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[PMID]:28466911
[Au] Autor:Scheller JS; Irvine GW; Wong DL; Hartwig A; Stillman MJ
[Ad] Endereço:Department of Chemistry, The University of Western Ontario, London, Ontario, N6A 5B7, Canada. martin.stillman@uwo.ca.
[Ti] Título:Stepwise copper(i) binding to metallothionein: a mixed cooperative and non-cooperative mechanism for all 20 copper ions.
[So] Source:Metallomics;9(5):447-462, 2017 May 24.
[Is] ISSN:1756-591X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Copper is a ubiquitous trace metal of vital importance in that it serves as a cofactor in many metalloenzymes. Excess copper becomes harmful if not sequestered appropriately in the cell. As a metal ion chaperone, metallothionein (MT) has been proposed as a key player in zinc and copper homeostasis within the cell. The underlying mechanisms by which MT sequesters and transfers copper ions, and subsequently achieves its proposed biological function remain unknown. Using a combination of electrospray ionization mass spectrometry (ESI-MS), circular dichroism (CD), and emission spectroscopy, we report that the Cu(i) to human apo-MT1a binding mechanism is highly pH-dependent. The 20 relative K -values for the binding of 1 to 20 Cu(i) to the 20 cysteines of MT were obtained from computational simulation of the experimental mass spectral results. These data identified the pH-dependent formation of three sequential but completely different Cu-S clusters, as a function of Cu(i) loading. These data provide the first overall sequence for Cu(i) binding in terms of domain specificity and transient binding site structures. Under cooperative binding at pH 7.4, a series of four clusters form: Cu S , followed by Cu S (ß), then a second Cu S (α), and finally Cu S (α) (x = up to 11). Upon further addition of Cu(i), a mixture of species is formed in a non-cooperative mechanism, saturating the 20 cysteines of MT1a. Using benzoquinone, a cysteine modifier, we were able to confirm that Cu S formed solely in the N-terminal ß-domain, as well as confirming the existence of the presumed Cu S cluster in the α-domain. Based on the results of ESI-MS and computational simulation we were able to identify Cu:MT speciation that resulted in specific emission and CD spectral properties.
[Mh] Termos MeSH primário: Cobre/metabolismo
Metalotioneína/metabolismo
[Mh] Termos MeSH secundário: Sítios de Ligação
Dicroísmo Circular
Cobre/química
Seres Humanos
Concentração de Íons de Hidrogênio
Metalotioneína/química
Modelos Moleculares
Ligação Proteica
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Espectrometria de Massas por Ionização por Electrospray
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MT1A protein, human); 0 (Recombinant Proteins); 789U1901C5 (Copper); 9038-94-2 (Metallothionein)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.1039/c7mt00041c


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[PMID]:29231000
[Au] Autor:Fan HL; Liu SF; Sun JH; Wang YY
[Ad] Endereço:School of Forensic Medicine, Shanxi Medical University, Taiyuan 030001, China.
[Ti] Título:Time-dependent Expression of MT1A mRNA and MT2A mRNA in the Contused Skeletal Muscle of Rats.
[So] Source:Fa Yi Xue Za Zhi;33(1):6-10, 2017 Feb.
[Is] ISSN:1004-5619
[Cp] País de publicação:China
[La] Idioma:eng
[Ab] Resumo:OBJECTIVES: To investigate the time-dependent expression of metallothionein (MT) 1A mRNA and MT2A mRNA in contused skeletal muscle of rats. METHODS: A total of 54 Sprague-Dawley rats were used in this study. The rats were divided into two parts: control group ( =6) and contusion groups (0.5, 1, 6, 12, 18, 24, 30, and 36 h after contusion, =6). Total RNA was extracted from skeletal muscle. The expression levels of MT1A mRNA and MT2A mRNA were detected by SYBR Green I real-time PCR. RESULTS: The expression trends of the two potential marker genes were related to wound age. In addition to 0.5 h, there were significant contrasts between the control group and contused group ( <0.05), about the expression levels of MT1A mRNA and MT2A mRNA in different phases. As the extension of wound age, the relative expression of MT1A mRNA and MT2A mRNA at 1 h, 6 h, 12 h and 18 h after contusion demonstrated upgrade tendency until its expression levels in 18 h peak with 239.41±15.20 and 717.42±50.76, respectively. When time extends to 24 h after injury, the expression of above two marks decreased, respectively. The MT1A mRNA and MT2A mRNA expression levels increased at 30 h and then decreased. CONCLUSIONS: Determination of MT1A mRNA and MT2A mRNA levels by real-time PCR may be useful for the estimation of wound age.
