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Mechanisms of Heavy Metal Toxicity: 3rd Edition
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Mechanisms of Heavy Metal Toxicity: 3rd Edition

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Toxicology".

Deadline for manuscript submissions: 30 November 2024 | Viewed by 517

Special Issue Editor

Prof. Dr. Toshiyuki Kaji

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Guest Editor
Department of Environmental Health, Faculty of Pharmaceutical Sciences, Tokyo University of Science, Noda 278-8510, Japan
Interests: signaling and cell response; transporter; vascular toxicity; extracellular matrix; atherosclerosis; blood coagulation-fibrinolytic system; growth factors; cytokines
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues, 

This Special Issue is a continuation of our previous Special Issue, entitled “Mechanisms of Heavy Metal Toxicity 2.0” (https://www.mdpi.com/journal/ijms/special_issues/H84PU90OTN).

The toxicity of heavy metals has been a popular research topic for a long time. In the past, it was important to elucidate the actual health hazards caused by environmental pollution, accidents, and crimes, involving metals, metalloids, and metal compounds, but now the main issues are related to the elucidation of the mechanisms of their toxicity and defense mechanisms against said toxicity.

This Special Issue is under production, with the aim of addressing this contemporary issue. In this Special Issue, we welcome the submission of full reviews, original research papers, short communications, and perspectives that cover the following topics:

  • Cellular and molecular mechanisms underlying heavy metals, metalloids, and metal(loid)-containing compounds;
  • Mechanisms underlying the induction of metallothionein;
  • Cellular defense systems against the toxicity of heavy metals, metalloids, and metal(loid)-containing compounds;
  • The regulation and mechanisms of the expression of metal transporters, such as SLC39A8;
  • Research that does not fit into the above topics but may contribute to them is also welcome.

By sharing these studies, we aim to make significant progress in metal toxicology.

Prof. Dr. Toshiyuki Kaji
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • heavy metal
  • metal compound
  • metallothionein
  • cellular defense mechanism
  • metal transporter

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Published Papers (1 paper)

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Research

14 pages, 1903 KiB  
Article
Metalloproteomics Reveals Multi-Level Stress Response in Escherichia coli When Exposed to Arsenite
by James Larson, Brett Sather, Lu Wang, Jade Westrum, Monika Tokmina-Lukaszewska, Jordan Pauley, Valérie Copié, Timothy R. McDermott and Brian Bothner
Int. J. Mol. Sci. 2024, 25(17), 9528; https://doi.org/10.3390/ijms25179528 - 2 Sep 2024
Viewed by 353
Abstract
The arsRBC operon encodes a three-protein arsenic resistance system. ArsR regulates the transcription of the operon, while ArsB and ArsC are involved in exporting trivalent arsenic and reducing pentavalent arsenic, respectively. Previous research into Agrobacterium tumefaciens 5A has demonstrated that ArsR has regulatory [...] Read more.
The arsRBC operon encodes a three-protein arsenic resistance system. ArsR regulates the transcription of the operon, while ArsB and ArsC are involved in exporting trivalent arsenic and reducing pentavalent arsenic, respectively. Previous research into Agrobacterium tumefaciens 5A has demonstrated that ArsR has regulatory control over a wide range of metal-related proteins and metabolic pathways. We hypothesized that ArsR has broad regulatory control in other Gram-negative bacteria and set out to test this. Here, we use differential proteomics to investigate changes caused by the presence of the arsR gene in human microbiome-relevant Escherichia coli during arsenite (AsIII) exposure. We show that ArsR has broad-ranging impacts such as the expression of TCA cycle enzymes during AsIII stress. Additionally, we found that the Isc [Fe-S] cluster and molybdenum cofactor assembly proteins are upregulated regardless of the presence of ArsR under these same conditions. An important finding from this differential proteomics analysis was the identification of response mechanisms that were strain-, ArsR-, and arsenic-specific, providing new clarity to this complex regulon. Given the widespread occurrence of the arsRBC operon, these findings should have broad applicability across microbial genera, including sensitive environments such as the human gastrointestinal tract. Full article
(This article belongs to the Special Issue Mechanisms of Heavy Metal Toxicity: 3rd Edition)
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Figure 1

