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[PMID]:28454695
[Au] Autor:Hu TX; Guo X; Wang G; Gao L; He P; Xia Y; Gu H; Ni X
[Ad] Endereço:Department of Physiology, Second Military Medical University, Shanghai, China; No.117 Hospital of PLA, Hangzhou, China.
[Ti] Título:MiR133b is involved in endogenous hydrogen sulfide suppression of sFlt-1 production in human placenta.
[So] Source:Placenta;52:33-40, 2017 Apr.
[Is] ISSN:1532-3102
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Increased production of soluble fms-like tyrosine kinase-1 (sFlt-1) from placenta is one of the major contributors to the development of preeclampsia. Our previous study has shown that hydrogen sulfide (H S) inhibits sFlt-1 release in placenta. In the present study, we sought to investigate whether endogenous H S affects sFlt-1 production and elucidate which H S-producing enzyme is responsible for its effect in placenta. It was found that, besides cystathionine ß-synthase (CBS) and cystathionine γ-lyase (CSE), 3-mercaptopyruvatesulfurtransferase (3-MST) was identified in human placenta and mainly localized in syncytiotrophoblasts. There was no significant difference in expression level of 3-MST among preeclamptic and normal placentas. Treatment of cultured syncytiotrophoblasts with NaHS and l-cysteine suppressed sFlt-1 mRNA expression and caused a decrease in sFlt-1 protein content in culture media of the cells. Transfection of syncytiotrophoblasts with CBS siRNA and CSE siRNA reversed the above effects of l-cysteine. Furthermore, NaHS and l-cysteine treatment decreased the half-life of sFlt-1 mRNA and increased the expression of miR-133b targeting sFlt-1. MiR-133b expression was downregulated in preeclamptic placentas and correlated with the level of CBS and CSE. These results indicate that H S is an important regulatory factor in sFlt-1 production in placenta. Reduced H S generation in placenta contributes to development of preeclampsia by enhancing sFlt-1 production.
[Mh] Termos MeSH primário: Sulfeto de Hidrogênio/metabolismo
MicroRNAs/metabolismo
Placenta/metabolismo
Receptor 1 de Fatores de Crescimento do Endotélio Vascular/metabolismo
[Mh] Termos MeSH secundário: Células Cultivadas
Cistationina beta-Sintase/metabolismo
Cistationina gama-Liase/metabolismo
Cisteína/farmacologia
Regulação para Baixo
Feminino
Seres Humanos
Sulfeto de Hidrogênio/farmacologia
Gravidez
Sulfurtransferases/metabolismo
Trofoblastos/efeitos dos fármacos
Trofoblastos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MIRN133 microRNA, human); 0 (MicroRNAs); EC 2.7.10.1 (FLT1 protein, human); EC 2.7.10.1 (Vascular Endothelial Growth Factor Receptor-1); EC 2.8.1.- (Sulfurtransferases); EC 2.8.1.2 (3-mercaptopyruvate sulphurtransferase); EC 4.2.1.22 (Cystathionine beta-Synthase); EC 4.4.1.1 (Cystathionine gamma-Lyase); K848JZ4886 (Cysteine); YY9FVM7NSN (Hydrogen Sulfide)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170430
[St] Status:MEDLINE


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[PMID]:29249255
[Au] Autor:Sun Q; Chen Z; He P; Li Y; Ding X; Huang Y; Gu H; Ni X
[Ad] Endereço:Department of Physiology, Second Military Medical University, Shanghai, China; Department of Gynecology and Obstetrics, Changhai Hospital, Shanghai, China.
[Ti] Título:Reduced Expression of Hydrogen Sulfide-Generating Enzymes Down-Regulates 15-Hydroxyprostaglandin Dehydrogenase in Chorion during Term and Preterm Labor.
[So] Source:Am J Pathol;188(1):63-71, 2018 01.
