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. 2018 Mar:46:76-82.
doi: 10.1016/j.jtemb.2017.11.012. Epub 2017 Nov 26.

Aluminium in brain tissue in autism

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Free article

Aluminium in brain tissue in autism

Matthew Mold et al. J Trace Elem Med Biol. 2018 Mar.
Free article

Abstract

Autism spectrum disorder is a neurodevelopmental disorder of unknown aetiology. It is suggested to involve both genetic susceptibility and environmental factors including in the latter environmental toxins. Human exposure to the environmental toxin aluminium has been linked, if tentatively, to autism spectrum disorder. Herein we have used transversely heated graphite furnace atomic absorption spectrometry to measure, for the first time, the aluminium content of brain tissue from donors with a diagnosis of autism. We have also used an aluminium-selective fluor to identify aluminium in brain tissue using fluorescence microscopy. The aluminium content of brain tissue in autism was consistently high. The mean (standard deviation) aluminium content across all 5 individuals for each lobe were 3.82(5.42), 2.30(2.00), 2.79(4.05) and 3.82(5.17) μg/g dry wt. for the occipital, frontal, temporal and parietal lobes respectively. These are some of the highest values for aluminium in human brain tissue yet recorded and one has to question why, for example, the aluminium content of the occipital lobe of a 15year old boy would be 8.74 (11.59) μg/g dry wt.? Aluminium-selective fluorescence microscopy was used to identify aluminium in brain tissue in 10 donors. While aluminium was imaged associated with neurones it appeared to be present intracellularly in microglia-like cells and other inflammatory non-neuronal cells in the meninges, vasculature, grey and white matter. The pre-eminence of intracellular aluminium associated with non-neuronal cells was a standout observation in autism brain tissue and may offer clues as to both the origin of the brain aluminium as well as a putative role in autism spectrum disorder.

Keywords: Aluminium-selective fluorescence microscopy; Autism spectrum disorder; Human brain tissue; Human exposure to aluminium; Transversely heated atomic absorption spectrometry.

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Review
. 2015 Apr:30:90-5.
doi: 10.1016/j.jtemb.2014.11.002. Epub 2014 Nov 20.

The binding, transport and fate of aluminium in biological cells

Affiliations
Review

The binding, transport and fate of aluminium in biological cells

Christopher Exley et al. J Trace Elem Med Biol. 2015 Apr.

Abstract

Aluminium is the most abundant metal in the Earth's crust and yet, paradoxically, it has no known biological function. Aluminium is biochemically reactive, it is simply that it is not required for any essential process in extant biota. There is evidence neither of element-specific nor evolutionarily conserved aluminium biochemistry. This means that there are no ligands or chaperones which are specific to its transport, there are no transporters or channels to selectively facilitate its passage across membranes, there are no intracellular storage proteins to aid its cellular homeostasis and there are no pathways which evolved to enable the metabolism and excretion of aluminium. Of course, aluminium is found in every compartment of every cell of every organism, from virus through to Man. Herein we have investigated each of the 'silent' pathways and metabolic events which together constitute a form of aluminium homeostasis in biota, identifying and evaluating as far as is possible what is known and, equally importantly, what is unknown about its uptake, transport, storage and excretion.

Keywords: Aluminium in biology; Cell biochemistry; Metal binding; Metal storage; Metal transport.

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. 2018 Aug 18;15(8):1777.
doi: 10.3390/ijerph15081777.

Aluminium in Brain Tissue in Multiple Sclerosis

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Aluminium in Brain Tissue in Multiple Sclerosis

Matthew Mold et al. Int J Environ Res Public Health. .

Abstract

Multiple sclerosis (MS) is a devastating and debilitating neurodegenerative disease of unknown cause. A consensus suggests the involvement of both genetic and environmental factors of which the latter may involve human exposure to aluminium. There are no data on the content and distribution of aluminium in human brain tissue in MS. The aluminium content of brain tissue from 14 donors with a diagnosis of MS was determined by transversely heated graphite furnace atomic absorption spectrometry. The location of aluminium in the brain tissue of two donors was investigated by aluminium-specific fluorescence microscopy. The aluminium content of brain tissue in MS was universally high with many tissues bearing concentrations in excess of 10 μg/g dry wt. (10 ppm) and some exceeding 50 ppm. There were no statistically significant relationships between brain lobes, donor age or donor gender. Aluminium-specific fluorescence successfully identified aluminium in brain tissue in both intracellular and extracellular locations. The association of aluminium with corpora amylacea suggests a role for aluminium in neurodegeneration in MS.