[Mh] Termos MeSH primário: Contusões/genética
Contusões/metabolismo
Músculo Esquelético/metabolismo
RNA Mensageiro/metabolismo
[Mh] Termos MeSH secundário: Animais
Contusões/patologia
Regulação da Expressão Gênica
Marcadores Genéticos
Metalotioneína
Músculo Esquelético/lesões
Ratos
Ratos Sprague-Dawley
Reação em Cadeia da Polimerase em Tempo Real
Fatores de Tempo
Cicatrização
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Genetic Markers); 0 (RNA, Messenger); 0 (metallothionein 2 protein, rat); 9038-94-2 (Metallothionein)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171213
[St] Status:MEDLINE
[do] DOI:10.3969/j.issn.1004-5619.2017.01.002


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[PMID]:29191452
[Au] Autor:Poetini MR; Araujo SM; Trindade de Paula M; Bortolotto VC; Meichtry LB; Polet de Almeida F; Jesse CR; Kunz SN; Prigol M
[Ad] Endereço:Laboratório de Avaliações Farmacológicas e Toxicológicas Aplicadas às Moléculas Bioativas- LaftamBio Pampa- Universidade Federal do Pampa, Itaqui, CEP 97650-000, RS, Brazil.
[Ti] Título:Hesperidin attenuates iron-induced oxidative damage and dopamine depletion in Drosophila melanogaster model of Parkinson's disease.
[So] Source:Chem Biol Interact;279:177-186, 2018 Jan 05.
[Is] ISSN:1872-7786
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:This study has evaluated the action of flavonoid hesperidin on the neurotoxic effects caused by the intake of iron (Fe) in Drosophila melanogaster. Male adult flies, aged 1-3 days, have been divided into four groups of 50 each: (1) control, (2) Hsd 10 µM, (3) Fe 20 mM (4) Hsd 10 µM + Fe 20 mM. During the exposure protocol, the flies have been exposed to a diet containing Hsd and/or Fe for 48 h. The survival and behavioral analyses have been carried out in vivo, and ex vivo. The analyses involved acetylcholinesterase (AChE) activity and Fe levels in the flies' heads and bodies and determination of dopaminergic levels, cellular and mitochondrial viability, activities of superoxide dismutase (SOD), catalase (CAT), glutathione-S-transferase (GST), reactive species levels (RS), thiobarbituric acid reactive substances (TBARS) and contents of total thiols and non-proteic thiols (NPSH) in the flies' heads. A significant negative correlation between Fe levels in the head of the flies and the survival, dopamine levels and antioxidant enzymes in the head of the flies has been found. Additionally, significant positive correlation between Fe levels in the head of the flies with negative geotaxis RS and AChE activity in the head of the flies has been found. It demonstrates that the flies which had higher levels of Fe in their heads have demonstrated more susceptibility to neurotoxicity. An important result from our study is that Hsd treatment promotes a decrease in Fe concentration in the head, restores dopamine levels and cholinergic activity of the flies and improves motor function caused by Fe. Hsd also ameliorates Fe induced mortality, oxidative stress and mitochondrial dysfunction. Our results have demonstrated the neuroprotective effect of Hsd and it suggests that flavonoid acts in different ways to protect against the Parkinson disease caused by Fe exposure such as the direct scavenging of RS and activation of antioxidant enzymes.