[Is] ISSN:1525-2191
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Chorionic NAD-dependent 15-hydroxyprostaglandin dehydrogenase (PGDH) plays a pivotal role in controlling the amount of prostaglandins in the uterus and has been implicated in the process of labor. Prior studies identified hydrogen sulfide-generating enzymes cystathionine-ß-synthetase (CBS) and cystathionine-γ-lyase (CSE) in fetal membranes. We investigated whether hydrogen sulfide is involved in the regulation of PGDH expression in the chorion during labor. The chorionic tissues were obtained from pregnant women at preterm in labor and at term in labor or not in labor at term. Levels of CSE and CBS and hydrogen sulfide production rate were down-regulated in term in labor and preterm in labor groups compared with not in labor at term group. The CBS level correlated to PGDH expression in the chorion. Hydrogen sulfide donor NaHS and precursor l-cysteine dose-dependently stimulated PGDH expression and activity in cultured chorionic trophoblasts. The effect of l-cysteine was blocked by CBS inhibitor and CBS siRNA but not by CSE inhibitor and CSE siRNA. Hydrogen sulfide treatment suppressed miR-26b and miR-199a expression in chorionic trophoblasts. miR-26b and miR-199a mimics blocked hydrogen sulfide upregulation of PGDH expression. Our results indicate that hydrogen sulfide plays pivotal roles in maintenance of PGDH expression in the chorion during human pregnancy. Reduced expression of hydrogen sulfide-generating enzymes contributes to an increased amount of prostaglandins in the uterus during labor.
[Mh] Termos MeSH primário: Córion/enzimologia
Cistationina beta-Sintase/metabolismo
Cistationina gama-Liase/metabolismo
Hidroxiprostaglandina Desidrogenases/metabolismo
Trabalho de Parto Prematuro/metabolismo
Nascimento a Termo/metabolismo
[Mh] Termos MeSH secundário: Cistationina gama-Liase/genética
Regulação para Baixo
Feminino
Seres Humanos
Sulfeto de Hidrogênio/metabolismo
Hidroxiprostaglandina Desidrogenases/genética
Trabalho de Parto Prematuro/genética
Gravidez
Nascimento a Termo/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 1.1.1.- (Hydroxyprostaglandin Dehydrogenases); EC 1.1.1.141 (15-hydroxyprostaglandin dehydrogenase); EC 4.2.1.22 (Cystathionine beta-Synthase); EC 4.4.1.1 (Cystathionine gamma-Lyase); YY9FVM7NSN (Hydrogen Sulfide)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180131
[Lr] Data última revisão:
180131
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:171219
[St] Status:MEDLINE


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[PMID]:28678427
[Au] Autor:Cochrane DR; Tessier-Cloutier B; Lawrence KM; Nazeran T; Karnezis AN; Salamanca C; Cheng AS; McAlpine JN; Hoang LN; Gilks CB; Huntsman DG
[Ad] Endereço:Department of Molecular Oncology, BC Cancer Agency, Vancouver, BC, Canada.
[Ti] Título:Clear cell and endometrioid carcinomas: are their differences attributable to distinct cells of origin?
[So] Source:J Pathol;243(1):26-36, 2017 Sep.
