Proteomic Analysis in Esophageal Eosinophilia Reveals Differential Galectin-3 Expression and S-Nitrosylation

Carla M. Davis, Girish Hiremath, John E. Wiktorowicz, Kizhake V. Soman, Christof Straub, Christina Nance, Norma Quintanilla, Konrad Pazdrak, Kalpesh Thakkar, Anthony P. Olive, Alexander Kurosky

Research output: Contribution to journalArticle

Abstract

Background Aims: Esophageal eosinophilia (EE) can be caused by gastroesophageal reflux disease (GERD), proton-pump inhibitor-responsive EE (PPI-REE) or eosinophilic esophagitis (EoE). This study quantified protein expression and S-nitrosylation (SNO) post-translational modifications in EE to elucidate potential disease biomarkers. Methods: Proximal and distal esophageal (DE) biopsy proteins in patients with EE and in controls were assayed for protein content and fluorescence-labeled with and without ascorbate treatment. Protein SNO was determined, and selected protein spots were identified by matrix-assisted laser desorption ionization time-of-flight/mass spectrometry. Western blot and ingenuity pathway analysis were performed. Results: Ninety-one of 648 proteins showed differential expression. There were significantly altered levels of abundance for 11 proximal and 14 DE proteins. Hierarchal clustering revealed differential SNO in inflamed tissues, indicating reactive nitrogen/oxygen species involvement. Galectin-3 was upregulated in both proximal (p <0.04) and distal (p <0.004) esophageal EE biopsies compared to controls. In distal EE samples, galectin-3 was significantly S-nitrosylated (p <0.004). Principal component analysis revealed sample group discrimination distally. Conclusion: Proteomic analysis in EE esophageal mucosa revealed a distinct abundance and nitrosylation profile, most prominently in distal biopsies. Galectin-3 was upregulated in expression and SNO, which may indicate its potential role in mucosal inflammation. These results call for more studies to be performed to investigate the role of galectin-3 in GERD, PPI-REE and EoE.

Original languageEnglish (US)
Pages (from-to)288-299
Number of pages12
JournalDigestion
DOIs
StateAccepted/In press - May 20 2016

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Galectin 3
Eosinophilia
Proteomics
Eosinophilic Esophagitis
Proton Pump Inhibitors
Protein S
Gastroesophageal Reflux
Proteins
Biopsy
Reactive Nitrogen Species
Post Translational Protein Processing
Principal Component Analysis
Cluster Analysis
Reactive Oxygen Species
Mass Spectrometry
Lasers
Biomarkers
Fluorescence
Western Blotting
Inflammation

Keywords

  • Esophageal eosinophilia
  • Galectin
  • Proteomic analysis

ASJC Scopus subject areas

  • Gastroenterology

Cite this

Davis, C. M., Hiremath, G., Wiktorowicz, J. E., Soman, K. V., Straub, C., Nance, C., ... Kurosky, A. (Accepted/In press). Proteomic Analysis in Esophageal Eosinophilia Reveals Differential Galectin-3 Expression and S-Nitrosylation. Digestion, 288-299. https://doi.org/10.1159/000444675

Proteomic Analysis in Esophageal Eosinophilia Reveals Differential Galectin-3 Expression and S-Nitrosylation. / Davis, Carla M.; Hiremath, Girish; Wiktorowicz, John E.; Soman, Kizhake V.; Straub, Christof; Nance, Christina; Quintanilla, Norma; Pazdrak, Konrad; Thakkar, Kalpesh; Olive, Anthony P.; Kurosky, Alexander.

In: Digestion, 20.05.2016, p. 288-299.