Keywords: TH GFAAS; aluminium-specific fluorescence; human brain tissue; human exposure to aluminium; multiple sclerosis.

Conflict of interest statement

The authors declare no conflicts of interest.

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. 2020;73(4):1627-1635.
doi: 10.3233/JAD-191140.

Aluminum and Amyloid-β in Familial Alzheimer's Disease

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Free article

Aluminum and Amyloid-β in Familial Alzheimer's Disease

Matthew Mold et al. J Alzheimers Dis. 2020.
Free article

Abstract

Genetic predispositions associated with metabolism of the amyloid-β protein precursor underlie familial Alzheimer's disease; a form of dementia characterized by early disease onset and elevated levels of cortical amyloid-β. Human exposure to aluminum is linked to the etiology of Alzheimer's disease and recent research measured a high content of aluminum in brain tissue in familial Alzheimer's disease. To elaborate upon this finding, we have obtained brain tissues from a Colombian cohort of donors with familial Alzheimer's disease. We have used established methods to measure the aluminum content of these tissues and we have compared the data with a recently measured dataset for control brain tissues. We report significantly higher levels of aluminum in brain tissues in donors with familial Alzheimer's disease than in control tissues from donors without neurological impairment or neurodegeneration. We have used aluminum-specific fluorescence microscopy along with complementary imaging for amyloid-β to demonstrate a very high degree of co-localization of these two risk factors in brain tissue in familial Alzheimer's disease. Aluminum and amyloid-β were co-located in senile plaques as well as vasculature, the latter resembling cerebral amyloid angiopathy. Aluminum was also found separately from amyloid-β in intracellular compartments including glia and neuronal axons. The research has identified an arguably unique association between high brain aluminum content and amyloid-β and allows postulation that genetic predispositions defining familial Alzheimer's disease underlie this relationship.

Keywords: Aluminum in human brain tissue; amyloid-β; familial Alzheimer’s disease; human exposure to aluminum.

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Observational Study
. 2022 Jan 27;12(1):1465.
doi: 10.1038/s41598-022-05627-8.

Aluminium co-localises with Biondi ring tangles in Parkinson's disease and epilepsy

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Observational Study

Aluminium co-localises with Biondi ring tangles in Parkinson's disease and epilepsy

Matthew John Mold et al. Sci Rep. .

Abstract

Aluminium is known to accumulate in neuropathological hallmarks. However, such has only tentatively been suggested in Biondi ring tangles. Owing to their intracellular and filamentous structure rich in β-pleated sheets, Biondi ring tangles might attract the adventitious binding of aluminium in regions of the blood-cerebrospinal fluid barrier. The study's objective was to establish whether aluminium co-localises with Biondi ring tangles in the brains of Parkinson's disease donors versus a donor that went on to develop late-onset epilepsy. Herein, we have performed immunohistochemistry for phosphorylated tau, complemented with aluminium-specific fluorescence microscopy in the choroid plexus of Parkinson's disease donors and in a donor that developed late-onset epilepsy. Aluminium co-localises with lipid-rich Biondi ring tangles in the choroid plexus. While Biondi ring tangles are not composed of phosphorylated tau, the latter is identified in nuclei of choroidal cells where aluminium and Biondi ring tangles are co-located. Although Biondi ring tangles are considered artefacts in imaging studies using positron emission tomography, their ability to bind aluminium and then release it upon their subsequent rupture and escape from choroidal cells may allow for a mechanism that may propagate for aluminium toxicity in vivo.

Conflict of interest statement

The authors declare no competing interests.

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. 2019 Dec;24(8):1279-1282.
doi: 10.1007/s00775-019-01710-0. Epub 2019 Aug 29.

Aluminium in human brain tissue: how much is too much?

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Aluminium in human brain tissue: how much is too much?

Christopher Exley et al. J Biol Inorg Chem. 2019 Dec.