[Is] ISSN:1096-9896
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Endometrial epithelium is the presumed tissue of origin for both eutopic and endometriosis-derived clear cell and endometrioid carcinomas. We had previously hypothesized that the morphological, biological and clinical differences between these carcinomas are due to histotype-specific mutations. Although some mutations and genomic landscape features are more likely to be found in one of these histotypes, we were not able to identify a single class of mutations that was exclusively present in one histotype and not the other. This lack of genomic differences led us to an alternative hypothesis that these cancers could arise from distinct cells of origin within endometrial tissue, and that it is the cellular context that accounts for their differences. In a proteomic screen, we identified cystathionine γ-lyase (CTH) as a marker for clear cell carcinoma, as it is expressed at high levels in clear cell carcinomas of the ovary and endometrium. In the current study, we analysed normal Müllerian tissues, and found that CTH is expressed in ciliated cells of endometrium (both eutopic endometrium and endometriosis) and fallopian tubes. We then demonstrated that other ciliated cell markers are expressed in clear cell carcinomas, whereas endometrial secretory cell markers are expressed in endometrioid carcinomas. The same differential staining of secretory and ciliated cells was demonstrable in a three-dimensional organoid culture system, in which stem cells were stimulated to differentiate into an admixture of secretory and ciliated cells. These data suggest that endometrioid carcinomas are derived from cells of the secretory cell lineage, whereas clear cell carcinomas are derived from, or have similarities to, cells of the ciliated cell lineage. Copyright © 2017 Pathological Society of Great Britain and Ireland. Published by John Wiley & Sons, Ltd.
[Mh] Termos MeSH primário: Biomarcadores Tumorais/metabolismo
Carcinoma Endometrioide/metabolismo
Diferenciação Celular
Linhagem da Célula
Cistationina gama-Liase/metabolismo
Neoplasias do Endométrio/metabolismo
Células Epiteliais/metabolismo
Células-Tronco/metabolismo
[Mh] Termos MeSH secundário: Carcinoma Endometrioide/patologia
Carcinoma Endometrioide/secreção
Células Cultivadas
Cílios/metabolismo
Cílios/patologia
Neoplasias do Endométrio/patologia
Neoplasias do Endométrio/secreção
Células Epiteliais/patologia
Células Epiteliais/secreção
Feminino
Imunofluorescência
Seres Humanos
Imunofenotipagem/métodos
Células-Tronco Neoplásicas/metabolismo
Células-Tronco Neoplásicas/patologia
Células-Tronco Neoplásicas/secreção
Células-Tronco/patologia
Células-Tronco/secreção
Análise Serial de Tecidos
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); EC 4.4.1.1 (Cystathionine gamma-Lyase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170706
[St] Status:MEDLINE
[do] DOI:10.1002/path.4934


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[PMID]:28633902
[Au] Autor:Wang Y; Zhao Z; Shi S; Gao F; Wu J; Dong S; Zhang W; Liu Y; Zhong X
[Ad] Endereço:Department of Clinical Laboratory, The second Affiliated Hospital of Harbin Medical University, Harbin 150086, China.
[Ti] Título:Calcium sensing receptor initiating cystathionine-gamma-lyase/hydrogen sulfide pathway to inhibit platelet activation in hyperhomocysteinemia rat.
[So] Source:Exp Cell Res;358(2):171-181, 2017 Sep 15.
[Is] ISSN:1090-2422
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hyperhomocysteinemia (HHcy, high homocysteine) induces the injury of endothelial cells (ECs). Hydrogen sulfide (H S) protects ECs and inhibits the activation of platelets. Calcium-sensing receptor (CaSR) regulates the production of endogenous H S. However, whether CaSR inhibits the injury of ECs and the activation of platelets by regulating the endogenous cystathionine-gamma-lyase (CSE, a major enzyme that produces H S)/H S pathway in hyperhomocysteinemia has not been previously investigated. Here, we tested the ultrastructure alterations of ECs and platelets, the changes in the concentration of serum homocysteine and the parameters of blood of hyperhomocysteinemia rats were measured. The aggregation rate and expression of P-selectin of platelets were assessed. Additionally, the expression levels of CaSR and CSE in the aorta of rats were examined by western blotting. The mitochondrial membrane potential and the production of reactive oxygen species (ROS) were measured; the expression of phospho-calmodulin kinases II (p-CaMK II) and Von Willebrand Factor (vWF) of cultured ECs from rat thoracic aortas were measured. We found that the aggregation rate and the expression of P-selectin of platelets increased, and the expression of CaSR and CSE decreased in HHcy rats. In the ECs of HHcy group, the ROS production increased and the mitochondrial membrane potential decreased markedly, the expression of CSE and the p-CaMK II increased after treatment with CaSR agonist while decreased upon administration of U73122 (PLC-specific inhibitor) and 2-APB (IP Receptor inhibitor). CaSR agonist or NaHS significantly reversed the ECs injured and platelet aggregation caused by hyperhomocysteinemia. Our results demonstrate that CaSR regulates the endogenous CSE/H S pathway to inhibit the activation of platelets which concerts the protection of ECs in hyperhomocysteinemia.