Research output: Contribution to journalArticle

Davis, CM, Hiremath, G, Wiktorowicz, JE, Soman, KV, Straub, C, Nance, C, Quintanilla, N, Pazdrak, K, Thakkar, K, Olive, AP & Kurosky, A 2016, 'Proteomic Analysis in Esophageal Eosinophilia Reveals Differential Galectin-3 Expression and S-Nitrosylation', Digestion, pp. 288-299. https://doi.org/10.1159/000444675
Davis, Carla M. ; Hiremath, Girish ; Wiktorowicz, John E. ; Soman, Kizhake V. ; Straub, Christof ; Nance, Christina ; Quintanilla, Norma ; Pazdrak, Konrad ; Thakkar, Kalpesh ; Olive, Anthony P. ; Kurosky, Alexander. / Proteomic Analysis in Esophageal Eosinophilia Reveals Differential Galectin-3 Expression and S-Nitrosylation. In: Digestion. 2016 ; pp. 288-299.
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T1 - Proteomic Analysis in Esophageal Eosinophilia Reveals Differential Galectin-3 Expression and S-Nitrosylation

AU - Davis, Carla M.

AU - Hiremath, Girish

AU - Wiktorowicz, John E.

AU - Soman, Kizhake V.

AU - Straub, Christof

AU - Nance, Christina

AU - Quintanilla, Norma

AU - Pazdrak, Konrad

AU - Thakkar, Kalpesh

AU - Olive, Anthony P.

AU - Kurosky, Alexander

PY - 2016/5/20

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N2 - Background Aims: Esophageal eosinophilia (EE) can be caused by gastroesophageal reflux disease (GERD), proton-pump inhibitor-responsive EE (PPI-REE) or eosinophilic esophagitis (EoE). This study quantified protein expression and S-nitrosylation (SNO) post-translational modifications in EE to elucidate potential disease biomarkers. Methods: Proximal and distal esophageal (DE) biopsy proteins in patients with EE and in controls were assayed for protein content and fluorescence-labeled with and without ascorbate treatment. Protein SNO was determined, and selected protein spots were identified by matrix-assisted laser desorption ionization time-of-flight/mass spectrometry. Western blot and ingenuity pathway analysis were performed. Results: Ninety-one of 648 proteins showed differential expression. There were significantly altered levels of abundance for 11 proximal and 14 DE proteins. Hierarchal clustering revealed differential SNO in inflamed tissues, indicating reactive nitrogen/oxygen species involvement. Galectin-3 was upregulated in both proximal (p <0.04) and distal (p <0.004) esophageal EE biopsies compared to controls. In distal EE samples, galectin-3 was significantly S-nitrosylated (p <0.004). Principal component analysis revealed sample group discrimination distally. Conclusion: Proteomic analysis in EE esophageal mucosa revealed a distinct abundance and nitrosylation profile, most prominently in distal biopsies. Galectin-3 was upregulated in expression and SNO, which may indicate its potential role in mucosal inflammation. These results call for more studies to be performed to investigate the role of galectin-3 in GERD, PPI-REE and EoE.

AB - Background Aims: Esophageal eosinophilia (EE) can be caused by gastroesophageal reflux disease (GERD), proton-pump inhibitor-responsive EE (PPI-REE) or eosinophilic esophagitis (EoE). This study quantified protein expression and S-nitrosylation (SNO) post-translational modifications in EE to elucidate potential disease biomarkers. Methods: Proximal and distal esophageal (DE) biopsy proteins in patients with EE and in controls were assayed for protein content and fluorescence-labeled with and without ascorbate treatment. Protein SNO was determined, and selected protein spots were identified by matrix-assisted laser desorption ionization time-of-flight/mass spectrometry. Western blot and ingenuity pathway analysis were performed. Results: Ninety-one of 648 proteins showed differential expression. There were significantly altered levels of abundance for 11 proximal and 14 DE proteins. Hierarchal clustering revealed differential SNO in inflamed tissues, indicating reactive nitrogen/oxygen species involvement. Galectin-3 was upregulated in both proximal (p <0.04) and distal (p <0.004) esophageal EE biopsies compared to controls. In distal EE samples, galectin-3 was significantly S-nitrosylated (p <0.004). Principal component analysis revealed sample group discrimination distally. Conclusion: Proteomic analysis in EE esophageal mucosa revealed a distinct abundance and nitrosylation profile, most prominently in distal biopsies. Galectin-3 was upregulated in expression and SNO, which may indicate its potential role in mucosal inflammation. These results call for more studies to be performed to investigate the role of galectin-3 in GERD, PPI-REE and EoE.

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KW - Galectin

KW - Proteomic analysis

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