Mercury's neurotoxicity is characterized by its disruption of selenium biochemistry
Methylmercury (CH3Hg+) toxicity is characterized by challenging conundrums: 1) “selenium (Se)-protective” effects, 2) undefined biochemical mechanism/s of toxicity, 3) brain-specific oxidative damage, 4) fetal vulnerability, and 5) its latency effect. The “protective effects of Se” against CH3Hg+ to...
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| Published in | Biochimica et biophysica acta. General subjects Vol. 1862; no. 11; pp. 2405 - 2416 |
|---|---|
| Main Authors | , |
| Format | Journal Article |
| Language | English |
| Published |
Netherlands
Elsevier B.V
01.11.2018
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| Subjects | |
| Online Access | Get full text |
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| Abstract | Methylmercury (CH3Hg+) toxicity is characterized by challenging conundrums: 1) “selenium (Se)-protective” effects, 2) undefined biochemical mechanism/s of toxicity, 3) brain-specific oxidative damage, 4) fetal vulnerability, and 5) its latency effect. The “protective effects of Se” against CH3Hg+ toxicity were first recognized >50 years ago, but awareness of Se's vital functions in the brain has transformed understanding of CH3Hg+ biochemical mechanisms. Mercury's affinity for Se is ~1 million times greater than its affinity for sulfur, revealing it as the primary target of CH3Hg+ toxicity.
This focused review examined research literature regarding distinctive characteristics of CH3Hg+ toxicity to identify Se-dependent aspects of its biochemical mechanisms and effects.
Research indicates that CH3Hg+ irreversibly inhibits the selenoenzymes that normally prevent/reverse oxidative damage in the brain. Unless supplemental Se is provided, consequences increase as CH3Hg+ approaches/exceeds equimolar stoichiometries with Se, thus forming HgSe and inducing a conditioned Se deficiency. As the biochemical target of CH3Hg+ toxicity, Se-physiology provides perspectives on the brain specificity of its oxidative damage, accentuated fetal vulnerability, and latency. This review reconsiders the concept that Se is a “tonic” that protects against CH3Hg+ toxicity and recognizes Se's role as Hg's molecular “target”. As the most potent intracellular nucleophile, the selenoenzyme inhibition paradigm has broad implications in toxicology, including resolution of conundrums of CH3Hg+ toxicity.
Mercury-dependent sequestration of selenium and the irreversible inhibition of selenoenzymes, especially those required to prevent and reverse oxidative damage in the brain, are primarily responsible for the characteristic effects of mercury toxicity.
This figure shows the electrostatic potential surfaces of mercury in covalent association with the biologically significant chalcogens (oxygen, sulfur, and selenium), their chemical potentials, and binding affinity constants.
The electron cloud depicted in blue indicates a lower e− abundance and a more positive charge, while yellow shading to red indicates increasingly negative charge. The balance of the HgSe charges stabilize the molecule, contributing to their remarkably high binding affinities. [Display omitted]
•The conundrums of mercury toxicity are consilient from the selenium-perspective.•Mercury toxicity had formerly been assumed to involve binding to cellular thiols.•Mercury's delayed neurotoxicity & fetal vulnerability reflect its effects on selenium.•Thiols help mercury bind selenocysteine-the 21st genetically encoded amino acid.•Mercury inhibits brain selenoenzymes that prevent and reverse oxidative damage. |
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| AbstractList | Methylmercury (CH₃Hg⁺) toxicity is characterized by challenging conundrums: 1) “selenium (Se)-protective” effects, 2) undefined biochemical mechanism/s of toxicity, 3) brain-specific oxidative damage, 4) fetal vulnerability, and 5) its latency effect. The “protective effects of Se” against CH₃Hg⁺ toxicity were first recognized >50 years ago, but awareness of Se's vital functions in the brain has transformed understanding of CH₃Hg⁺ biochemical mechanisms. Mercury's affinity for Se is ~1 million times greater than its affinity for sulfur, revealing it as the primary target of CH₃Hg⁺ toxicity.This focused review examined research literature regarding distinctive characteristics of CH₃Hg⁺ toxicity to identify Se-dependent aspects of its biochemical mechanisms and effects.Research indicates that CH₃Hg⁺ irreversibly inhibits the selenoenzymes that normally prevent/reverse oxidative damage in the brain. Unless supplemental Se is provided, consequences increase as CH₃Hg⁺ approaches/exceeds equimolar stoichiometries with Se, thus forming HgSe and inducing a conditioned Se deficiency. As the biochemical target of CH₃Hg⁺ toxicity, Se-physiology provides perspectives on the brain specificity of its oxidative damage, accentuated fetal vulnerability, and latency. This review reconsiders the concept that Se is a “tonic” that protects against CH₃Hg⁺ toxicity and recognizes Se's role as Hg's molecular “target”. As the most potent intracellular nucleophile, the selenoenzyme inhibition paradigm has broad implications in toxicology, including resolution of conundrums of CH₃Hg⁺ toxicity.Mercury-dependent sequestration of selenium