and monomeric forms tau on the transgenic animals. Levels of amyloid precursor protein were also increased. In addition, pathological and phosphorylated forms of tau were detected, but no difference was observed between the groups. Conclusion: These data suggest that monomeric and oligomeric forms of Aβ and tau are secreted into serum via brain exosomes, most likely derived from astrocytes in the transgenic mouse model of AD with CAA. Studies on the implication of this event in the propagation of AD are underway.
MeSH term(s)	Alzheimer Disease/metabolism ; Amyloid beta-Peptides/metabolism ; Animals ; Disease Models, Animal ; Exosomes/metabolism ; Female ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; tau Proteins/metabolism
Chemical Substances	Amyloid beta-Peptides ; MAPT protein, human ; tau Proteins
Language	English
Publishing date	2019-03-21
Publishing country	United Arab Emirates
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	2205170-3
ISSN	1875-5828 ; 1567-2050
ISSN (online)	1875-5828
ISSN	1567-2050
DOI	10.2174/1567205016666190321155422
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Article ; Online: An Alternative In Vitro Method for Examining Nanoparticle-Induced Cytotoxicity.

Gu, Qiang / Cuevas, Elvis / Ali, Syed F / Paule, Merle G / Krauthamer, Victor / Jones, Yvonne / Zhang, Yongbin

International journal of toxicology

2019 Volume 38, Issue 5, Page(s) 385–394

Abstract: Conventional in vitro assays are often used as initial screens to identify potential toxic effects of nanoparticles (NPs). However, many NPs have shown interference with conventional in vitro assays, resulting in either false-positive or -negative ... ...

Abstract	Conventional in vitro assays are often used as initial screens to identify potential toxic effects of nanoparticles (NPs). However, many NPs have shown interference with conventional in vitro assays, resulting in either false-positive or -negative outcomes. Here, we report an alternative method for the in vitro assessment of NP-induced cytotoxicity utilizing Fluoro-Jade C (FJ-C). To provide proof of concept and initial validation data, Ag-NPs and Au-NPs were tested in 3 different cell cultures including rat brain microvessel endothelial cells, mouse neural stem cells, and the human SH-SY5Y cell line. Conventional 2,3-bis-(2-methoxy-4-nitro-5-sulfophenyl)-2H-tetrazolium-5-carboxanilide (XTT) and lactate dehydrogenase (LDH) assays were run in parallel with the new method and served as references. The results demonstrate for the first time that FJ-C labeling can be a useful tool for assessing NP-induced cytotoxicity in vitro. Using these approaches, it was also demonstrated that removal of Ag-NPs-while keeping the Ag-ions that were released from the Ag-NPs in culture media-abolished the measured cytotoxicity, indicating that Ag-NPs rather than Ag-ions in solution contributed to the observed cytotoxic effects. Further, co-treatment of Ag-NPs with N-acetyl cysteine (NAC) prevented the observed cytotoxicity, suggesting a protective role of NAC in Ag-NP-induced cytotoxicity. Thus, this alternative in vitro assay is well suited for identify potential cytotoxicity associated with exposure to NPs.
MeSH term(s)	Animals ; Biological Assay ; Cell Survival/drug effects ; Cells, Cultured ; Endothelial Cells/drug effects ; Fluoresceins ; Fluorescent Dyes ; Gold/toxicity ; Humans ; Male ; Metal Nanoparticles/toxicity ; Mice ; Microvessels/cytology ; Neural Stem Cells/drug effects ; Rats, Sprague-Dawley ; Silver/toxicity ; Toxicity Tests/methods
Chemical Substances	Fluoresceins ; Fluorescent Dyes ; fluoro jade ; Silver (3M4G523W1G) ; Gold (7440-57-5)
Language	English
Publishing date	2019-06-24
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	1379845-5
ISSN	1092-874X ; 1091-5818
ISSN (online)	1092-874X
ISSN	1091-5818
DOI	10.1177/1091581819859267
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Zs.A 1870: Show issues

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Article ; Online: Amyloid Beta 25-35 induces blood-brain barrier disruption in vitro.

Cuevas, Elvis / Rosas-Hernandez, Hector / Burks, Susan M / Ramirez-Lee, Manuel A / Guzman, Aida / Imam, Syed Z / Ali, Syed F / Sarkar, Sumit

Metabolic brain disease

2019 Volume 34, Issue 5, Page(s) 1365–1374

Abstract: The amyloid β-peptide (Aβ) is transported across the blood-brain barrier (BBB) by binding with the receptor for advanced glycation end products (RAGE). Previously, we demonstrated that the Aβ fraction 25-35 ( ... ...

Abstract	The amyloid β-peptide (Aβ) is transported across the blood-brain barrier (BBB) by binding with the receptor for advanced glycation end products (RAGE). Previously, we demonstrated that the Aβ fraction 25-35 (Aβ
MeSH term(s)	Amyloid beta-Peptides/pharmacology ; Animals ; Blood-Brain Barrier/drug effects ; Blood-Brain Barrier/metabolism ; Cell Survival/drug effects ; Endothelial Cells/drug effects ; Endothelial Cells/metabolism ; Glutathione Peroxidase/metabolism ; Male ; Mice ; Oxidative Stress/drug effects ; Peptide Fragments/pharmacology ; Rats ; Rats, Wistar ; Reactive Oxygen Species/metabolism ; Receptor for Advanced Glycation End Products/metabolism ; Tight Junction Proteins/metabolism
Chemical Substances	Amyloid beta-Peptides ; Peptide Fragments ; Reactive Oxygen Species ; Receptor for Advanced Glycation End Products ; Tight Junction Proteins ; amyloid beta-protein (25-35) ; Glutathione Peroxidase (EC 1.11.1.9)
Language	English
Publishing date	2019-07-02
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	632824-6
ISSN	1573-7365 ; 0885-7490
ISSN (online)	1573-7365
ISSN	0885-7490
DOI	10.1007/s11011-019-00447-8
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