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[PMID]:28684420
[Au] Autor:Motl N; Skiba MA; Kabil O; Smith JL; Banerjee R
[Ad] Endereço:From the Department of Biological Chemistry, University of Michigan Medical Center, Ann Arbor, Michigan 48109-0600 and.
[Ti] Título:Structural and biochemical analyses indicate that a bacterial persulfide dioxygenase-rhodanese fusion protein functions in sulfur assimilation.
[So] Source:J Biol Chem;292(34):14026-14038, 2017 Aug 25.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hydrogen sulfide (H S) is a signaling molecule that is toxic at elevated concentrations. In eukaryotes, it is cleared via a mitochondrial sulfide oxidation pathway, which comprises sulfide quinone oxidoreductase, persulfide dioxygenase (PDO), rhodanese, and sulfite oxidase and converts H S to thiosulfate and sulfate. Natural fusions between the non-heme iron containing PDO and rhodanese, a thiol sulfurtransferase, exist in some bacteria. However, little is known about the role of the PDO-rhodanese fusion (PRF) proteins in sulfur metabolism. Herein, we report the kinetic properties and the crystal structure of a PRF from the Gram-negative endophytic bacterium The crystal structures of wild-type PRF and a sulfurtransferase-inactivated C314S mutant with and without glutathione were determined at 1.8, 2.4, and 2.7 Å resolution, respectively. We found that the two active sites are distant and do not show evidence of direct communication. The PRF exhibited robust PDO activity and preferentially catalyzed sulfur transfer in the direction of thiosulfate to sulfite and glutathione persulfide; sulfur transfer in the reverse direction was detectable only under limited turnover conditions. Together with the kinetic data, our bioinformatics analysis reveals that PRF is poised to metabolize thiosulfate to sulfite in a sulfur assimilation pathway rather than in sulfide stress response as seen, for example, with the PRF or sulfide oxidation and disposal as observed with the homologous mammalian proteins.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Burkholderiaceae/enzimologia
Modelos Moleculares
Proteínas Mutantes Quiméricas/metabolismo
Quinona Redutases/metabolismo
Tiossulfato Sulfurtransferase/metabolismo
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Apoenzimas/química
Apoenzimas/genética
Apoenzimas/metabolismo
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Biocatálise
Domínio Catalítico
Biologia Computacional
Cristalografia por Raios X
Cisteína/química
Dissulfetos/metabolismo
Estabilidade Enzimática
Glutationa/análogos & derivados
Glutationa/química
Glutationa/metabolismo
Sulfeto de Hidrogênio/metabolismo
Proteínas Mutantes Quiméricas/química
Proteínas Mutantes Quiméricas/genética
Mutação
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Conformação Proteica
Quinona Redutases/química
Quinona Redutases/genética
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Tiossulfato Sulfurtransferase/química
Tiossulfato Sulfurtransferase/genética
Tiossulfatos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Apoenzymes); 0 (Bacterial Proteins); 0 (Disulfides); 0 (Mutant Chimeric Proteins); 0 (Peptide Fragments); 0 (Recombinant Proteins); 0 (Thiosulfates); 0 (glutathione persulfide); EC 1.6.99.- (Quinone Reductases); EC 1.8.5.- (sulfide quinone reductase); EC 2.8.1.1 (Thiosulfate Sulfurtransferase); GAN16C9B8O (Glutathione); K848JZ4886 (Cysteine); YY9FVM7NSN (Hydrogen Sulfide)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170708
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.790170


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[PMID]:28346391
[Au] Autor:Bronowicka-Adamska P; Wróbel M; Magierowski M; Magierowska K; Kwiecien S; Brzozowski T
[Ad] Endereço:Chair of Medical Biochemistry, Jagiellonian University Medical College, Krakow, 7 Kopernika St., 31-034 Cracow, Poland. mbbronow@cyf-kr.edu.pl.
[Ti] Título:Hydrogen Sulphide Production in Healthy and Ulcerated Gastric Mucosa of Rats.
[So] Source:Molecules;22(4), 2017 Mar 27.
