Blockade of the trans-sulfuration pathway in acute pancreatitis due to nitration of cystathionine ß-synthase
Acute pancreatitis is an inflammatory process of the pancreatic gland that may lead to dysregulation of the trans-sulfuration pathway. The aims of this work were firstly to study the methionine cycle as well as the trans-sulfuration pathway using metabolomic and proteomic approaches identifying the...
| Authors: | , , , , , , , , , , , |
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| Format: | article |
| Status: | Published version |
| Publication Date: | 2020 |
| Country: | España |
| Institution: | INCLIVA |
| Repository: | r-INCLIVA. Repositorio Institucional de Producción Científica de INCLIVA |
| OAI Identifier: | oai:incliva.fundanetsuite.com:p4022 |
| Online Access: | https://incliva.portalinvestigacion.com/publicaciones/4022 |
| Access Level: | Open access |
| Keyword: | Acute inflammation S-adenosylmethionine Homocysteine Cystathionine beta-synthase Nitrosative stress |
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Blockade of the trans-sulfuration pathway in acute pancreatitis due to nitration of cystathionine ß-synthaseRius-Perez, SergioPerez, SalvadorTorres-Cuevas, IsabelMarti-Andres, PabloTalens-Visconti, RaquelParadela, AlbertoGuerrero, LauraFranco, LuisLopez-Rodas, GerardoTorres, LuisCorrales, FernandoSastre, JuanAcute inflammationS-adenosylmethionineHomocysteineCystathionine beta-synthaseNitrosative stressAcute pancreatitis is an inflammatory process of the pancreatic gland that may lead to dysregulation of the trans-sulfuration pathway. The aims of this work were firstly to study the methionine cycle as well as the trans-sulfuration pathway using metabolomic and proteomic approaches identifying the causes of this dysregulation in an experimental model of acute pancreatitis; and secondly to reveal the effects of S-adenosylmethionine administration on these pathways. Acute pancreatitis was induced by cerulein in mice, and a group of animals received S-adenosylmethionine treatment. Cerulein-induced acute pancreatitis rapidly caused marked depletion of methionine, S-adenosylmethionine, 5'-methylthioadenosine, cystathionine, cysteine, and glutathione levels in pancreas, but S-adenosylhomocysteine and homocysteine remained unchanged. Protein steady-state levels of S-adenosylhomocysteine-hydrolase and cystathionine gamma-lyase diminished but methylthioadenosine phosphorylase levels increased in pancreas with acute pancreatitis. Although cystathionine beta-synthase protein levels did not change with acute pancreatitis, Nos2 mRNA and protein levels were markedly up-regulated and caused tyrosine nitration of cystathionine beta-synthase in pancreas. S-adenosylmethionine administration enhanced Nos2 mRNA expression and cystathionine beta-synthase nitration and triggered homocysteine accumulation in acute pancreatitis. Furthermore, S-adenosylmethionine administration promoted enrichment of the euchromatin marker H3K4me3 in the promoters of Tnf-alpha, Il-6, and Nos2 and enhanced the mRNA up-regulation of these genes. Accordingly, S-adenosylmethionine administration increased inflammatory infiltrate and edema in pancreas with acute pancreatitis. In conclusion, tyrosine-nitration of cystathionine beta-synthase blockades the trans-sulfuration pathway in acute pancreatitis promoting homocysteine accumulation upon S-adenosylmethionine treatment. Copyright © 2019. Published by Elsevier B.V.ELSEVIER2020info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttps://incliva.portalinvestigacion.com/publicaciones/4022Redox BiologyISSN: 22132317reponame:r-INCLIVA. Repositorio Institucional de Producción Científica de INCLIVAinstname:INCLIVAInglésinfo:eu-repo/semantics/openAccessoai:incliva.fundanetsuite.com:p40222026-06-07T16:35:31Z |
| dc.title.none.fl_str_mv |
Blockade of the trans-sulfuration pathway in acute pancreatitis due to nitration of cystathionine ß-synthase |
| title |
Blockade of the trans-sulfuration pathway in acute pancreatitis due to nitration of cystathionine ß-synthase |
| spellingShingle |
Blockade of the trans-sulfuration pathway in acute pancreatitis due to nitration of cystathionine ß-synthase Rius-Perez, Sergio Acute inflammation S-adenosylmethionine Homocysteine Cystathionine beta-synthase Nitrosative stress |
| title_short |
Blockade of the trans-sulfuration pathway in acute pancreatitis due to nitration of cystathionine ß-synthase |
| title_full |
Blockade of the trans-sulfuration pathway in acute pancreatitis due to nitration of cystathionine ß-synthase |
| title_fullStr |