[Mh] Termos MeSH primário: Cistationina gama-Liase/metabolismo
Sulfeto de Hidrogênio/metabolismo
Hiper-Homocisteinemia/metabolismo
Ativação Plaquetária
Receptores de Detecção de Cálcio/metabolismo
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Masculino
Ativação Plaquetária/efeitos dos fármacos
Ratos Wistar
Espécies Reativas de Oxigênio/metabolismo
Sulfetos/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Reactive Oxygen Species); 0 (Receptors, Calcium-Sensing); 0 (Sulfides); EC 4.4.1.1 (Cystathionine gamma-Lyase); FWU2KQ177W (sodium bisulfide); YY9FVM7NSN (Hydrogen Sulfide)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171018
[Lr] Data última revisão:
171018
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170622
[St] Status:MEDLINE


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[PMID]:28552745
[Au] Autor:Donovan J; Wong PS; Roberts RE; Garle MJ; Alexander SPH; Dunn WR; Ralevic V
[Ad] Endereço:School of Life Sciences, University of Nottingham, Nottingham, UK.
[Ti] Título:A critical role for cystathionine-ß-synthase in hydrogen sulfide-mediated hypoxic relaxation of the coronary artery.
[So] Source:Vascul Pharmacol;93-95:20-32, 2017 Aug.
[Is] ISSN:1879-3649
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hypoxia-induced coronary artery vasodilatation protects the heart by increasing blood flow under ischemic conditions, however its mechanism is not fully elucidated. Hydrogen sulfide (H S) is reported to be an oxygen sensor/transducer in the vasculature. The present study aimed to identify and characterise the role of H S in the hypoxic response of the coronary artery, and to define the H S synthetic enzymes involved. Immunoblotting and immunohistochemistry showed expression of all three H S-producing enzymes, cystathionine-ß-synthase (CBS), cystathionine-γ-lyase (CSE) and 3-mercaptopyruvate sulfurtransferase (MPST), in porcine coronary artery. Artery segments were mounted for isometric tension recording; hypoxia caused a transient endothelium-dependent contraction followed by prolonged endothelium-independent relaxation. The CBS inhibitor amino-oxyacetate (AOAA) reduced both phases of the hypoxic response. The CSE inhibitor dl-propargylglycine (PPG) and aspartate (limits MPST) had no effect alone, but when applied together with AOAA the hypoxic relaxation response was further reduced. Exogenous H S (Na S and NaHS) produced concentration-dependent contraction followed by prolonged relaxation. Responses to both hypoxia and exogenous H S were dependent on the endothelium, NO, cGMP, K channels and Cl /HCO exchange. H S production in coronary arteries was blocked by CBS inhibition (AOAA), but not by CSE inhibition (PPG). These data show that H S is an endogenous mediator of the hypoxic response in coronary arteries. Of the three H S-producing enzymes, CBS, expressed in the vascular smooth muscle, appears to be the most important for H S generated during hypoxic relaxation of the coronary artery. A contribution from other H S-producing enzymes only becomes apparent when CBS activity is inhibited.