Figure 1
<p>ArsR confers As<sup>III</sup> resistance. (<b>a</b>) Growth of AW3110 and <span class="html-italic">arsR</span>-complemented AW3110. Cultures were grown in triplicate (<span class="html-italic">n</span> = 3) in the presence (red) and absence of arsenic (black) for AW3110 (solid line) and <span class="html-italic">arsR</span>-complement (dashed). A 100 µM As<sup>III</sup> treatment was given at 2 h post-inoculation. (<b>b</b>) Growth of K-12. Cultures were grown in triplicate (<span class="html-italic">n</span> = 3) in the presence (red) and absence of arsenic (black). The arsenic concentrations were 100 µM (dashed) or 1 mM As<sup>III</sup> (solid). Arsenite was added 2 h post-inoculation, indicated by the arrow. Samples were collected 2 h later for proteomics analysis. Error bars are ± 1 standard deviation.</p> Full article ">Figure 2
<p>Statistical analysis of the metal-related proteome. (<b>a</b>) PCA analysis of <span class="html-italic">E. coli</span> strains K-12, AW3110, and the <span class="html-italic">arsR</span>−complement with and without As<sup>III</sup> stress. The labels are as follows: K12 H is K-12 with high As<sup>III</sup> stress, K12 L is K-12 with low As<sup>III</sup> stress, K12 C is the unstressed K-12 control, AW_As is the AW3110 high As<sup>II</sup> stress, AW_C is the AW3110 control, arsR_As is the <span class="html-italic">arsR</span>-complement high As<sup>III</sup> stress, and arsR_C is the <span class="html-italic">arsR</span>-complement control. (<b>b</b>) Hierarchical clustering based on the top 30 features of a one-way ANOVA. Protein cluster based on strain differences, high arsenite stress, and the presence of ArsR. Proteins are given as their Uniprot accession numbers. Proteins whose expression was altered based upon the presence of ArsR are outlined with solid boxes, proteins clustered due to high As<sup>III</sup> stress are outlined with dashed boxes, and clusters due to strain differences are not outlined. The ArsR (P37309) and ArsC (P0AB96) proteins and highlighted.</p> Full article ">Figure 3
<p>Metallocofactor proteins affected by high As<sup>III</sup> stress. Based on a one-way ANOVA, these proteins increased in abundance in all strains under high As<sup>III</sup> stress and were in the top 30 metalloproteins. Increasing darkness indicates the severity of As<sup>III</sup> stress. The no As<sup>III</sup> control for each strain is white, low As<sup>III</sup> stress is grey, and high As<sup>III</sup> stress is black. The boxes are colored to match the sample group colors in <a href="#ijms-25-09528-f002" class="html-fig">Figure 2</a>.</p> Full article ">Figure 4
<p>ArsR regulates expression of TCA cycle protein expression under As<sup>III</sup> stress. The expression of TCA cycle proteins under high As<sup>III</sup> stress compared to the no As<sup>III</sup> controls is indicated by arrows and is color coordinated. AW3110 is indicated in blue, the <span class="html-italic">arsR</span>-complement is in black, and K-12 is in pink. An up arrow indicates an increase in expression. A down arrow indicates a decrease in expression. No arrow means the expression was unchanged. Dashed arrows indicate a marginal change in expression.</p> Full article ">Figure 5
<p>Soluble intracellular metal concentrations. The soluble cellular metal concentrations from each condition (<span class="html-italic">n</span> = 3) were measured with ICP-MS. Bars denote significant differences at <span class="html-italic">p</span>-value &lt; 0.05. Only significance intragroup is displayed.</p> Full article ">Figure 5 Cont.
<p>Soluble intracellular metal concentrations. The soluble cellular metal concentrations from each condition (<span class="html-italic">n</span> = 3) were measured with ICP-MS. Bars denote significant differences at <span class="html-italic">p</span>-value &lt; 0.05. Only significance intragroup is displayed.</p> Full article ">
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