[Is] ISSN:1420-3049
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Hydrogen sulphide (H2S) is produced endogenously via two enzymes dependent on pyridoxal phosphate (PLP): cystathionine beta-synthase (CBS, EC 4.2.1.22), cystathionase γ-liase (CTH, EC 4.4.1.1), and a third, 3-mercaptopyruvate sulfurtransferase (MPST, EC 2.8.1.2). H2S strengthens the defence mechanisms of the gastric mucosal barrier, and plays an important role in gastroprotection, including the increased resistance to damage caused by various irritants and non-steroidal anti-inflammatory drugs. The study was conducted to determine the role of H2S in ulcerated gastric mucosa of rats caused by immobilization in cold water (WRS). The activity and expression of γ-cystathionase, cystathionine ß-synthase, 3-mercaptopyruvate sulfurtransferase, and rhodanese was compared with healthy mucosa, together with H2S generation, and cysteine, glutathione, and cystathionine levels. The results showed that the defence mechanism against stress is associated with stimulation of the production of H2S in the tissue and confirmed the observed advantageous effect of H2S on healing of gastric ulcers. In case of animals pretreated with exogenous sources of H2S and NaHS, and some changes observed in the ulcerated gastric mucosa tend to return to values found in the healthy tissue, a finding that is in accordance with the previously determined gastroprotective properties of H2S. The results presented in this paper point to the possible role of rhodanese in H2S production in the gastric mucosa of rats, together with the earlier mentioned three enzymes, which are all active in this tissue.
[Mh] Termos MeSH primário: Mucosa Gástrica/metabolismo
Sulfeto de Hidrogênio/administração & dosagem
Úlcera Gástrica/tratamento farmacológico
[Mh] Termos MeSH secundário: Animais
Cistationina beta-Sintase/metabolismo
Cistationina gama-Liase/metabolismo
Modelos Animais de Doenças
Mucosa Gástrica/efeitos dos fármacos
Mucosa Gástrica/patologia
Regulação Enzimológica da Expressão Gênica/efeitos dos fármacos
Sulfeto de Hidrogênio/metabolismo
Masculino
Ratos
Úlcera Gástrica/metabolismo
Sulfurtransferases/metabolismo
Tiossulfato Sulfurtransferase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.8.1.- (Sulfurtransferases); EC 2.8.1.1 (Thiosulfate Sulfurtransferase); EC 2.8.1.2 (3-mercaptopyruvate sulphurtransferase); EC 4.2.1.22 (Cystathionine beta-Synthase); EC 4.4.1.1 (Cystathionine gamma-Lyase); YY9FVM7NSN (Hydrogen Sulfide)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170517
[Lr] Data última revisão:
170517
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170328
[St] Status:MEDLINE


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[PMID]:27878988
[Au] Autor:Shigi N; Asai SI; Watanabe K
[Ad] Endereço:Biotechnology Research Institute for Drug Discovery, National Institute of Advanced Industrial Science and Technology (AIST), Tokyo, Japan.
[Ti] Título:Identification of a rhodanese-like protein involved in thiouridine biosynthesis in Thermus thermophilus tRNA.
[So] Source:FEBS Lett;590(24):4628-4637, 2016 Dec.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Incorporation of a sulfur atom into 2-thioribothymidine (s T or 5-methyl-2-thiouridine) at position 54 in thermophile tRNA is accomplished by an elaborate system composed of many proteins which confers thermostability to the translation system. We identified ttuD (tRNA-two-thiouridine D) as a gene for the synthesis of s T54 in Thermus thermophilus. The rhodanese-like protein TtuD enhances the activity of cysteine desulfurases and receives the persulfide generated by cysteine desulfurases in vitro. TtuD also enhances the formation of thiocarboxylated TtuB, the sulfur donor for the tRNA sulfurtransferase TtuA. Since cysteine desulfurases are the first enzymes in the synthesis of s T and other sulfur-containing compounds, TtuD has a role to direct sulfur flow to s T synthesis.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
RNA de Transferência/metabolismo
Sulfurtransferases/metabolismo
Thermus thermophilus/química
Tiouridina/análogos & derivados
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Bactérias/genética
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Mimetismo Molecular
RNA Bacteriano/genética
RNA Bacteriano/metabolismo
RNA de Transferência/genética
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
Sulfurtransferases/genética
Thermus thermophilus/enzimologia
Tiossulfato Sulfurtransferase/genética
Tiossulfato Sulfurtransferase/metabolismo
Tiouridina/metabolismo
[Pt] Tipo de publicação:LETTER
[Nm] Nome de substância:
0 (2-thiouridine); 0 (Bacterial Proteins); 0 (RNA, Bacterial); 0 (Recombinant Proteins); 13957-31-8 (Thiouridine); 32738-09-3 (2-thioribothymidine); 9014-25-9 (RNA, Transfer); EC 2.8.1.- (Sulfurtransferases); EC 2.8.1.- (thiouridine-tRNA sulfurtransferase); EC 2.8.1.1 (Thiosulfate Sulfurtransferase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170515
[Lr] Data última revisão:
170515
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161124
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12499


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[PMID]:27473602
[Au] Autor:Eichmann C; Tzitzilonis C; Nakamura T; Kwiatkowski W; Maslennikov I; Choe S; Lipton SA; Riek R
[Ad] Endereço:Laboratory of Physical Chemistry, Swiss Federal Institute of Technology, ETH-Hönggerberg, CH-8093 Zürich, Switzerland.