Blockade of the trans-sulfuration pathway in acute pancreatitis due to nitration of cystathionine ß-synthase |
| title_full_unstemmed |
Blockade of the trans-sulfuration pathway in acute pancreatitis due to nitration of cystathionine ß-synthase |
| title_sort |
Blockade of the trans-sulfuration pathway in acute pancreatitis due to nitration of cystathionine ß-synthase |
| dc.creator.none.fl_str_mv |
Rius-Perez, Sergio Perez, Salvador Torres-Cuevas, Isabel Marti-Andres, Pablo Talens-Visconti, Raquel Paradela, Alberto Guerrero, Laura Franco, Luis Lopez-Rodas, Gerardo Torres, Luis Corrales, Fernando Sastre, Juan |
| author |
Rius-Perez, Sergio |
| author_facet |
Rius-Perez, Sergio Perez, Salvador Torres-Cuevas, Isabel Marti-Andres, Pablo Talens-Visconti, Raquel Paradela, Alberto Guerrero, Laura Franco, Luis Lopez-Rodas, Gerardo Torres, Luis Corrales, Fernando Sastre, Juan |
| author_role |
author |
| author2 |
Perez, Salvador Torres-Cuevas, Isabel Marti-Andres, Pablo Talens-Visconti, Raquel Paradela, Alberto Guerrero, Laura Franco, Luis Lopez-Rodas, Gerardo Torres, Luis Corrales, Fernando Sastre, Juan |
| author2_role |
author author author author author author author author author author author |
| dc.subject.none.fl_str_mv |
Acute inflammation S-adenosylmethionine Homocysteine Cystathionine beta-synthase Nitrosative stress |
| topic |
Acute inflammation S-adenosylmethionine Homocysteine Cystathionine beta-synthase Nitrosative stress |
| description |
Acute pancreatitis is an inflammatory process of the pancreatic gland that may lead to dysregulation of the trans-sulfuration pathway. The aims of this work were firstly to study the methionine cycle as well as the trans-sulfuration pathway using metabolomic and proteomic approaches identifying the causes of this dysregulation in an experimental model of acute pancreatitis; and secondly to reveal the effects of S-adenosylmethionine administration on these pathways. Acute pancreatitis was induced by cerulein in mice, and a group of animals received S-adenosylmethionine treatment. Cerulein-induced acute pancreatitis rapidly caused marked depletion of methionine, S-adenosylmethionine, 5'-methylthioadenosine, cystathionine, cysteine, and glutathione levels in pancreas, but S-adenosylhomocysteine and homocysteine remained unchanged. Protein steady-state levels of S-adenosylhomocysteine-hydrolase and cystathionine gamma-lyase diminished but methylthioadenosine phosphorylase levels increased in pancreas with acute pancreatitis. Although cystathionine beta-synthase protein levels did not change with acute pancreatitis, Nos2 mRNA and protein levels were markedly up-regulated and caused tyrosine nitration of cystathionine beta-synthase in pancreas. S-adenosylmethionine administration enhanced Nos2 mRNA expression and cystathionine beta-synthase nitration and triggered homocysteine accumulation in acute pancreatitis. Furthermore, S-adenosylmethionine administration promoted enrichment of the euchromatin marker H3K4me3 in the promoters of Tnf-alpha, Il-6, and Nos2 and enhanced the mRNA up-regulation of these genes. Accordingly, S-adenosylmethionine administration increased inflammatory infiltrate and edema in pancreas with acute pancreatitis. In conclusion, tyrosine-nitration of cystathionine beta-synthase blockades the trans-sulfuration pathway in acute pancreatitis promoting homocysteine accumulation upon S-adenosylmethionine treatment. Copyright © 2019. Published by Elsevier B.V. |
| publishDate |
2020 |
| dc.date.none.fl_str_mv |
2020 |
| dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion |
| format |
article |
| status_str |
publishedVersion |
| dc.identifier.none.fl_str_mv |
https://incliva.portalinvestigacion.com/publicaciones/4022 |
| url |
https://incliva.portalinvestigacion.com/publicaciones/4022 |
| dc.language.none.fl_str_mv |
Inglés |
| language_invalid_str_mv |
Inglés |
| dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess |
| eu_rights_str_mv |
openAccess |
| dc.publisher.none.fl_str_mv |
ELSEVIER |
| publisher.none.fl_str_mv |
ELSEVIER |
| dc.source.none.fl_str_mv |
Redox Biology ISSN: 22132317 reponame:r-INCLIVA. Repositorio Institucional de Producción Científica de INCLIVA instname:INCLIVA |
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INCLIVA |
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r-INCLIVA. Repositorio Institucional de Producción Científica de INCLIVA |
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r-INCLIVA. Repositorio Institucional de Producción Científica de INCLIVA |
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|
| repository.mail.fl_str_mv |
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15,812429 |