and the irreversible inhibition of selenoenzymes, especially those required to prevent and reverse oxidative damage in the brain, are primarily responsible for the characteristic effects of mercury toxicity. Methylmercury (CH3Hg+) toxicity is characterized by challenging conundrums: 1) “selenium (Se)-protective” effects, 2) undefined biochemical mechanism/s of toxicity, 3) brain-specific oxidative damage, 4) fetal vulnerability, and 5) its latency effect. The “protective effects of Se” against CH3Hg+ toxicity were first recognized >50 years ago, but awareness of Se's vital functions in the brain has transformed understanding of CH3Hg+ biochemical mechanisms. Mercury's affinity for Se is ~1 million times greater than its affinity for sulfur, revealing it as the primary target of CH3Hg+ toxicity. This focused review examined research literature regarding distinctive characteristics of CH3Hg+ toxicity to identify Se-dependent aspects of its biochemical mechanisms and effects. Research indicates that CH3Hg+ irreversibly inhibits the selenoenzymes that normally prevent/reverse oxidative damage in the brain. Unless supplemental Se is provided, consequences increase as CH3Hg+ approaches/exceeds equimolar stoichiometries with Se, thus forming HgSe and inducing a conditioned Se deficiency. As the biochemical target of CH3Hg+ toxicity, Se-physiology provides perspectives on the brain specificity of its oxidative damage, accentuated fetal vulnerability, and latency. This review reconsiders the concept that Se is a “tonic” that protects against CH3Hg+ toxicity and recognizes Se's role as Hg's molecular “target”. As the most potent intracellular nucleophile, the selenoenzyme inhibition paradigm has broad implications in toxicology, including resolution of conundrums of CH3Hg+ toxicity. Mercury-dependent sequestration of selenium and the irreversible inhibition of selenoenzymes, especially those required to prevent and reverse oxidative damage in the brain, are primarily responsible for the characteristic effects of mercury toxicity. This figure shows the electrostatic potential surfaces of mercury in covalent association with the biologically significant chalcogens (oxygen, sulfur, and selenium), their chemical potentials, and binding affinity constants. The electron cloud depicted in blue indicates a lower e− abundance and a more positive charge, while yellow shading to red indicates increasingly negative charge. The balance of the HgSe charges stabilize the molecule, contributing to their remarkably high binding affinities. [Display omitted] •The conundrums of mercury toxicity are consilient from the selenium-perspective.•Mercury toxicity had formerly been assumed to involve binding to cellular thiols.•Mercury's delayed neurotoxicity & fetal vulnerability reflect its effects on selenium.•Thiols help mercury bind selenocysteine-the 21st genetically encoded amino acid.•Mercury inhibits brain selenoenzymes that prevent and reverse oxidative damage. Methylmercury (CH Hg ) toxicity is characterized by challenging conundrums: 1) "selenium (Se)-protective" effects, 2) undefined biochemical mechanism/s of toxicity, 3) brain-specific oxidative damage, 4) fetal vulnerability, and 5) its latency effect. The "protective effects of Se" against CH Hg toxicity were first recognized >50 years ago, but awareness of Se's vital functions in the brain has transformed understanding of CH Hg biochemical mechanisms. Mercury's affinity for Se is ~1 million times greater than its affinity for sulfur, revealing it as the primary target of CH Hg toxicity. This focused review examined research literature regarding distinctive characteristics of CH Hg toxicity to identify Se-dependent aspects of its biochemical mechanisms and effects. Research indicates that CH Hg irreversibly inhibits the selenoenzymes that normally prevent/reverse oxidative damage in the brain. Unless supplemental Se is provided, consequences increase as CH Hg approaches/exceeds equimolar stoichiometries with Se, thus forming HgSe and inducing a conditioned Se deficiency. As the biochemical target of CH Hg toxicity, Se-physiology provides perspectives on the brain specificity of its oxidative damage, accentuated fetal vulnerability, and latency. This review reconsiders the concept that Se is a "tonic" that protects against CH Hg toxicity and recognizes Se's role as Hg's molecular "target". As the most potent intracellular nucleophile, the selenoenzyme inhibition paradigm has broad implications in toxicology, including resolution of conundrums of CH Hg toxicity. Mercury-dependent sequestration of selenium and the irreversible inhibition of selenoenzymes, especially those required to prevent and reverse oxidative damage in the brain, are primarily responsible for the characteristic effects of mercury toxicity. Methylmercury (CH3Hg+) toxicity is characterized by challenging conundrums: 1) "selenium (Se)-protective" effects, 2) undefined biochemical mechanism/s of toxicity, 3) brain-specific oxidative damage, 4) fetal vulnerability, and 5) its latency effect. The "protective effects of Se" against CH3Hg+ toxicity were first recognized >50 years ago, but awareness of Se's vital functions in the brain has transformed understanding of CH3Hg+ biochemical mechanisms. Mercury's affinity for Se is ~1 million