[Mh] Termos MeSH primário: Vasos Coronários/efeitos dos fármacos
Cistationina beta-Sintase/metabolismo
Sulfeto de Hidrogênio/farmacologia
Sulfetos/farmacologia
Vasodilatação/efeitos dos fármacos
Vasodilatadores/farmacologia
[Mh] Termos MeSH secundário: Animais
Hipóxia Celular
Células Cultivadas
Antiportadores de Cloreto-Bicarbonato/efeitos dos fármacos
Antiportadores de Cloreto-Bicarbonato/metabolismo
Vasos Coronários/enzimologia
GMP Cíclico/metabolismo
Cistationina beta-Sintase/antagonistas & inibidores
Cistationina gama-Liase/antagonistas & inibidores
Cistationina gama-Liase/metabolismo
Relação Dose-Resposta a Droga
Endotélio Vascular/efeitos dos fármacos
Endotélio Vascular/metabolismo
Inibidores Enzimáticos/farmacologia
Feminino
Seres Humanos
Sulfeto de Hidrogênio/metabolismo
Técnicas In Vitro
Masculino
Músculo Liso Vascular/efeitos dos fármacos
Músculo Liso Vascular/enzimologia
Óxido Nítrico/metabolismo
Canais de Potássio/efeitos dos fármacos
Canais de Potássio/metabolismo
Transdução de Sinais
Sulfetos/metabolismo
Sulfurtransferases/metabolismo
Sus scrofa
Vasodilatadores/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chloride-Bicarbonate Antiporters); 0 (Enzyme Inhibitors); 0 (Potassium Channels); 0 (Sulfides); 0 (Vasodilator Agents); 31C4KY9ESH (Nitric Oxide); EC 2.8.1.- (Sulfurtransferases); EC 2.8.1.2 (3-mercaptopyruvate sulphurtransferase); EC 4.2.1.22 (Cystathionine beta-Synthase); EC 4.4.1.1 (Cystathionine gamma-Lyase); FWU2KQ177W (sodium bisulfide); H2D2X058MU (Cyclic GMP); YGR27ZW0Y7 (sodium sulfide); YY9FVM7NSN (Hydrogen Sulfide)
[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:170530
[St] Status:MEDLINE


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[PMID]:28550177
[Au] Autor:Leskova A; Pardue S; Glawe JD; Kevil CG; Shen X
[Ad] Endereço:Department of Pathology and Translational Pathobiology, Louisiana State University Health Sciences Center-Shreveport, Shreveport, Louisiana.
[Ti] Título:Role of thiosulfate in hydrogen sulfide-dependent redox signaling in endothelial cells.
[So] Source:Am J Physiol Heart Circ Physiol;313(2):H256-H264, 2017 Aug 01.
[Is] ISSN:1522-1539
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Recent reports have revealed that hydrogen sulfide (H S) exerts critical actions to promote cardiovascular homeostasis and health. Thiosulfate is one of the products formed during oxidative H S metabolism, and thiosulfate has been used extensively and safely to treat calcific uremic arteriopathy in dialysis patients. Yet despite its significance, fundamental questions regarding how thiosulfate and H S interact during redox signaling remain unanswered. In the present study, we examined the effect of exogenous thiosulfate on hypoxia-induced H S metabolite bioavailability in human umbilical vein endothelial cells (HUVECs). Under hypoxic conditions, we observed a decrease of GSH and GSSG levels in HUVECs at 0.5 and 4 h as well as decreased free H S and acid-labile sulfide and increased bound sulfide at all time points. Treatment with exogenous thiosulfate significantly decreased the ratio of GSH/GSSG to total sulfide of HUVECs under 0.5 h of hypoxia but significantly increased this ratio in HUVECs under 4 h of hypoxia. These responses reveal that thiosulfate has different effects at low and high doses and under different O tensions. In addition, treatment with thiosulfate also diminished VEGF-induced cystathionine-γ-lyase expression and reduced VEGF-induced HUVEC proliferation under both normoxic and hypoxic conditions. These results indicate that thiosulfate can modulate H S metabolites and signaling under various culture conditions that impact angiogenic activity. Thus, thiosulfate may serve as a unique sulfide donor to modulate endothelial responses under pathophysiological conditions involving angiogenesis. This report provides new evidence that different levels of exogenous thiosulfate dynamically change discrete sulfide biochemical metabolite bioavailability in endothelial cells under normoxia or hypoxia, acting in a slow manner to modulate sulfide metabolites. Moreover, our findings also reveal that thiosulfate surprisingly inhibits VEGF-dependent endothelial cell proliferation associated with a reduction in cystathionine-γ-lyase protein levels.