[Ti] Título:S-Nitrosylation Induces Structural and Dynamical Changes in a Rhodanese Family Protein.
[So] Source:J Mol Biol;428(19):3737-51, 2016 Sep 25.
[Is] ISSN:1089-8638
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:S-Nitrosylation is well established as an important post-translational regulator in protein function and signaling. However, relatively little is known about its structural and dynamical consequences. We have investigated the effects of S-nitrosylation on the rhodanese domain of the Escherichia coli integral membrane protein YgaP by NMR, X-ray crystallography, and mass spectrometry. The results show that the active cysteine in the rhodanese domain of YgaP is subjected to two competing modifications: S-nitrosylation and S-sulfhydration, which are naturally occurring in vivo. It has been observed that in addition to inhibition of the sulfur transfer activity, S-nitrosylation of the active site residue Cys63 causes an increase in slow motion and a displacement of helix 5 due to a weakening of the interaction between the active site and the helix dipole. These findings provide an example of how nitrosative stress can exert action at the atomic level.
[Mh] Termos MeSH primário: Proteínas de Escherichia coli/química
Proteínas de Escherichia coli/metabolismo
Escherichia coli/enzimologia
Processamento de Proteína Pós-Traducional
Tiossulfato Sulfurtransferase/química
Tiossulfato Sulfurtransferase/metabolismo
[Mh] Termos MeSH secundário: Domínio Catalítico
Cristalografia por Raios X
Cisteína/metabolismo
Espectroscopia de Ressonância Magnética
Espectrometria de Massas
Modelos Moleculares
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (YgaP protein, E coli); EC 2.8.1.1 (Thiosulfate Sulfurtransferase); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170619
[Lr] Data última revisão:
170619
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160731
[St] Status:MEDLINE


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[PMID]:27287690
[Au] Autor:Beltram J; Morton NM; Kunej T; Horvat S
[Ad] Endereço:Biotechnical Faculty, Animal Science Department, University of Ljubljana, Groblje 3, 1230, Domzale, Slovenia.
[Ti] Título:Construction of an integrative regulatory element and variation map of the murine Tst locus.
[So] Source:BMC Genet;17(1):77, 2016 Jun 11.
[Is] ISSN:1471-2156
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Given the abundance of new genomic projects and gene annotations, researchers trying to pinpoint causal genetic variants are faced with a challenging task of how to efficiently integrate all current genomic information. The objective of the study was to develop an approach to integrate various genomic annotations for a recently positionally-cloned Tst gene (Thiosulfate Sulfur Transferase, synonym Rhodanese) responsible for the Fob3b2 QTL effect on leanness and improved metabolic parameters. The second aim was to identify and prioritize Tst genetic variants that may be causal for the phenotypic effects. RESULTS: A bioinformatics approach was developed to integrate existing knowledge of regulatory elements of the Tst gene. The entire Tst locus along with flanking segments was sequenced between our unique polygenic mouse Fat and Lean strains that were generated by divergent selection on adiposity for over 60 generations. The bioinformatics-generated regulatory element map of the Tst locus was then combined with genetic variants between the Fat and Lean mice and with comparative analyses of polymorphisms across 17 mouse strains in order to prioritise likely causal polymorphisms. Two candidate regulatory variants were identified, one overlapping an evolutionary constrained Tst intronic element and the other residing in the seed region of a predicted 3'UTR miRNA binding site. CONCLUSIONS: This study developed a map of regulatory elements for the Tst locus in mice and identified candidate genetic variants with increased causal likelihood. This map provides a basis for experimental validation and functional analyses of this novel candidate leanness and antidiabetic gene. Our methodological approach is of general utility for analyzing regulation of loci that have limited annotations and experimental evidence and for identifying candidate causal regulatory genetic variants in post-GWAS or post-QTL- cloning studies.