Erratum in

Abstract

A burgeoning body of research confirms and affirms the presence of aluminium in human brain tissue. Recently, the first data on aluminium content of brain tissue from donors with diagnoses of familial Alzheimer's disease, autism spectrum disorder, multiple sclerosis and epilepsy have been published. Quantitative data are supported by aluminium-specific fluorescence microscopy identifying the locations of aluminium in human brain tissue. The challenge in the future will be to confirm or refute the role played by brain aluminium intoxication in human neurodegenerative disease.

Keywords: Aluminium in brain tissue; Aluminium-specific fluorescence microscopy; Alzheimer’s disease; Autism; Epilepsy; Multiple sclerosis; Neurodegenerative disease.

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. 2023 Aug 31;14(1):5294.
doi: 10.1038/s41467-023-41064-5.

Screening non-conventional yeasts for acid tolerance and engineering Pichia occidentalis for production of muconic acid

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Screening non-conventional yeasts for acid tolerance and engineering Pichia occidentalis for production of muconic acid

Michael E Pyne et al. Nat Commun. .

Abstract

Saccharomyces cerevisiae is a workhorse of industrial biotechnology owing to the organism's prominence in alcohol fermentation and the suite of sophisticated genetic tools available to manipulate its metabolism. However, S. cerevisiae is not suited to overproduce many bulk bioproducts, as toxicity constrains production at high titers. Here, we employ a high-throughput assay to screen 108 publicly accessible yeast strains for tolerance to 20 g L-1 adipic acid (AA), a nylon precursor. We identify 15 tolerant yeasts and select Pichia occidentalis for production of cis,cis-muconic acid (CCM), the precursor to AA. By developing a genome editing toolkit for P. occidentalis, we demonstrate fed-batch production of CCM with a maximum titer (38.8 g L-1), yield (0.134 g g-1 glucose) and productivity (0.511 g L-1 h-1) that surpasses all metrics achieved using S. cerevisiae. This work brings us closer to the industrial bioproduction of AA and underscores the importance of host selection in bioprocessing.

Conflict of interest statement

The authors declare no competing interests.

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. 2018 Nov 7:14:80.
doi: 10.1186/s13223-018-0305-2. eCollection 2018.

Unraveling the enigma: elucidating the relationship between the physicochemical properties of aluminium-based adjuvants and their immunological mechanisms of action

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Review

Unraveling the enigma: elucidating the relationship between the physicochemical properties of aluminium-based adjuvants and their immunological mechanisms of action

Emma Shardlow et al. Allergy Asthma Clin Immunol. .

Abstract

Aluminium salts are by far the most commonly used adjuvants in vaccines. There are only two aluminium salts which are used in clinically-approved vaccines, Alhydrogel® and AdjuPhos®, while the novel aluminium adjuvant used in Gardasil® is a sulphated version of the latter. We have investigated the physicochemical properties of these two aluminium adjuvants and specifically in milieus approximating to both vaccine vehicles and the composition of injection sites. Additionally we have used a monocytic cell line to establish the relationship between their physicochemical properties and their internalisation and cytotoxicity. We emphasise that aluminium adjuvants used in clinically approved vaccines are chemically and biologically dissimilar with concomitantly potentially distinct roles in vaccine-related adverse events.

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. 2018 Feb 5;8(1):2437.
doi: 10.1038/s41598-018-20845-9.

Intracellular tracing of amyloid vaccines through direct fluorescent labelling

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Intracellular tracing of amyloid vaccines through direct fluorescent labelling

Matthew Mold et al. Sci Rep. .

Abstract

Alzheimer's disease is a debilitating neurodegenerative condition that progressively causes synaptic loss and major neuronal damage. Immunotherapy utilising Aβ as an active immunogen or via passive treatment utilising antibodies raised to amyloid have shown therapeutic promise. The migratory properties of peripheral blood-borne monocytes and their ability to enter the central nervous system, suggests a beneficial role in mediating tissue damage and neuroinflammation. However, the intrinsic phagocytic properties of such cells have pre-disposed them to internalise misfolded amyloidogenic peptides that could act as seeds capable of nucleating amyloid formation in the brain. Mechanisms governing the cellular fate of amyloid therefore, may prove to be key in the development of future vaccination regimes. Herein, we have developed unequivocal and direct conformation-sensitive fluorescent molecular probes that reveal the intracytoplasmic and intranuclear persistence of amyloid in a monocytic T helper 1 (THP-1) cell line. Use of the pathogenic Aβ42 species as a model antigen in simulated vaccine formulations suggested differing mechanisms of cellular internalisation, in which fibrillar amyloid evaded lysosomal capture, even when co-deposited on particulate adjuvant materials. Taken collectively, direct fluorescent labelling of antigen-adjuvant complexes may serve as critical tools in understanding subsequent immunopotentiation in vaccines directed against amyloidosis and wider dementia.