[Mh] Termos MeSH primário: Inibidores da Angiogênese/farmacologia
Células Endoteliais da Veia Umbilical Humana/efeitos dos fármacos
Sulfeto de Hidrogênio/farmacologia
Neovascularização Fisiológica/efeitos dos fármacos
Transdução de Sinais/efeitos dos fármacos
Tiossulfatos/farmacologia
[Mh] Termos MeSH secundário: Indutores da Angiogênese/farmacologia
Inibidores da Angiogênese/metabolismo
Disponibilidade Biológica
Hipóxia Celular
Proliferação Celular/efeitos dos fármacos
Células Cultivadas
Microambiente Celular
Cistationina gama-Liase/metabolismo
Relação Dose-Resposta a Droga
Glutationa/metabolismo
Dissulfeto de Glutationa/metabolismo
Células Endoteliais da Veia Umbilical Humana/metabolismo
Seres Humanos
Sulfeto de Hidrogênio/metabolismo
Oxirredução
Tiossulfatos/metabolismo
Fatores de Tempo
Fator A de Crescimento do Endotélio Vascular/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Angiogenesis Inducing Agents); 0 (Angiogenesis Inhibitors); 0 (Thiosulfates); 0 (Vascular Endothelial Growth Factor A); EC 4.4.1.1 (Cystathionine gamma-Lyase); GAN16C9B8O (Glutathione); ULW86O013H (Glutathione Disulfide); YY9FVM7NSN (Hydrogen Sulfide)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170907
[Lr] Data última revisão:
170907
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170528
[St] Status:MEDLINE
[do] DOI:10.1152/ajpheart.00723.2016


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[PMID]:28481637
[Au] Autor:Bazhanov N; Ansar M; Ivanciuc T; Garofalo RP; Casola A
[Ad] Endereço:Departments of 1 Pediatrics and.
[Ti] Título:Hydrogen Sulfide: A Novel Player in Airway Development, Pathophysiology of Respiratory Diseases, and Antiviral Defenses.
[So] Source:Am J Respir Cell Mol Biol;57(4):403-410, 2017 Oct.
[Is] ISSN:1535-4989
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hydrogen sulfide (H S) is a biologically relevant signaling molecule in mammals. Along with the volatile substances nitric oxide (NO) and carbon monoxide (CO), H S is defined as a gasotransmitter. It plays a physiological role in a variety of functions, including synaptic transmission, vascular tone, angiogenesis, inflammation, and cellular signaling. The generation of H S is catalyzed by cystathionine ß-synthase (CBS), cystathionine γ-lyase (CSE), and 3-mercaptopyruvate sulfurtransferase (3-MST). The expression of CBS and CSE is tissue specific, with CBS being expressed predominantly in the brain, and CSE in peripheral tissues, including lungs. CSE expression and activity are developmentally regulated, and recent studies suggest that CSE plays an important role in lung alveolarization during fetal development. In the respiratory tract, endogenous H S has been shown to participate in the regulation of important functions such as airway tone, pulmonary circulation, cell proliferation or apoptosis, fibrosis, oxidative stress, and inflammation. In the past few years, changes in the generation of H S have been linked to the pathogenesis of a variety of acute and chronic inflammatory lung diseases, including asthma and chronic obstructive pulmonary disease. Recently, our laboratory made the critical discovery that cellular H S exerts broad-spectrum antiviral activity both in vitro and in vivo, in addition to independent antiinflammatory activity. These findings have important implications for the development of novel therapeutic strategies for viral respiratory infections, as well as other inflammatory lung diseases, especially in light of recent significant efforts to generate controlled-release H S donors for clinical therapeutic applications.