[Mh] Termos MeSH primário: Obesidade/genética
Sequências Reguladoras de Ácido Nucleico
Magreza/genética
Tiossulfato Sulfurtransferase/genética
[Mh] Termos MeSH secundário: Regiões 3' não Traduzidas
Animais
Biologia Computacional/métodos
Loci Gênicos
Camundongos
MicroRNAs/metabolismo
Anotação de Sequência Molecular
Fenótipo
Locos de Características Quantitativas
Análise de Sequência de DNA
Tiossulfato Sulfurtransferase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (3' Untranslated Regions); 0 (MicroRNAs); EC 2.8.1.1 (Thiosulfate Sulfurtransferase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170921
[Lr] Data última revisão:
170921
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160612
[St] Status:MEDLINE
[do] DOI:10.1186/s12863-016-0381-6


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[PMID]:27270587
[Au] Autor:Morton NM; Beltram J; Carter RN; Michailidou Z; Gorjanc G; McFadden C; Barrios-Llerena ME; Rodriguez-Cuenca S; Gibbins MT; Aird RE; Moreno-Navarrete JM; Munger SC; Svenson KL; Gastaldello A; Ramage L; Naredo G; Zeyda M; Wang ZV; Howie AF; Saari A; Sipilä P; Stulnig TM; Gudnason V; Kenyon CJ; Seckl JR; Walker BR; Webster SP; Dunbar DR; Churchill GA; Vidal-Puig A; Fernandez-Real JM; Emilsson V; Horvat S
[Ad] Endereço:University-British Heart Foundation Centre for Cardiovascular Science, University of Edinburgh, Queen's Medical Research Institute, Edinburgh, UK.
[Ti] Título:Genetic identification of thiosulfate sulfurtransferase as an adipocyte-expressed antidiabetic target in mice selected for leanness.
[So] Source:Nat Med;22(7):771-9, 2016 Jul.
[Is] ISSN:1546-170X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The discovery of genetic mechanisms for resistance to obesity and diabetes may illuminate new therapeutic strategies for the treatment of this global health challenge. We used the polygenic 'lean' mouse model, which has been selected for low adiposity over 60 generations, to identify mitochondrial thiosulfate sulfurtransferase (Tst; also known as rhodanese) as a candidate obesity-resistance gene with selectively increased expression in adipocytes. Elevated adipose Tst expression correlated with indices of metabolic health across diverse mouse strains. Transgenic overexpression of Tst in adipocytes protected mice from diet-induced obesity and insulin-resistant diabetes. Tst-deficient mice showed markedly exacerbated diabetes, whereas pharmacological activation of TST ameliorated diabetes in mice. Mechanistically, TST selectively augmented mitochondrial function combined with degradation of reactive oxygen species and sulfide. In humans, TST mRNA expression in adipose tissue correlated positively with insulin sensitivity in adipose tissue and negatively with fat mass. Thus, the genetic identification of Tst as a beneficial regulator of adipocyte mitochondrial function may have therapeutic significance for individuals with type 2 diabetes.
[Mh] Termos MeSH primário: Adipócitos/metabolismo
Tecido Adiposo/metabolismo
Diabetes Mellitus Experimental/genética
Diabetes Mellitus Tipo 2/genética
Resistência à Insulina/genética
Mitocôndrias/metabolismo
Obesidade/genética
Tiossulfato Sulfurtransferase/genética
[Mh] Termos MeSH secundário: Animais
Diferenciação Celular
Diabetes Mellitus Experimental/metabolismo
Diabetes Mellitus Tipo 2/metabolismo
Dieta Hiperlipídica
Técnicas de Introdução de Genes
Técnica Clamp de Glucose
Teste de Tolerância a Glucose
Seres Humanos
Camundongos
Camundongos Endogâmicos
Camundongos Transgênicos
Modelos Animais
Terapia de Alvo Molecular
Obesidade/metabolismo
RNA Mensageiro/metabolismo
Reação em Cadeia da Polimerase em Tempo Real
Tiossulfato Sulfurtransferase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Messenger); EC 2.8.1.1 (Thiosulfate Sulfurtransferase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160609
[St] Status:MEDLINE
[do] DOI:10.1038/nm.4115


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[PMID]:27073879
[Au] Autor:Jäger G; Chen P; Björk GR
[Ad] Endereço:Department of Molecular Biology, Umeå university, 901 87, Umeå, Sweden.