[Mh] Termos MeSH primário: Dopamina/metabolismo
Drosophila melanogaster/efeitos dos fármacos
Hesperidina/farmacologia
Ferro/toxicidade
Estresse Oxidativo/efeitos dos fármacos
Doença de Parkinson Secundária/induzido quimicamente
[Mh] Termos MeSH secundário: Animais
Biomarcadores
Masculino
Metalotioneína/metabolismo
Mitocôndrias
Atividade Motora/efeitos dos fármacos
Oxirredução
Doença de Parkinson Secundária/prevenção & controle
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 9038-94-2 (Metallothionein); E1UOL152H7 (Iron); E750O06Y6O (Hesperidin); VTD58H1Z2X (Dopamine)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180103
[Lr] Data última revisão:
180103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171202
[St] Status:MEDLINE


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[PMID]:29206858
[Au] Autor:de Francisco P; Martín-González A; Turkewitz AP; Gutiérrez JC
[Ad] Endereço:Departamento de Microbiología-III, Facultad de Biología, Universidad Complutense de Madrid (UCM), Madrid, Spain.
[Ti] Título:Extreme metal adapted, knockout and knockdown strains reveal a coordinated gene expression among different Tetrahymena thermophila metallothionein isoforms.
[So] Source:PLoS One;12(12):e0189076, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Metallothioneins (MT) constitute a superfamily of small cytosolic proteins that are able to bind metal cations through numerous cysteine (Cys) residues. Like other organisms the ciliate Tetrahymena thermophila presents several MT isoforms, which have been classified into two subfamilies (Cd- and Cu-metallothioneins). The main aim of this study was to examine the specific functions and transcriptional regulation of the five MT isoforms present in T. thermophila, by using several strains of this ciliate. After a laboratory evolution experiment over more than two years, three different T. thermophila strains adapted to extreme metal stress (Cd2+, Cu2+ or Pb2+) were obtained. In addition, three knockout and/or knockdown strains for different metallothionein (MT) genes were generated. These strains were then analyzed for expression of the individual MT isoforms. Our results provide a strong basis for assigning differential roles to the set of MT isoforms. MTT1 appears to have a key role in adaptation to Cd. In contrast, MTT2/4 are crucial for Cu-adaptation and MTT5 appears to be important for Pb-adaptation and might be considered as an "alarm" MT gene for responding to metal stress. Moreover, results indicate that likely a coordinated transcriptional regulation exists between the MT genes, particularly among MTT1, MTT5 and MTT2/4. MTT5 appears to be an essential gene, a first such report in any organism of an essential MT gene.
[Mh] Termos MeSH primário: Adaptação Fisiológica
Expressão Gênica
Metalotioneína/genética
Metais/toxicidade
Isoformas de Proteínas/genética
Tetrahymena thermophila/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Genes de Protozoários
Tetrahymena thermophila/genética
Tetrahymena thermophila/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Metals); 0 (Protein Isoforms); 9038-94-2 (Metallothionein)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171229
[Lr] Data última revisão:
171229
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171206
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189076


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[PMID]:28974419
[Au] Autor:Yang P; Hong W; Zhou P; Chen B; Xu H
[Ad] Endereço:State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, China.
[Ti] Título:Nano and bulk ZnO trigger diverse Zn-transport-related gene transcription in distinct regions of the small intestine in mice after oral exposure.