Conflict of interest statement

The authors declare that they have no competing interests.

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. 2020 Apr 25;6(4):e03839.
doi: 10.1016/j.heliyon.2020.e03839. eCollection 2020 Apr.

Imaging of aluminium and amyloid β in neurodegenerative disease

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Imaging of aluminium and amyloid β in neurodegenerative disease

Christopher Exley et al. Heliyon. .

Abstract

Objectives: Recent research has confirmed the presence of aluminium in human brain tissue. Quantitative analyses suggest increased brain aluminium content in a number of neurodegenerative diseases including familial Alzheimer's disease, congophilic amyloid angiopathy, epilepsy and autism. Complementary aluminium-specific fluorescence microscopy identifies the location of aluminium in human brain tissue and demonstrates significant differences in distribution between diseases. Herein we combine these approaches in investigating associations between aluminium in human brain tissue and specific disease-associated neuropathologies.

Methods: We have used aluminium-specific fluorescence microscopy, Congo red staining using light and polarised light and thioflavin S fluorescence microscopy on serial sections of brain tissues to identify co-localisation of aluminium and amyloid β and tau neuropathology.

Results: A combination of light, polarised and fluorescence microscopy demonstrates an intimate relationship between aluminium and amyloid β in familial Alzheimer's disease but not in other conditions and diseases, such as congophilic amyloid angiopathy and autism. We demonstrate preliminary evidence of amyloid β pathology, including associations with vasculature and parenchymal tissues, in autism in tissues heavily loaded with aluminium.

Conclusion: We suggest that complementary aluminium-specific fluorescence microscopy may reveal important information about the putative toxicity of aluminium in neurodegenerative and neurodevelopmental disorders.

Keywords: Aluminium in brain tissue; Aluminium-specific fluorescence microscopy; Alzheimer's disease; Autism; Congophilic amyloid angiopathy; Epilepsy; Health sciences; Neuroscience.

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. 2021 Apr 9;5(1):283-294.
doi: 10.3233/ADR-210011.

Aluminum and Tau in Neurofibrillary Tangles in Familial Alzheimer's Disease

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Aluminum and Tau in Neurofibrillary Tangles in Familial Alzheimer's Disease

Matthew John Mold et al. J Alzheimers Dis Rep. .

Abstract

Background: Familial Alzheimer's disease (fAD) is driven by genetic predispositions affecting the expression and metabolism of the amyloid-β protein precursor. Aluminum is a non-essential yet biologically-reactive metal implicated in the etiology of AD. Recent research has identified aluminum intricately and unequivocally associated with amyloid-β in senile plaques and, more tentatively, co-deposited with neuropil-like threads in the brains of a Colombian cohort of donors with fAD.

Objective: Herein, we have assessed the co-localization of aluminum to immunolabelled phosphorylated tau to probe the potential preferential binding of aluminum to senile plaques or neurofibrillary tangles in the same Colombian kindred.

Methods: Herein, we have performed phosphorylated tau-specific immunolabelling followed by aluminum-specific fluorescence microscopy of the identical brain tissue sections via a sequential labelling method.

Results: Aluminum was co-localized with immunoreactive phosphorylated tau in the brains of donors with fAD. While aluminum was predominantly co-located to neurofibrillary tangles in the temporal cortex, aluminum was more frequently co-deposited with cortical senile plaques.

Conclusion: These data suggest that the co-deposition of aluminum with amyloid-β precedes that with neurofibrillary tangles. Extracellularly deposited amyloid-β may also be more immediately available to bind aluminum versus intracellular aggregates of tau. Therapeutic approaches to reduce tau have demonstrated the amelioration of its synergistic interactions with amyloid-β, ultimately reducing tau pathology and reducing neuronal loss. These data support the intricate associations of aluminum in the neuropathology of fAD, of which its subsequent reduction may further therapeutic benefits observed in ongoing clinical trials in vivo.