[Ti] Título:Transfer RNA Bound to MnmH Protein Is Enriched with Geranylated tRNA--A Possible Intermediate in Its Selenation?
[So] Source:PLoS One;11(4):e0153488, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The wobble nucleoside 5-methylaminomethyl-2-thio-uridine (mnm5s2U) is present in bacterial tRNAs specific for Lys and Glu and 5-carboxymethylaminomethyl-2-thio-uridine (cmnm5s2U) in tRNA specific for Gln. The sulfur of (c)mnm5s2U may be exchanged by selenium (Se)-a reaction catalyzed by the selenophosphate-dependent tRNA 2-selenouridine synthase encoded by the mnmH (ybbB, selU, sufY) gene. The MnmH protein has a rhodanese domain containing one catalytic Cys (C97) and a P-loop domain containing a Walker A motif, which is a potential nucleotide binding site. We have earlier isolated a mutant of Salmonella enterica, serovar Typhimurium with an alteration in the rhodanese domain of the MnmH protein (G67E) mediating the formation of modified nucleosides having a geranyl (ge)-group (C10H17-fragment) attached to the s2 group of mnm5s2U and of cmnm5s2U in tRNA. To further characterize the structural requirements to increase the geranylation activity, we here report the analysis of 39 independently isolated mutants catalyzing the formation of mnm5ges2U. All these mutants have amino acid substitutions in the rhodanese domain demonstrating that this domain is pivotal to increase the geranylation activity. The wild type form of MnmH+ also possesses geranyltransferase activity in vitro although only a small amount of the geranyl derivatives of (c)mnm5s2U is detected in vivo. The selenation activity in vivo has an absolute requirement for the catalytic Cys97 in the rhodanese domain whereas the geranylation activity does not. Clearly, MnmH has two distinct enzymatic activities for which the rhodanese domain is pivotal. An intact Walker motif in the P-loop domain is required for the geranylation activity implying that it is the binding site for geranylpyrophosphate (GePP), which is the donor molecule in vitro in the geranyltransfer reaction. Purified MnmH from wild type and from the MnmH(G67E) mutant have bound tRNA, which is enriched with geranylated tRNA. This in conjunction with earlier published data, suggests that this bound geranylated tRNA may be an intermediate in the selenation of the tRNA.
[Mh] Termos MeSH primário: RNA Bacteriano/metabolismo
RNA de Transferência/metabolismo
Selênio/metabolismo
Sulfurtransferases/metabolismo
[Mh] Termos MeSH secundário: Sítios de Ligação
Escherichia coli/genética
Fosfatos/metabolismo
RNA Bacteriano/genética
RNA de Transferência/genética
Salmonella typhimurium/genética
Compostos de Selênio/metabolismo
Sulfurtransferases/genética
Tiossulfato Sulfurtransferase/genética
Tiossulfato Sulfurtransferase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Phosphates); 0 (RNA, Bacterial); 0 (Selenium Compounds); 12509-41-0 (selenophosphate); 9014-25-9 (RNA, Transfer); EC 2.8.1.- (Sulfurtransferases); EC 2.8.1.- (tRNA 2-selenouridine synthase); EC 2.8.1.1 (Thiosulfate Sulfurtransferase); H6241UJ22B (Selenium)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160414
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0153488


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[PMID]:26939832
[Au] Autor:Rockwood GA; Thompson DE; Petrikovics I
[Ad] Endereço:Analytical Toxicology Division, US Army Medical Research Institute of Chemical Defense, Aberdeen Proving Ground, MD, USA gary.a.rockwood.civ@mail.mil.
[Ti] Título:Dimethyl trisulfide: A novel cyanide countermeasure.
[So] Source:Toxicol Ind Health;32(12):2009-2016, 2016 Dec.