[So] Source:Biochem Biophys Res Commun;493(3):1364-1369, 2017 Nov 25.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The oral ingestion of ZnO nanoparticles (NPs) has attracted considerable attention because of the wide usage in food packaging and additives. The small intestine is the major absorption site for ZnO NPs. Unfortunately, studies on the absorption of ZnO NPs in the GIT were still scarce. This study evaluated the absorption characteristics of ZnO NPs (30 nm) and bulk ZnO (rod morphology with a mean size of 139-846 nm). Results showed that ZnO NPs and bulk ZnO were absorbed and redistributed in various organs of mice at 4 h after exposure. Significantly higher levels of MT1 were observed in the duodenums of bulk ZnO and ZnO NPs groups than those of the control (9.8 and 5660.11 fold increases, respectively). The MT4 levels in the bulk ZnO and ZnO NPs groups also showed 4.07 and 43.21fold increases, respectively. In addition, the transcript levels of ZIPs, ZnTs, and MTs in the jejunum of bulk ZnO group were higher than those of ZnO NPs group. And the transcript levels of ZIPs, ZnTs, and MTs were all lower in the ileum than in the jejunum. The results suggested that ZnO NPs were mainly absorbed in the duodenum in the form of particles and can be absorbed as Zn in the jejunum and secondly in the ileum. By contrast, bulk ZnO was more easily absorbed as Zn in the jejunum and secondly in the ileum.
[Mh] Termos MeSH primário: Regulação da Expressão Gênica/efeitos dos fármacos
Intestino Delgado/efeitos dos fármacos
Nanopartículas/toxicidade
Óxido de Zinco/toxicidade
Zinco/metabolismo
[Mh] Termos MeSH secundário: Administração Oral
Animais
Transporte Biológico/efeitos dos fármacos
Transporte Biológico/genética
Intestino Delgado/metabolismo
Metalotioneína/genética
Camundongos
Nanopartículas/administração & dosagem
Distribuição Tecidual
Zinco/farmacocinética
Óxido de Zinco/administração & dosagem
Óxido de Zinco/farmacocinética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
9038-94-2 (Metallothionein); J41CSQ7QDS (Zinc); SOI2LOH54Z (Zinc Oxide)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171005
[St] Status:MEDLINE


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[PMID]:28870952
[Au] Autor:Wojtczak B; Pula B; Gomulkiewicz A; Olbromski M; Podhorska-Okolow M; Domoslawski P; Bolanowski M; Daroszewski J; Dziegiel P
[Ad] Endereço:First Department and Clinic of General, Gastroenterological and Endocrine Surgery, Wroclaw Medical University, Wroclaw, Poland beatawojtczak@wp.pl.
[Ti] Título:Metallothionein Isoform Expression in Benign and Malignant Thyroid Lesions.
[So] Source:Anticancer Res;37(9):5179-5185, 2017 09.
[Is] ISSN:1791-7530
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Metallothioneins (MTs) are involved in numerous cell processes such as binding and transport of zinc and copper ions, differentiation, proliferation and apoptosis, therefore contributing to carcinogenesis. Scarce data exist on their expression in benign and malignant lesions of the thyroid. MATERIALS AND METHODS: mRNA expression of functional isoforms of MT genes (MT1A, MT1B, MT1E, MT1F, MT1G, MT1H, MT1X, MT2A, MT4) was studied in 17 nodular goiters (NG), 12 follicular adenomas (FA) and 26 papillary thyroid carcinomas (PTC). RESULTS: One-way ANOVA revealed significant differences in mRNA expression levels of MT1A (p<0.05), MT1E (p<0.005), MT1F (p<0.0001), MT1G (p<0.005), MT1X (p<0.0005) and MT2A (p<0.005) in the analyzed samples. Post hoc analysis confirmed a significantly lower expression of MT1A mRNA in PTC compared to NG (p<0.05). Significant down-regulation was also noted for other MT isoforms in PTC in comparison to NG: MT1E (p<0.05), MT1F (p<0.0001), MT1G (p<0.005), MT1X (p<0.0005) and MT2A (p<0.05). In addition, significant down-regulation of MT1F and MT1G in FA compared to NG was observed (p<0.005 and p<0.05, respectively). CONCLUSION: Expression of functional MT isoforms may contribute to thyroid carcinogenesis and potentially serve as a diagnostic marker in distinguishing benign and malignant lesions.