Keywords: Aluminum in human brain tissue; amyloid-β; familial Alzheimer’s disease; neurofibrillary tangles; senile plaques; tau.

Conflict of interest statement

The authors have no conflict of interest to report.

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. 2014 Dec:50:43-8.
doi: 10.1016/j.reprotox.2014.10.001. Epub 2014 Oct 14.

Aluminum content of human semen: implications for semen quality

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Aluminum content of human semen: implications for semen quality

J P Klein et al. Reprod Toxicol. 2014 Dec.

Abstract

A deterioration of human semen quality has been observed over recent decades. A possible explanation could be an increased exposure to environmental pollutants, including aluminum. Our aim was to measure the aluminum concentration in the semen of 62 patients and to carry out a preliminary evaluation on its impact on specific semen parameters. For each patient, semen analyses were performed according to WHO guidelines. A graphite furnace atomic absorption spectrometry method was used to determine semen aluminum concentration. A cytological analysis using an aluminum-specific fluor, lumogallion, was also performed. The mean aluminum concentration in human semen was 339 μg/L. Patients with oligozoospermia had a statistically higher aluminum concentration than others. No significant difference was observed for other semen parameters. Cytological analysis showed the presence of aluminum in spermatozoa. This study provided unequivocal evidence of high concentrations of aluminum in human semen and suggested possible implications for spermatogenesis and sperm count.

Keywords: Aluminum; Environmental effects; Male infertility; Sperm analysis.

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. 2019 May;56(3):418-428.
doi: 10.1177/0300985818809142. Epub 2018 Oct 31.

Granulomas Following Subcutaneous Injection With Aluminum Adjuvant-Containing Products in Sheep

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Granulomas Following Subcutaneous Injection With Aluminum Adjuvant-Containing Products in Sheep

Javier Asín et al. Vet Pathol. 2019 May.

Abstract

The use of vaccines including aluminum (Al)-based adjuvants is widespread among small ruminants and other animals. They are associated with the appearance of transient injection site nodules corresponding to granulomas. This study aims to characterize the morphology of these granulomas, to understand the role of the Al adjuvant in their genesis, and to establish the presence of the metal in regional lymph nodes. A total of 84 male neutered lambs were selected and divided into 3 treatment groups of 28 animals each: (1) vaccine (containing Al-based adjuvant), (2) adjuvant-only, and (3) control. A total of 19 subcutaneous injections were performed in a time frame of 15 months. Granulomas and regional lymph nodes were evaluated by clinicopathological means. All of the vaccine and 92.3% of the adjuvant-only lambs presented injection-site granulomas; the granulomas were more numerous in the group administered the vaccine. Bacterial culture in granulomas was always negative. Histologically, granulomas in the vaccine group presented a higher degree of severity. Al was specifically identified by lumogallion staining in granulomas and lymph nodes. Al median content was significantly higher ( P < .001) in the lymph nodes of the vaccine group (82.65 μg/g) compared with both adjuvant-only (2.53 μg/g) and control groups (0.96 μg/g). Scanning transmission electron microscopy demonstrated aggregates of Al within macrophages in vaccine and adjuvant-only groups. In these two groups, Al-based adjuvants induce persistent, sterile, subcutaneous granulomas with macrophage-driven translocation of Al to regional lymph nodes. Local translocation of Al may induce further accumulation in distant tissues and be related to the appearance of systemic signs.

Keywords: aluminum-based adjuvants; granuloma; lymph node; macrophage; sheep; vaccine.

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. 2021 Feb 17;13(1):45.
doi: 10.1186/s13195-021-00780-0.

CERTL reduces C16 ceramide, amyloid-β levels, and inflammation in a model of Alzheimer's disease

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CERTL reduces C16 ceramide, amyloid-β levels, and inflammation in a model of Alzheimer's disease

Simone M Crivelli et al. Alzheimers Res Ther. .

Abstract

Background: Dysregulation of ceramide and sphingomyelin levels have been suggested to contribute to the pathogenesis of Alzheimer's disease (AD). Ceramide transfer proteins (CERTs) are ceramide carriers which are crucial for ceramide and sphingomyelin balance in cells. Extracellular forms of CERTs co-localize with amyloid-β (Aβ) plaques in AD brains. To date, the significance of these observations for the pathophysiology of AD remains uncertain.