[Is] ISSN:1477-0393
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In the present studies, the in vitro and in vivo efficacies of a novel cyanide countermeasure, dimethyl trisulfide (DMTS), were evaluated. DMTS is a sulfur-based molecule found in garlic, onion, broccoli, and similar plants. DMTS was studied for effectiveness as a sulfur donor-type cyanide countermeasure. The sulfur donor reactivity of DMTS was determined by measuring the rate of the formation of the cyanide metabolite thiocyanate. In experiments carried out in vitro in the presence of the sulfurtransferase rhodanese (Rh) and at the experimental pH of 7.4, DMTS was observed to convert cyanide to thiocyanate with greater than 40 times higher efficacy than does thiosulfate, the sulfur donor component of the US Food and Drug Administration-approved cyanide countermeasure Nithiodote In the absence of Rh, DMTS was observed to be almost 80 times more efficient than sodium thiosulfate in vitro The fact that DMTS converts cyanide to thiocyanate more efficiently than does thiosulfate both with and without Rh makes it a promising sulfur donor-type cyanide antidote (scavenger) with reduced enzyme dependence in vitro The therapeutic cyanide antidotal efficacies for DMTS versus sodium thiosulfate were measured following intramuscular administration in a mouse model and expressed as antidotal potency ratios (APR = LD of cyanide with antidote/LD of cyanide without antidote). A dose of 100 mg/kg sodium thiosulfate given intramuscularly showed only slight therapeutic protection (APR = 1.1), whereas the antidotal protection from DMTS given intramuscularly at the same dose was substantial (APR = 3.3). Based on these data, DMTS will be studied further as a promising next-generation countermeasure for cyanide intoxication.
[Mh] Termos MeSH primário: Antídotos/farmacologia
Cianetos/toxicidade
Sulfetos/farmacologia
[Mh] Termos MeSH secundário: Animais
Antídotos/química
Brassica/química
Cianetos/química
Modelos Animais de Doenças
Relação Dose-Resposta a Droga
Alho/química
Concentração de Íons de Hidrogênio
Injeções Intramusculares
Dose Letal Mediana
Masculino
Camundongos
Cebolas/química
Tiocianatos/metabolismo
Tiossulfato Sulfurtransferase/metabolismo
Tiossulfatos/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antidotes); 0 (Cyanides); 0 (Sulfides); 0 (Thiocyanates); 0 (Thiosulfates); 302-04-5 (thiocyanate); 3E691T3NL1 (dimethyl trisulfide); EC 2.8.1.1 (Thiosulfate Sulfurtransferase); HX1032V43M (sodium thiosulfate)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170417
[Lr] Data última revisão:
170417
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160305
[St] Status:MEDLINE


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[PMID]:26845441
[Au] Autor:Daniyan MO; Boshoff A; Prinsloo E; Pesce ER; Blatch GL
[Ad] Endereço:Biomedical Biotechnology Research Unit, Department of Biochemistry and Microbiology, Rhodes University, Grahamstown, South Africa.
[Ti] Título:The Malarial Exported PFA0660w Is an Hsp40 Co-Chaperone of PfHsp70-x.
[So] Source:PLoS One;11(2):e0148517, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Plasmodium falciparum, the human pathogen responsible for the most dangerous malaria infection, survives and develops in mature erythrocytes through the export of proteins needed for remodelling of the host cell. Molecular chaperones of the heat shock protein (Hsp) family are prominent members of the exportome, including a number of Hsp40s and a Hsp70. PFA0660w, a type II Hsp40, has been shown to be exported and possibly form a complex with PfHsp70-x in the infected erythrocyte cytosol. However, the chaperone properties of PFA0660w and its interaction with human and parasite Hsp70s are yet to be investigated. Recombinant PFA0660w was found to exist as a monomer in solution, and was able to significantly stimulate the ATPase activity of PfHsp70-x but not that of a second plasmodial Hsp70 (PfHsp70-1) or a human Hsp70 (HSPA1A), indicating a potential specific functional partnership with PfHsp70-x. Protein binding studies in the presence and absence of ATP suggested that the interaction of PFA0660w with PfHsp70-x most likely represented a co-chaperone/chaperone interaction. Also, PFA0660w alone produced a concentration-dependent suppression of rhodanese aggregation, demonstrating its chaperone properties. Overall, we have provided the first biochemical evidence for the possible role of PFA0660w as a chaperone and as co-chaperone of PfHsp70-x. We propose that these chaperones boost the chaperone power of the infected erythrocyte, enabling successful protein trafficking and folding, and thereby making a fundamental contribution to the pathology of malaria.