[Mh] Termos MeSH primário: Regulação Neoplásica da Expressão Gênica
Metalotioneína/genética
Neoplasias da Glândula Tireoide/genética
[Mh] Termos MeSH secundário: Adenoma/genética
Adulto
Idoso
Idoso de 80 Anos ou mais
Carcinoma/genética
Carcinoma Papilar
Feminino
Bócio Nodular/genética
Seres Humanos
Masculino
Metalotioneína/metabolismo
Meia-Idade
Isoformas de Proteínas/genética
Isoformas de Proteínas/metabolismo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protein Isoforms); 0 (RNA, Messenger); 9038-94-2 (Metallothionein)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170906
[St] Status:MEDLINE


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[PMID]:28865957
[Au] Autor:Jayawardena DP; Heinemann IU; Stillman MJ
[Ad] Endereço:Department of Biology, The University of Western Ontario, London, Ontario N6A 5B7, Canada.
[Ti] Título:Zinc binds non-cooperatively to human liver metallothionein 2a at physiological pH.
[So] Source:Biochem Biophys Res Commun;493(1):650-653, 2017 Nov 04.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Maintenance of the homeostasis of zinc is very important in regulating bodily functions. There are over 300 Zn-dependent enzymes identified where Zn(II) plays a structural or catalytic role. However, an excess of Zn(II) in a cell is toxic and free Zn(II) is tightly controlled. Metallothioneins (MTs) are small cysteine rich proteins that can bind up to seven Zn(II) and act as a Zn(II) reservoir. The MT2a isoform is predominantly found in the liver. This study focused on designing an MT2a construct of recombinant human MT2a to determine the Zn(II) binding profile of MT2a in vitro. We analyzed the pH dependence of Zn-MT2a speciation from electrospray ionization mass spectral data. At physiological pH, Zn(II) is terminally bound to the cysteine thiols of MT2a, making bead-like structures (non-cooperative metal binding), while at low pH, Zn(II) formed Zn S -MT2a clusters involving bridged cysteinyl thiols to the Zn(II) (cooperative metal binding). The Zn(II) binding profile of MT2a was compared to Zn(II) binding profile of human kidney MT1a, which was reported in literature, and found that the Zn(II) binding profile of MT2a is similar to that of MT1a. The facility of forming bead-like structures at physiological pH for Zn -MT2a means that Zn -MT2a can donate up to two Zn(II) to Zn-dependent enzymes.
[Mh] Termos MeSH primário: Fígado/química
Fígado/enzimologia
Metalotioneína/química
Metalotioneína/metabolismo
Zinco/química
Zinco/metabolismo
[Mh] Termos MeSH secundário: Sítios de Ligação
Seres Humanos
Concentração de Íons de Hidrogênio
Ligação Proteica
Mapeamento de Interação de Proteínas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MT2A protein, human); 9038-94-2 (Metallothionein); J41CSQ7QDS (Zinc)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170904
[St] Status:MEDLINE


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[PMID]:28753743
[Au] Autor:Driessnack MK; Jamwal A; Niyogi S
[Ad] Endereço:Toxicology Centre, University of Saskatchewan, 44 Campus Drive, Saskatoon, SK, Canada.
[Ti] Título:Effects of chronic exposure to waterborne copper and nickel in binary mixture on tissue-specific metal accumulation and reproduction in fathead minnow (Pimephales promelas).
[So] Source:Chemosphere;185:964-974, 2017 Oct.
