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Differential Proteomics of Helicobacter pylori Associated with Autoimmune Atrophic Gastritis

Authors :
Valli De Re
Stefania Zanussi
Ombretta Repetto
Vincenzo Canzonieri
Mariateresa Casarotto
Paolo De Paoli
Renato Cannizzaro
Source :
Molecular Medicine. 20:57-71
Publication Year :
2013
Publisher :
Springer Science and Business Media LLC, 2013.

Abstract

Atrophic autoimmune gastritis (AAG) is a condition of chronic inflammation and atrophy of stomach mucosa, for which development can be partially triggered by the bacterial pathogen Helicobacter pylori (HP). HP can cause a variety of gastric diseases, such as duodenal ulcer (DU) or gastric cancer (GC). In this study, a comparative proteomic approach was used by two-dimensional fluorescence difference gel electrophoresis (DIGE) to identify differentially expressed proteins of HP strains isolated from patients with AAG, to identify markers of HP strain associated with AAG. Proteome profiles of HP isolated from GC or DU were used as a reference to compare proteomic levels. Proteomics analyses revealed 27 differentially expressed spots in AAG-associated HP in comparison with GC, whereas only 9 differential spots were found in AAG-associated HP profiles compared with DU. Proteins were identified after matrix-assisted laser desorption ionization (MALDI)-TOF and peptide mass fingerprinting. Some AAG-HP differential proteins were common between DU- and GC-HP (peroxiredoxin, heat shock protein 70 [HSP70], adenosine 5'-triphosphate [ATP] synthase subunit α, flagellin A). Our results presented here may suggest that comparative proteomes of HP isolated from AAG and DU share more common protein expression than GC and provide subsets of putative AAG-specific upregulated or downregulated proteins that could be proposed as putative markers of AAG-associated HP. Other comparative studies by two-dimensional maps integrated with functional genomics of candidate proteins will undoubtedly contribute to better decipher the biology of AAG-associated HP strains.

Details

ISSN :
15283658 and 10761551
Volume :
20
Database :
OpenAIRE
Journal :
Molecular Medicine
Accession number :
edsair.doi.dedup.....2752233f18db0b4b53f2c3cb3eac9e45
Full Text :
https://doi.org/10.2119/molmed.2013.00076