[Mh] Termos MeSH primário: Sulfeto de Hidrogênio/metabolismo
Sistema Respiratório
Infecções Respiratórias
Transdução de Sinais
Viroses
[Mh] Termos MeSH secundário: Animais
Cistationina beta-Sintase/biossíntese
Cistationina gama-Liase/biossíntese
Regulação da Expressão Gênica no Desenvolvimento
Regulação Enzimológica da Expressão Gênica
Seres Humanos
Especificidade de Órgãos
Sistema Respiratório/embriologia
Sistema Respiratório/metabolismo
Sistema Respiratório/patologia
Sistema Respiratório/virologia
Infecções Respiratórias/embriologia
Infecções Respiratórias/metabolismo
Infecções Respiratórias/patologia
Infecções Respiratórias/virologia
Viroses/embriologia
Viroses/metabolismo
Viroses/patologia
Viroses/virologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
EC 4.2.1.22 (Cystathionine beta-Synthase); EC 4.4.1.1 (Cystathionine gamma-Lyase); YY9FVM7NSN (Hydrogen Sulfide)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170509
[St] Status:MEDLINE
[do] DOI:10.1165/rcmb.2017-0114TR


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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]:28336559
[Au] Autor:Candela J; Wang R; White C
[Ad] Endereço:From the Department of Physiology and Biophysics, Chicago Medical School, Rosalind Franklin University of Medicine and Science, North Chicago, IL (J.C., C.W.); and Cardiovascular and Metabolic Research Unit, Laurentian University, Sudbury, Canada (R.W.).
[Ti] Título:Microvascular Endothelial Dysfunction in Obesity Is Driven by Macrophage-Dependent Hydrogen Sulfide Depletion.
[So] Source:Arterioscler Thromb Vasc Biol;37(5):889-899, 2017 May.
[Is] ISSN:1524-4636
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: The function of perivascular adipose tissue as an anticontractile mediator in the microvasculature is lost during obesity. Obesity results in inflammation and recruitment of proinflammatory macrophages to the perivascular adipose tissue that is paralleled by depletion of the vasorelaxant signaling molecule hydrogen sulfide (H S) in the vessel. The current objective was to assess the role of macrophages in determining vascular [H S] and defining how this impinged on vasodilation. APPROACH AND RESULTS: Contractility and [H S] were measured in mesenteric resistance arterioles from lean and obese mice by using pressure myography and confocal microscopy, respectively. Vasodilation was impaired and smooth muscle and endothelial [H S] decreased in vessels from obese mice compared with those from lean controls. Coculturing vessels from lean mice with macrophages from obese mice, or macrophage-conditioned media, recapitulated obese phenotypes in vessels. These effects were mediated by low molecular weight species and dependent on macrophage inducible nitric oxide synthase activity. CONCLUSIONS: The inducible nitric oxide synthase activity of perivascular adipose tissue-resident proinflammatory macrophages promotes microvascular endothelial dysfunction by reducing the bioavailability of H S in the vessel. These findings support a model in which vascular H S depletion underpins the loss of perivascular adipose tissue anticontractile function in obesity.