[Is] ISSN:1879-1298
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The current study evaluated the interactive effects of chronic waterborne copper (Cu) and nickel (Ni) exposure on tissue-specific metal accumulation and reproductive performance in fathead minnow (Pimephales promelas). Fish trios (1 male: 2 female; n = 5-6) were exposed for 21 days to: (i) control (no added Cu or Ni), (ii) waterborne Cu (45 µg/L), (iii) waterborne Ni (270 µg/L), and (iv) binary mixture of waterborne Cu and Ni (45 and 270 µg/L, respectively). Fish fecundity (cumulative egg production) was found to be the most sensitive reproductive endpoint, and the interaction of Cu and Ni elicited an additive effect on egg production. Tissue-specific accumulation of both metals was not influenced by the interaction of Cu and Ni, except an increased Cu and Ni burden in the carcass and ovary, respectively, were recorded. The expressions of hepatic estrogen receptor genes (ER-α and ER-ß) and the circulating estradiol level in females were also not affected by the metal-mixture treatment. However, co-exposure to waterborne Cu and Ni resulted in a significant downregulation of the hepatic vitellogenin gene in females, which was associated with the maximum upregulation of the hepatic metallothionein gene. In addition, a significant alteration of ovarian histopathology (decreased abundance of post-vitellogenic follicles, and increased follicular atresia) was also observed only in females exposed to Cu and Ni in mixture. Collectively, these observations suggest that chronic waterborne exposure to Cu and Ni in binary mixture may impair fish reproductive capacity by inducing histopathological damage in ovarian tissue, and disrupting of energy homeostasis in fish.
[Mh] Termos MeSH primário: Cobre/toxicidade
Cyprinidae/fisiologia
Níquel/toxicidade
Poluentes Químicos da Água/toxicidade
[Mh] Termos MeSH secundário: Animais
Cobre/metabolismo
Feminino
Fertilidade
Masculino
Metalotioneína/metabolismo
Níquel/metabolismo
Reprodução/efeitos dos fármacos
Testes de Toxicidade Crônica
Vitelogeninas/metabolismo
Poluentes Químicos da Água/análise
Poluentes Químicos da Água/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Vitellogenins); 0 (Water Pollutants, Chemical); 789U1901C5 (Copper); 7OV03QG267 (Nickel); 9038-94-2 (Metallothionein)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171011
[Lr] Data última revisão:
171011
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170730
[St] Status:MEDLINE


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[PMID]:28731302
[Au] Autor:Wong DL; Merrifield-MacRae ME; Stillman MJ
[Ti] Título:Lead(II) Binding in Metallothioneins.
[So] Source:Met Ions Life Sci;17, 2017 04 10.
[Is] ISSN:1559-0836
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Heavy metal exposure has long been associated with metallothionein (MT) regulation and its functions. MT is a ubiquitous, cysteine-rich protein that is involved in homeostatic metal response for the essential metals zinc and copper, as well as detoxification of heavy metals; the most commonly proposed being cadmium. MT binds in vivo to a number of metals in addition to zinc, cadmium and copper, such as bismuth. In vitro, metallation with a wide range of metals (especially mercury, arsenic, and lead) has been reported using a variety of analytical methods. To fully understand MT and its role with lead metabolism, we will describe how MT interacts with a wide variety of metals that bind in vitro. In general, affinity to the metal-binding cysteine residues of MT follows that of metal binding to thiols: Zn(II) < Pb(II) < Cd (II) < Cu(I) < Ag(I) < Hg(II) < Bi(III). To introduce the metal binding properties that we feel directly relate to the metallation of metallothionein by Pb(II), we will explore MT's interactions with metals long known as toxic, particularly, Cd(II), Hg(II), and As(III), along with xenobiotic metals, and how these metal-binding studies complement those of lead binding. Lead's effects on an organism's physiological functions are not fully understood, but it is known that chronic exposure inflicts amongst other factors pernicious anemia and developmental issues in the brain, especially in children who are more vulnerable to its toxic effects. Understanding the interaction of lead with metallothioneins throughout the biosphere, from bacteria, to algae, to fish, to humans, is important in determining pathways for lead to enter and damage physiologically significant protein function, and thereby its toxicity.