[Mh] Termos MeSH primário: Proteínas de Choque Térmico HSP40/metabolismo
Proteínas de Choque Térmico HSP70/metabolismo
Chaperonas Moleculares/metabolismo
Plasmodium falciparum/metabolismo
Proteínas de Protozoários/metabolismo
[Mh] Termos MeSH secundário: Adenosina Trifosfatases/metabolismo
Proteínas de Choque Térmico HSP40/química
Proteínas de Choque Térmico HSP40/genética
Proteínas de Choque Térmico HSP40/isolamento & purificação
Proteínas de Choque Térmico HSP70/química
Proteínas de Choque Térmico HSP70/genética
Proteínas de Choque Térmico HSP70/isolamento & purificação
Seres Humanos
Cinética
Malária Falciparum/parasitologia
Chaperonas Moleculares/química
Chaperonas Moleculares/genética
Chaperonas Moleculares/isolamento & purificação
Plasmodium falciparum/genética
Agregados Proteicos
Ligação Proteica
Proteínas de Protozoários/química
Proteínas de Protozoários/genética
Proteínas de Protozoários/isolamento & purificação
Proteínas Recombinantes
Tiossulfato Sulfurtransferase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (HSP40 Heat-Shock Proteins); 0 (HSP70 Heat-Shock Proteins); 0 (Molecular Chaperones); 0 (Protein Aggregates); 0 (Protozoan Proteins); 0 (Recombinant Proteins); EC 2.8.1.1 (Thiosulfate Sulfurtransferase); EC 3.6.1.- (Adenosine Triphosphatases)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160205
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0148517


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[PMID]:26836478
[Au] Autor:de Araújo FT; Caseli L
[Ad] Endereço:Institute of Environmental, Chemical and Pharmaceutical Sciences, Federal University of São Paulo, Diadema, SP, Brazil.
[Ti] Título:Rhodanese incorporated in Langmuir and Langmuir-Blodgett films of dimyristoylphosphatidic acid: Physical chemical properties and improvement of the enzyme activity.
[So] Source:Colloids Surf B Biointerfaces;141:59-64, 2016 May 01.
[Is] ISSN:1873-4367
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Preserving the catalytic activity of enzymes immobilized in bioelectronics devices is essential for optimal performance in biosensors. Therefore, ultrathin films in which the architecture can be controlled at the molecular level are of interest. In this work, the enzyme rhodanese was adsorbed onto Langmuir monolayers of the phospholipid dimyristoylphosphatidic acid and characterized by surface pressure-area isotherms, polarization-modulated infrared reflection-absorption spectroscopy (PM-IRRAS), and Brewster angle microscopy (BAM). The incorporation of the enzyme (5% in mol) in the lipid monolayer expanded the film, providing small surface domains, as visualized by BAM. Also, amide bands could be identified in the PM-IRRAS spectra, confirming the presence of the enzyme at the air-water interface. Structuring of the enzyme into α-helices was identified in the mixed monolayer and was preserved when the film was transferred from the liquid interface to solids supports as Langmuir-Blodgett (LB) films. The enzyme-lipid LB films were then characterized by fluorescence spectroscopy, PM-IRRAS, and atomic force microscopy. Measurements of the catalytic activity towards cyanide showed that the enzyme accommodated in the LB films preserved more than 87% of the enzyme activity in relation to the homogeneous medium. After 1 month, the enzyme in the LB film maintained 85% of the activity in contrast to the homogeneous medium, which 24% of the enzyme activity was kept. The method presented in this work not only points to an enhanced catalytic activity toward cyanide, but also may explain why certain film architectures exhibit an improved performance.
[Mh] Termos MeSH primário: Enzimas Imobilizadas/metabolismo
Glicerofosfolipídeos/química
Tiossulfato Sulfurtransferase/metabolismo
Lipossomas Unilamelares/metabolismo
[Mh] Termos MeSH secundário: Adsorção
Técnicas Biossensoriais/métodos
Ensaios Enzimáticos
Enzimas Imobilizadas/química
Cinética
Microscopia de Força Atômica
Espectrometria de Fluorescência
Espectrofotometria Infravermelho
Propriedades de Superfície
Termodinâmica
Tiossulfato Sulfurtransferase/química
Lipossomas Unilamelares/química
Água/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Enzymes, Immobilized); 0 (Glycerophospholipids); 0 (Unilamellar Liposomes); 059QF0KO0R (Water); 30170-00-4 (dimyristoylphosphatidic acid); EC 2.8.1.1 (Thiosulfate Sulfurtransferase)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:170912
[Lr] Data última revisão:
170912
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160203
[St] Status:MEDLINE



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