Methods: A plasmid expressing CERTL, the long isoform of CERTs, was used to study the interaction of CERTL with amyloid precursor protein (APP) by co-immunoprecipitation and immunofluorescence in HEK cells. The recombinant CERTL protein was employed to study interaction of CERTL with amyloid-β (Aβ), Aβ aggregation process in presence of CERTL, and the resulting changes in Aβ toxicity in neuroblastoma cells. CERTL was overexpressed in neurons by adeno-associated virus (AAV) in a mouse model of familial AD (5xFAD). Ten weeks after transduction, animals were challenged with behavior tests for memory, anxiety, and locomotion. At week 12, brains were investigated for sphingolipid levels by mass spectrometry, plaques, and neuroinflammation by immunohistochemistry, gene expression, and/or immunoassay.

Results: Here, we report that CERTL binds to APP, modifies Aβ aggregation, and reduces Aβ neurotoxicity in vitro. Furthermore, we show that intracortical injection of AAV, mediating the expression of CERTL, decreases levels of ceramide d18:1/16:0 and increases sphingomyelin levels in the brain of male 5xFAD mice. CERTL in vivo over-expression has a mild effect on animal locomotion, decreases Aβ formation, and modulates microglia by decreasing their pro-inflammatory phenotype.

Conclusion: Our results demonstrate a crucial role of CERTL in regulating ceramide levels in the brain, in amyloid plaque formation and neuroinflammation, thereby opening research avenues for therapeutic targets of AD and other neurodegenerative diseases.

Keywords: 5xFAD; Adeno-associated virus (AAV); Alzheimer’s disease (AD); Amyloid-β plaques; Ceramide; Ceramide transporter protein (CERT); Microglia; Neuroinflammation; Sphingomyelin.

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The authors declare that they have no competing interests.

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. 2014 Sep 5:4:6287.
doi: 10.1038/srep06287.

Unequivocal identification of intracellular aluminium adjuvant in a monocytic THP-1 cell line

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Unequivocal identification of intracellular aluminium adjuvant in a monocytic THP-1 cell line

Matthew Mold et al. Sci Rep. .

Abstract

Aluminium-based adjuvants (ABA) are the predominant adjuvants used in human vaccinations. While a consensus is yet to be reached on the aetiology of the biological activities of ABA several studies have identified shape, crystallinity and size as critical factors affecting their adjuvanticity. In spite of recent advances, the fate of ABA following their administration remains unclear. Few if any studies have demonstrated the unequivocal presence of intracellular ABA. Herein we demonstrate for the first time the unequivocal identification of ABA within a monocytic T helper 1 (THP-1) cell line, using lumogallion as a fluorescent molecular probe for aluminium. Use of these new methods revealed that particulate ABA was only found in the cell cytoplasm. Transmission electron microscopy revealed that ABA were contained within vesicle-like structures of approximately 0.5-1 μm in diameter.

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. 2011 Aug;9(8):577-9.
doi: 10.1586/eri.11.73.

New insights into pathogen recognition

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New insights into pathogen recognition

Paola Quattroni et al. Expert Rev Anti Infect Ther. 2011 Aug.

Abstract

The Society for General Microbiology (SGM) Spring Conference covers a range of topics of microbiology and comprises mixed sessions including symposia, workshops, debates, offered papers and invited presentations from international experts. This year the SGM Conference was held 11-14 April 2011 at the Harrogate Conference Centre in Harrogate, Yorkshire (UK). The main aim of the meeting is generally to provide a variety of programs that reflect current knowledge on different topics and introduce the recent advances in general and applied microbiology. Aspects of microbial recognition and interaction with the host immune response were addressed during a session of the meeting, where leaders in the field highlighted how the immune system is designed to recognize and destroy microorganisms by detecting microbial signature molecules (pathogen-associated molecular patterns) via interaction with specific receptors. This article focuses on the current research on pathogen recognition by the host through the interaction with surface structures present on microorganisms, with particular interest on the family of lectins, an emerging area in the understanding of infectious diseases. Discovering the mechanisms used by bacteria to survive in the host environment and at the same time elucidating the processes by which the immune system interacts with pathogens is vital for the development of vaccines and the design of new therapies.

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