times greater than its affinity for sulfur, revealing it as the primary target of CH3Hg+ toxicity.BACKGROUNDMethylmercury (CH3Hg+) toxicity is characterized by challenging conundrums: 1) "selenium (Se)-protective" effects, 2) undefined biochemical mechanism/s of toxicity, 3) brain-specific oxidative damage, 4) fetal vulnerability, and 5) its latency effect. The "protective effects of Se" against CH3Hg+ toxicity were first recognized >50 years ago, but awareness of Se's vital functions in the brain has transformed understanding of CH3Hg+ biochemical mechanisms. Mercury's affinity for Se is ~1 million times greater than its affinity for sulfur, revealing it as the primary target of CH3Hg+ toxicity.This focused review examined research literature regarding distinctive characteristics of CH3Hg+ toxicity to identify Se-dependent aspects of its biochemical mechanisms and effects.SCOPE OF REVIEWThis focused review examined research literature regarding distinctive characteristics of CH3Hg+ toxicity to identify Se-dependent aspects of its biochemical mechanisms and effects.Research indicates that CH3Hg+ irreversibly inhibits the selenoenzymes that normally prevent/reverse oxidative damage in the brain. Unless supplemental Se is provided, consequences increase as CH3Hg+ approaches/exceeds equimolar stoichiometries with Se, thus forming HgSe and inducing a conditioned Se deficiency. As the biochemical target of CH3Hg+ toxicity, Se-physiology provides perspectives on the brain specificity of its oxidative damage, accentuated fetal vulnerability, and latency. This review reconsiders the concept that Se is a "tonic" that protects against CH3Hg+ toxicity and recognizes Se's role as Hg's molecular "target". As the most potent intracellular nucleophile, the selenoenzyme inhibition paradigm has broad implications in toxicology, including resolution of conundrums of CH3Hg+ toxicity.CONCLUSIONSResearch indicates that CH3Hg+ irreversibly inhibits the selenoenzymes that normally prevent/reverse oxidative damage in the brain. Unless supplemental Se is provided, consequences increase as CH3Hg+ approaches/exceeds equimolar stoichiometries with Se, thus forming HgSe and inducing a conditioned Se deficiency. As the biochemical target of CH3Hg+ toxicity, Se-physiology provides perspectives on the brain specificity of its oxidative damage, accentuated fetal vulnerability, and latency. This review reconsiders the concept that Se is a "tonic" that protects against CH3Hg+ toxicity and recognizes Se's role as Hg's molecular "target". As the most potent intracellular nucleophile, the selenoenzyme inhibition paradigm has broad implications in toxicology, including resolution of conundrums of CH3Hg+ toxicity.Mercury-dependent sequestration of selenium and the irreversible inhibition of selenoenzymes, especially those required to prevent and reverse oxidative damage in the brain, are primarily responsible for the characteristic effects of mercury toxicity.GENERAL SIGNIFICANCEMercury-dependent sequestration of selenium and the irreversible inhibition of selenoenzymes, especially those required to prevent and reverse oxidative damage in the brain, are primarily responsible for the characteristic effects of mercury toxicity. |
| Author | Raymond, Laura J. Ralston, Nicholas V.C. |
| Author_xml | – sequence: 1 givenname: Nicholas V.C. surname: Ralston fullname: Ralston, Nicholas V.C. email: nick.ralston@und.edu organization: Earth System Science and Policy, University of North Dakota, Grand Forks, ND, USA – sequence: 2 givenname: Laura J. surname: Raymond fullname: Raymond, Laura J. organization: Translational Medicine Research Consultants, Grand Forks, ND, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/29753115$$D View this record in MEDLINE/PubMed |
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| Keywords | Ser Brain RSe Toxicity SELENOF SeMet SELENOK SeO3 SeO42 Selenium Cys CH3HgCH3 CH3Hg SEPHS2 Hg+ or Hg2 GPX4 TXNRD2 RSH TXNRD1 DIO1 DIO ApoER2 Hg0 Sec LAT1 SELENON SELENOM SELENOP SELENOW HSe Selenoproteins SeO32 Met Mercury MSRB1 |
| Language | English |
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| PublicationTitle | Biochimica et biophysica acta. General subjects |
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| Snippet | Methylmercury (CH3Hg+) toxicity is characterized by challenging conundrums: 1) “selenium (Se)-protective” effects, 2) undefined biochemical mechanism/s of... Methylmercury (CH Hg ) toxicity is characterized by challenging conundrums: 1) "selenium (Se)-protective" effects, 2) undefined biochemical mechanism/s of... Methylmercury (CH3Hg+) toxicity is characterized by challenging conundrums: 1) "selenium (Se)-protective" effects, 2) undefined biochemical mechanism/s of... Methylmercury (CH₃Hg⁺) toxicity is characterized by challenging conundrums: 1) “selenium (Se)-protective” effects, 2) undefined biochemical mechanism/s of... |
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| SubjectTerms | biochemical mechanisms Brain Lewis bases Mercury methylmercury compounds neurotoxicity nutrient deficiencies protective effect Selenium Selenoproteins sulfur Toxicity toxicology |
| Title | Mercury's neurotoxicity is characterized by its disruption of selenium biochemistry |
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