[Mh] Termos MeSH primário: Tecido Adiposo/metabolismo
Arteríolas/metabolismo
Sulfeto de Hidrogênio/metabolismo
Macrófagos/metabolismo
Mesentério/irrigação sanguínea
Obesidade/metabolismo
Vasodilatação
[Mh] Termos MeSH secundário: Animais
Arteríolas/efeitos dos fármacos
Arteríolas/fisiopatologia
Comunicação Celular
Técnicas de Cocultura
Cistationina gama-Liase/deficiência
Cistationina gama-Liase/genética
Modelos Animais de Doenças
Relação Dose-Resposta a Droga
Células Endoteliais/metabolismo
Mediadores da Inflamação/metabolismo
Masculino
Camundongos Endogâmicos C57BL
Camundongos Knockout
Miócitos de Músculo Liso/metabolismo
Óxido Nítrico Sintase Tipo II/metabolismo
Obesidade/fisiopatologia
Técnicas de Cultura de Tecidos
Vasodilatação/efeitos dos fármacos
Vasodilatadores/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Inflammation Mediators); 0 (Vasodilator Agents); EC 1.14.13.39 (Nitric Oxide Synthase Type II); EC 1.14.13.39 (Nos2 protein, mouse); EC 4.4.1.1 (Cystathionine gamma-Lyase); YY9FVM7NSN (Hydrogen Sulfide)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170621
[Lr] Data última revisão:
170621
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170325
[St] Status:MEDLINE
[do] DOI:10.1161/ATVBAHA.117.309138


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[PMID]:28291844
[Au] Autor:Bronowicka-Adamska P; Bentke A; Wróbel M
[Ad] Endereço:Chair of Medical Biochemistry, Jagiellonian University, Collegium Medicum, Kraków, Poland.
[Ti] Título:Hydrogen sulfide generation from l-cysteine in the human glioblastoma-astrocytoma U-87 MG and neuroblastoma SHSY5Y cell lines.
[So] Source:Acta Biochim Pol;64(1):171-176, 2017.
[Is] ISSN:1734-154X
[Cp] País de publicação:Poland
[La] Idioma:eng
[Ab] Resumo:Hydrogen sulfide (H S) is endogenously synthesized from l-cysteine in reactions catalyzed by cystathionine beta-synthase (CBS, EC 4.2.1.22) and gamma-cystathionase (CSE, EC 4.4.1.1). The role of 3-mercaptopyruvate sulfurtransferase (MPST, EC 2.8.1.2) in H S generation is also considered; it could be important for tissues with low CTH activity, e.g. cells of the nervous system. The expression and activity of CBS, CTH, and MPST were detected in the human glioblastoma-astrocytoma (U-87 MG) and neuroblastoma (SHSY5Y) cell lines. In both cell lines, the expression and activity of MPST were the highest among the investigated enzymes, suggesting its possible role in the generation of H S. The RP-HPLC method was used to determine the concentration of cystathionine and alpha-ketobutyrate, products of the CBS- and CTH-catalyzed reactions. The difference in cystathionine levels between cell homogenates treated with totally CTH-inhibiting concentrations of dl-propargylglycine and without the inhibitor was used to evaluate the activity of CBS. The higher expression and activity of CBS, CTH and MPST in the neuroblastoma cells were associated with more intensive generation of H S in the presence of 2 mM cysteine. A threefold higher level of sulfane sulfur, a potential source of hydrogen sulfide, was detected in the astrocytoma cells in comparison to the neuroblastoma cells.
[Mh] Termos MeSH primário: Astrocitoma/enzimologia
Cisteína/metabolismo
Glioblastoma/enzimologia
Sulfeto de Hidrogênio/metabolismo
Neuroblastoma/enzimologia
[Mh] Termos MeSH secundário: Astrocitoma/patologia
Linhagem Celular Tumoral
Cistationina/metabolismo
Cistationina beta-Sintase/metabolismo
Cistationina gama-Liase/metabolismo
Glioblastoma/patologia
Seres Humanos
Neuroblastoma/patologia
Sulfurtransferases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
375YFJ481O (Cystathionine); EC 2.8.1.- (Sulfurtransferases); EC 2.8.1.2 (3-mercaptopyruvate sulphurtransferase); EC 4.2.1.22 (Cystathionine beta-Synthase); EC 4.4.1.1 (Cystathionine gamma-Lyase); K848JZ4886 (Cysteine); YY9FVM7NSN (Hydrogen Sulfide)
[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:170315
[St] Status:MEDLINE
[do] DOI:10.18388/abp.2016_1394



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