Aluminum does not enhance β-amyloid toxicity in rat hippocampal cultures

Nday, Christiane M.; Drever, Benjamin D.; Salifoglou, Thanos; Platt, Bettina

doi:10.1016/j.brainres.2010.07.008

Cited by 10 publications

(7 citation statements)

References 83 publications

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“…The Nday et al (2010) conclusion appears to conflict with that by Drago et al (2007) who reported reduced survival of cultured rat endothelial cells after treatment with rat or human Aβ 1–42 and that cytotoxicity was enhanced after exposure to human Aβ-Al. The Nday (2010a) conclusion is also at odds with that by Drago et al (2008) who compared the viability and morphology of cultured human neuroblastoma cells treated with synthetic Aβ 1–42 or Aβ-Al, Aβ-Cu, Aβ-Fe or Aβ-Zn conjugates (prepared via Aβ-binding with bare ions to yield monometalated molecules).…”

Section: Organ Systems and Functionmentioning

confidence: 60%

“…The Nday (2010a) conclusion is also at odds with that by Drago et al (2008) who compared the viability and morphology of cultured human neuroblastoma cells treated with synthetic Aβ 1–42 or Aβ-Al, Aβ-Cu, Aβ-Fe or Aβ-Zn conjugates (prepared via Aβ-binding with bare ions to yield monometalated molecules). Unlike Nday et al (2010) who found native Aβ 1–40 was cytotoxic for rat primary hippocampal neurons after 96 h incubation, Drago and associates (2008) found no significant toxicity of synthetic Aβ 1–42 in transformed human neuroblastoma cells after 24 h in culture. Notably, of the Aβ 1–42 metal conjugates only the Aβ-Al reduced cell survival.…”

Section: Organ Systems and Functionmentioning

confidence: 96%

“…For example, Nday et al (2010) cultured Sprague-Dawly rat hippocampal cells with 0, 10, 100, or 500 μM Al +3 (as AlCl 3 ). Neuronal dendrite skrinkage and lethality increased with concentration and duration of exposure and neurons were far more susceptible than glial cells.…”

Section: Organ Systems and Functionmentioning

confidence: 99%

“…Notably, of the Aβ 1–42 metal conjugates only the Aβ-Al reduced cell survival. It is not clear whether the differences between the results from Nday et al (2010) and Drago et al (2008) are due to the specific nature of the N2a-produced Aβ 1–40 compared to the synthetic Aβ 1–42 , to different culture conditions and durations of exposure, or to differential uptake of Aβ 1–40 and Aβ 1–42 by primary and transformed cells. While Aβ 1–40 incubation with rat neurons and glial cells was prolonged (4 days) and fluorescent stains were used to measure polymerized tubulin, Nday et al (2010) made no confirmation by ElISA or other means to determine the extent of mouse N2a-generated Aβ 1–40 uptake into cultured rat hippocampal cells.…”

Section: Organ Systems and Functionmentioning

confidence: 99%

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Systematic review of potential health risks posed by pharmaceutical, occupational and consumer exposures to metallic and nanoscale aluminum, aluminum oxides, aluminum hydroxide and its soluble salts

Willhite¹,

Karyakina²,

Yokel³

et al. 2014

Critical Reviews in Toxicology

339

201

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Aluminum (Al) is a ubiquitous substance encountered both naturally (as the third most abundant element) and intentionally (used in water, foods, pharmaceuticals, and vaccines); it is also present in ambient and occupational airborne particulates. Existing data underscore the importance of Al physical and chemical forms in relation to its uptake, accumulation, and systemic bioavailability.Address for correspondence: Calvin C. Willhite, Risk Sciences International, 55 Metcalfe Street, Suite 700, Ottawa, ON, Canada. calvinwillhite@hotmail.com. Declaration of interestPartial funding for this work was provided by a contract to review the recent scientific literature on health effects of aluminum between the International Aluminium Institute (IAI, www.world-aluminium.org), the Aluminium Reach Consortium (ARC, www.aluminium-reach-consortium.eu), and Risk Sciences International (RSI, www.risksciences.com), a Canadian company established in 2006 in partnership with the University of Ottawa. Additional financial support was provided by the Natural Sciences and Engineering Research Council of Canada (NSERC) to D. Krewski, who holds the NSERC Chair in Risk Science at the University of Ottawa. C.C. Willhite, N.A. Karyakina, F. Momoli, and N. Yenugadhati were compensated by RSI for their contributions to the review. I. Arnold, T. Wisniewski and R. Yokel received no compensation from RSI for their contributions to this work. The authors, whose affiliations are shown on the title page, had sole responsibility for preparation of this paper, including determining the strategy for reviewing the scientific literature summarized in this article, synthesizing the findings, and drawing conclusions. Scientists associated with IAI/ARC were given the opportunity to review and offer technical comments on the paper, prior to submission to Critical Reviews in Toxicology. I. Arnold serves as a consultant to the International Aluminium Institute. None of the authors have appeared before regulatory agencies on behalf of the sponsors, or appeared as experts in legal proceedings concerning matters reviewed in this paper. The scientific opinions and conclusions expressed in the paper are exclusively those of the authors, and are independent of the sources of financial support. HHS Public Access Author Manuscript Author ManuscriptAuthor Manuscript Author ManuscriptThe present review represents a systematic examination of the peer-reviewed literature on the adverse health effects of Al materials published since a previous critical evaluation compiled by Krewski et al. (2007). The scientific literature on the adverse health effects of Al is extensive. Health risk assessments for Al must take into account individual co-factors (e.g., age, renal function, diet, gastric pH). Conclusions from the current review point to the need for refinement of the PTWI, reduction of Al contamination in PN solutions, justification for routine addition of Al to vaccines, and harmonization of OELs for Al substances.

