Liver Proteome in Diabetes Type 1 Rat Model: Insulin-Dependent and -Independent Changes

Detalhes bibliográficos
Autor(a) principal: Braga, Camila Pereira [UNESP]
Data de Publicação: 2016
Outros Autores: Boone, Cory H. T., Grove, Ryan A., Adamcova, Dana, Henrique Fernandes, Ana Angelica [UNESP], Adamec, Jiri, Padilha, Pedro de Magalhaes [UNESP]
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1089/omi.2016.0135
http://hdl.handle.net/11449/162279
Resumo: Diabetes mellitus type 1 (DM1) is a major public health problem that continues to burden the healthcare systems worldwide, costing exponentially more as the epidemic grows. Innovative strategies and omics system diagnostics for earlier diagnosis or prognostication of DM1 are essential to prevent secondary complications and alleviate the associated economic burden. In a preclinical study design that involved streptozotocin (STZ)-induced DM1, insulin-treated STZ-induced DM1, and control rats, we characterized the insulin-dependent and -independent changes in protein profiles in liver samples. Digested proteins were subjected to LC-MSE for proteomic data. Progenesis QI data processing and analysis of variance were utilized for statistical analyses. We found 305 proteins with significantly altered abundance among the control, DM1, and insulin-treated DM1 groups (p<0.05). These differentially regulated proteins were related to enzymes that function in key metabolic pathways and stress responses. For example, gluconeogenesis appeared to return to control levels in the DM1 group after insulin treatment, with the restoration of gluconeogenesis regulatory enzyme, FBP1. Insulin administration to DM1 rats also restored the blood glucose levels and enzymes of general stress and antioxidant response systems. These observations are crucial for insights on DM1 pathophysiology and new molecular targets for future clinical biomarkers, drug discovery, and development. Additionally, we underscore that proteomics offers much potential in preclinical biomarker discovery for diabetes as well as common complex diseases such as cancer, dementia, and infectious disorders.
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spelling Liver Proteome in Diabetes Type 1 Rat Model: Insulin-Dependent and -Independent Changesbiomarkersbioinformaticsproteomicspersonalized medicineDiabetes mellitus type 1 (DM1) is a major public health problem that continues to burden the healthcare systems worldwide, costing exponentially more as the epidemic grows. Innovative strategies and omics system diagnostics for earlier diagnosis or prognostication of DM1 are essential to prevent secondary complications and alleviate the associated economic burden. In a preclinical study design that involved streptozotocin (STZ)-induced DM1, insulin-treated STZ-induced DM1, and control rats, we characterized the insulin-dependent and -independent changes in protein profiles in liver samples. Digested proteins were subjected to LC-MSE for proteomic data. Progenesis QI data processing and analysis of variance were utilized for statistical analyses. We found 305 proteins with significantly altered abundance among the control, DM1, and insulin-treated DM1 groups (p<0.05). These differentially regulated proteins were related to enzymes that function in key metabolic pathways and stress responses. For example, gluconeogenesis appeared to return to control levels in the DM1 group after insulin treatment, with the restoration of gluconeogenesis regulatory enzyme, FBP1. Insulin administration to DM1 rats also restored the blood glucose levels and enzymes of general stress and antioxidant response systems. These observations are crucial for insights on DM1 pathophysiology and new molecular targets for future clinical biomarkers, drug discovery, and development. Additionally, we underscore that proteomics offers much potential in preclinical biomarker discovery for diabetes as well as common complex diseases such as cancer, dementia, and infectious disorders.Sao Paulo State Univ, Inst Biosci, Dept Chem & Biochem, Botucatu, SP, BrazilUniv Nebraska, Dept Biochem, Redox Biol Ctr, Lincoln, NE 68583 USASao Paulo State Univ, Inst Biosci, Dept Chem & Biochem, Botucatu, SP, BrazilMary Ann Liebert, IncUniversidade Estadual Paulista (Unesp)Univ NebraskaBraga, Camila Pereira [UNESP]Boone, Cory H. T.Grove, Ryan A.Adamcova, DanaHenrique Fernandes, Ana Angelica [UNESP]Adamec, JiriPadilha, Pedro de Magalhaes [UNESP]2018-11-26T17:15:27Z2018-11-26T17:15:27Z2016-12-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article711-726http://dx.doi.org/10.1089/omi.2016.0135Omics-a Journal Of Integrative Biology. New Rochelle: Mary Ann Liebert, Inc, v. 20, n. 12, p. 711-726, 2016.1536-2310http://hdl.handle.net/11449/16227910.1089/omi.2016.0135WOS:000390592400004Web of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengOmics-a Journal Of Integrative Biology0,941info:eu-repo/semantics/openAccess2021-10-23T15:01:06Zoai:repositorio.unesp.br:11449/162279Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462021-10-23T15:01:06Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Liver Proteome in Diabetes Type 1 Rat Model: Insulin-Dependent and -Independent Changes
title Liver Proteome in Diabetes Type 1 Rat Model: Insulin-Dependent and -Independent Changes
spellingShingle Liver Proteome in Diabetes Type 1 Rat Model: Insulin-Dependent and -Independent Changes
Braga, Camila Pereira [UNESP]
biomarkers
bioinformatics
proteomics
personalized medicine
title_short Liver Proteome in Diabetes Type 1 Rat Model: Insulin-Dependent and -Independent Changes
title_full Liver Proteome in Diabetes Type 1 Rat Model: Insulin-Dependent and -Independent Changes
title_fullStr Liver Proteome in Diabetes Type 1 Rat Model: Insulin-Dependent and -Independent Changes
title_full_unstemmed Liver Proteome in Diabetes Type 1 Rat Model: Insulin-Dependent and -Independent Changes
title_sort Liver Proteome in Diabetes Type 1 Rat Model: Insulin-Dependent and -Independent Changes
author Braga, Camila Pereira [UNESP]
author_facet Braga, Camila Pereira [UNESP]
Boone, Cory H. T.