[Mh] Termos MeSH primário: Chumbo/química
Metalotioneína/química
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Intoxicação por Chumbo
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
2P299V784P (Lead); 9038-94-2 (Metallothionein)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170914
[Lr] Data última revisão:
170914
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170722
[St] Status:MEDLINE


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[PMID]:28709982
[Au] Autor:Bengalli R; Gualtieri M; Capasso L; Urani C; Camatini M
[Ad] Endereço:Department of Earth and Environmental Sciences, University of Milan Bicocca, Piazza della Scienza 1, 20126, Milan, Italy; POLARIS Research Centre, University of Milan Bicocca, Piazza della Scienza 1, 20126, Milan, Italy. Electronic address: rossella.bengalli@unimib.it.
[Ti] Título:Impact of zinc oxide nanoparticles on an in vitro model of the human air-blood barrier.
[So] Source:Toxicol Lett;279:22-32, 2017 Sep 05.
[Is] ISSN:1879-3169
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The inhalation of zinc oxide nanoparticles (nZnO) may induce systemic diseases, damages to the alveolar epithelium and inflammatory response to endothelial cells. In this work the use of an in vitro air-blood barrier (ABB) model provided a tool to elucidate the biological mechanisms underlying the potential effects of inhaled nanoparticles (NPs). The ABB model used is composed of a Transwell co-culture of a lung epithelial cell line (NCI-H441) and an immortalized pulmonary microvascular endothelial cell line (HPMEC-ST1.6R). In addition, a tri-culture model was developed by adding monocytes (THP-1) on the basal compartment of the inserts. These models have been set up to analyse the importance of the interplay among the different cell types on various responses after nZnO exposure: inflammation, endothelial damage and modulation of the immune system. The barrier integrity was assessed by measuring the transepithelial electrical resistance (TEER); the pro-inflammatory and immune cells responses were analysed by ELISA. The results have evidenced that nZnO do not affect the barrier integrity, since no TEER reduction was measured after 24h of exposure, but an activation of endothelial cells, which released pro-inflammatory mediators (IL-6, IL-8), and endothelial dysfunction markers (sICAM-1 and sVCAM-1) were induced. These results confirm that apical exposure to NPs promote endothelium activation. The in vitro-ABB model here used is thus a useful tool able to evidence the interaction between lung epithelium and endothelium in inducing biological response, and the role of endothelium dysfunction following NPs inhalation.
[Mh] Termos MeSH primário: Barreira Alveolocapilar/efeitos dos fármacos
Células Endoteliais/efeitos dos fármacos
Células Epiteliais/efeitos dos fármacos
Nanopartículas Metálicas/toxicidade
Monócitos/efeitos dos fármacos
Óxido de Zinco/toxicidade
[Mh] Termos MeSH secundário: Barreira Alveolocapilar/metabolismo
Barreira Alveolocapilar/patologia
Linhagem Celular Tumoral
Técnicas de Cocultura
Relação Dose-Resposta a Droga
Condutividade Elétrica
Células Endoteliais/metabolismo
Células Endoteliais/patologia
Células Epiteliais/metabolismo
Células Epiteliais/patologia
Seres Humanos
Mediadores da Inflamação/metabolismo
Molécula 1 de Adesão Intercelular/metabolismo
Interleucina-6/metabolismo
Interleucina-8/metabolismo
Metalotioneína/metabolismo
Monócitos/metabolismo
Monócitos/patologia
Permeabilidade
Junções Íntimas/efeitos dos fármacos
Junções Íntimas/metabolismo
Junções Íntimas/patologia
Molécula 1 de Adesão de Célula Vascular/metabolismo
Proteína da Zônula de Oclusão-1/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ICAM1 protein, human); 0 (IL6 protein, human); 0 (IL8 protein, human); 0 (Inflammation Mediators); 0 (Interleukin-6); 0 (Interleukin-8); 0 (TJP1 protein, human); 0 (Vascular Cell Adhesion Molecule-1); 0 (Zonula Occludens-1 Protein); 126547-89-5 (Intercellular Adhesion Molecule-1); 9038-94-2 (Metallothionein); SOI2LOH54Z (Zinc Oxide)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170716
[St] Status:MEDLINE



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