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Section: Organ Systems and Functionmentioning

confidence: 60%

Section: Organ Systems and Functionmentioning

confidence: 96%

Section: Organ Systems and Functionmentioning

confidence: 99%

Section: Organ Systems and Functionmentioning

confidence: 99%

See 2 more Smart Citations

Systematic review of potential health risks posed by pharmaceutical, occupational and consumer exposures to metallic and nanoscale aluminum, aluminum oxides, aluminum hydroxide and its soluble salts

Willhite¹,

Karyakina²,

Yokel³

et al. 2014

Critical Reviews in Toxicology

339

201

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“…4b). It has been demonstrated previously that tubulin staining of live cells is an appropriate method to analyze cytotoxicity in neurons (23,48). Primary neurons at div2 were incubated with sAPP695 and .…”

Section: Meprin ␤ Processing Of Recombinant App Isoforms In Vitro-mentioning

confidence: 99%

Metalloprotease Meprin β Generates Nontoxic N-terminal Amyloid Precursor Protein Fragments in Vivo

Jefferson

Čaušević

Keller³

et al. 2011

Journal of Biological Chemistry

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Identification of physiologically relevant substrates is still the most challenging part in protease research for understanding the biological activity of these enzymes. The zinc-dependent metalloprotease meprin ␤ is known to be expressed in many tissues with functions in health and disease. Here, we demonstrate unique interactions between meprin ␤ and the amyloid precursor protein (APP). Although APP is intensively studied as a ubiquitously expressed cell surface protein, which is involved in Alzheimer disease, its precise physiological role and relevance remain elusive. Based on a novel proteomics technique termed terminal amine isotopic labeling of substrates (TAILS), APP was identified as a substrate for meprin ␤. Processing of APP by meprin ␤ was subsequently validated using in vitro and in vivo approaches. N-terminal APP fragments of about 11 and 20 kDa were found in human and mouse brain lysates but not in meprin ␤ ؊/؊ mouse brain lysates. Although these APP fragments were in the range of those responsible for caspase-induced neurodegeneration, we did not detect cytotoxicity to primary neurons treated by these fragments. Our data demonstrate that meprin ␤ is a physiologically relevant enzyme in APP processing.

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Correlation between Al³⁺‐induced thermal stability and inhibition of fibrillation of N‐terminal domain of the hydrogenase maturation factor

et al. 2013

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Fibrillation can be induced in proteins by altering solvent conditions. Stabilization of the protofibrillar structure arrests formation of longer fibers. Thermal stability and fibrillation of N-terminal domain of the hydrogenase maturation factor (HypF-N) were studied in the presence of a series of metal ions. Only Al(3+) was able to reverse the thermal denaturation of HypF-N upon heating. On being exposed to denaturing conditions, the native protein formed fibrillar structure under moderately denaturing conditions, whereas in the presence of Al(3+) , the protein was found to retain its native conformation. Under strongly denaturing conditions, only Al(3+) was able to stabilize the protein in the fibrillar state. Spectrofluorimetric analysis revealed that Al(3+) alone was able to stabilize the partially unfolded intermediate state of HypF-N. Based on the similarity in observations, we propose a link between reversal of thermal instability of HypF-N and its ability to form an intermediate structure in the presence of Al(3+) . Al(3+) stabilizes the partially unfolded state in the N↔I↔U equilibrium so that upon heating, the three-dimensional structure of the protein is not lost completely. Kinetic analysis confirmed that Al(3+) interacts with an early structure on the aggregation landscape and delays fibrillation. Under mildly denaturing state, HypF-N is able to recover its native conformation in the presence of Al(3+) and under strongly denaturing conditions, the protein does not acquire a completely disordered structure. Instead, it forms an ordered β-sheet-rich structure.

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Aluminum does not enhance β-amyloid toxicity in rat hippocampal cultures

Cited by 10 publications

References 83 publications

Systematic review of potential health risks posed by pharmaceutical, occupational and consumer exposures to metallic and nanoscale aluminum, aluminum oxides, aluminum hydroxide and its soluble salts

Systematic review of potential health risks posed by pharmaceutical, occupational and consumer exposures to metallic and nanoscale aluminum, aluminum oxides, aluminum hydroxide and its soluble salts

Metalloprotease Meprin β Generates Nontoxic N-terminal Amyloid Precursor Protein Fragments in Vivo

Correlation between Al³⁺‐induced thermal stability and inhibition of fibrillation of N‐terminal domain of the hydrogenase maturation factor

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Aluminum does not enhance β-amyloid toxicity in rat hippocampal cultures

Cited by 10 publications

References 83 publications

Systematic review of potential health risks posed by pharmaceutical, occupational and consumer exposures to metallic and nanoscale aluminum, aluminum oxides, aluminum hydroxide and its soluble salts

Systematic review of potential health risks posed by pharmaceutical, occupational and consumer exposures to metallic and nanoscale aluminum, aluminum oxides, aluminum hydroxide and its soluble salts

Metalloprotease Meprin β Generates Nontoxic N-terminal Amyloid Precursor Protein Fragments in Vivo

Correlation between Al3+‐induced thermal stability and inhibition of fibrillation of N‐terminal domain of the hydrogenase maturation factor

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Resources

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Correlation between Al³⁺‐induced thermal stability and inhibition of fibrillation of N‐terminal domain of the hydrogenase maturation factor