Grove, Ryan A.
Adamcova, Dana
Henrique Fernandes, Ana Angelica [UNESP]
Adamec, Jiri
Padilha, Pedro de Magalhaes [UNESP]
author_role author
author2 Boone, Cory H. T.
Grove, Ryan A.
Adamcova, Dana
Henrique Fernandes, Ana Angelica [UNESP]
Adamec, Jiri
Padilha, Pedro de Magalhaes [UNESP]
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (Unesp)
Univ Nebraska
dc.contributor.author.fl_str_mv Braga, Camila Pereira [UNESP]
Boone, Cory H. T.
Grove, Ryan A.
Adamcova, Dana
Henrique Fernandes, Ana Angelica [UNESP]
Adamec, Jiri
Padilha, Pedro de Magalhaes [UNESP]
dc.subject.por.fl_str_mv biomarkers
bioinformatics
proteomics
personalized medicine
topic biomarkers
bioinformatics
proteomics
personalized medicine
description Diabetes mellitus type 1 (DM1) is a major public health problem that continues to burden the healthcare systems worldwide, costing exponentially more as the epidemic grows. Innovative strategies and omics system diagnostics for earlier diagnosis or prognostication of DM1 are essential to prevent secondary complications and alleviate the associated economic burden. In a preclinical study design that involved streptozotocin (STZ)-induced DM1, insulin-treated STZ-induced DM1, and control rats, we characterized the insulin-dependent and -independent changes in protein profiles in liver samples. Digested proteins were subjected to LC-MSE for proteomic data. Progenesis QI data processing and analysis of variance were utilized for statistical analyses. We found 305 proteins with significantly altered abundance among the control, DM1, and insulin-treated DM1 groups (p<0.05). These differentially regulated proteins were related to enzymes that function in key metabolic pathways and stress responses. For example, gluconeogenesis appeared to return to control levels in the DM1 group after insulin treatment, with the restoration of gluconeogenesis regulatory enzyme, FBP1. Insulin administration to DM1 rats also restored the blood glucose levels and enzymes of general stress and antioxidant response systems. These observations are crucial for insights on DM1 pathophysiology and new molecular targets for future clinical biomarkers, drug discovery, and development. Additionally, we underscore that proteomics offers much potential in preclinical biomarker discovery for diabetes as well as common complex diseases such as cancer, dementia, and infectious disorders.
publishDate 2016
dc.date.none.fl_str_mv 2016-12-01
2018-11-26T17:15:27Z
2018-11-26T17:15:27Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1089/omi.2016.0135
Omics-a Journal Of Integrative Biology. New Rochelle: Mary Ann Liebert, Inc, v. 20, n. 12, p. 711-726, 2016.
1536-2310
http://hdl.handle.net/11449/162279
10.1089/omi.2016.0135
WOS:000390592400004
url http://dx.doi.org/10.1089/omi.2016.0135
http://hdl.handle.net/11449/162279
identifier_str_mv Omics-a Journal Of Integrative Biology. New Rochelle: Mary Ann Liebert, Inc, v. 20, n. 12, p. 711-726, 2016.
1536-2310
10.1089/omi.2016.0135
WOS:000390592400004
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Omics-a Journal Of Integrative Biology
0,941
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 711-726
dc.publisher.none.fl_str_mv Mary Ann Liebert, Inc
publisher.none.fl_str_mv Mary Ann Liebert, Inc
dc.source.none.fl_str_mv Web of Science
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
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