Oxidative-stress-related proteome changes in Helicobacter pylori-infected human gastric mucosa

Hye Yeon Baek, Joo Weon Lim, Hyeyoung Kim, Jung Mogg Kim, Joo Sung Kim, Hyun Chae Jung, Kyung Hwan Kim

Research output: Contribution to journalArticle

47 Citations (Scopus)

Abstract

Helicobacter pylori infection leads to gastroduodenal inflammation, peptic ulceration and gastric carcinoma. Proteomic analysis of the human gastric mucosa from the patients with erosive gastritis, peptic ulcer or gastric cancer, which were either infected or not with H. pylori, was used to determine the differentially expressed proteins by H. pylori in the human gastric mucosa in order to investigate the pathogenic mechanism of H. pylori-induced gastric diseases. Prior to the experiment, the expression of the main 18 proteins were identified in the gastric mucosa and used for a proteome map of the human gastric mucosa. Using two-dimensional electrophoresis of the protein isolated from the H. pylori-infected tissues, Coomassie Brilliant Blue staining and computerized analysis of the stained gel, the expression of eight proteins were altered in the H. pylori-infected tissues compared with the non-infected tissues. MS analysis (matrix-assisted laser desorption/ionization-time of flight MS) of the tryptic fragment and a data search allowed the the identification of the four increased proteins (78 kDa glucose-regulated protein precursor, endoplasmin precursor, aldehyde dehydrogenase 2 and L-lactate dehydrogenase B chain) and the four decreased proteins (intracellular chloride channel protein 1, glutathione S-transferase, heat-shock protein 60 and cytokeratin 8) caused by H. pylori infection in the gastric mucosa. These proteins are related to cell proliferation, carcinogenesis, cytoskeletal function and cellular defence mechanism. The common feature is that these proteins are related to oxidative-stress-mediated cell damage. In conclusion, the established gastric mucosal proteome map might be useful for detecting the disease-related protein changes. The H. pylori-induced alterations in protein expression demonstrate the involvement of oxidative stress in the pathogenesis of H. pylori-induced gastric diseases, including inflammation, ulceration and carcinogenesis.

Original languageEnglish
Pages (from-to)291-299
Number of pages9
JournalBiochemical Journal
Volume379
Issue number2
DOIs
Publication statusPublished - 2004 Apr 15

Fingerprint

Oxidative stress
Proteome
Gastric Mucosa
Helicobacter pylori
Oxidative Stress
Proteins
Stomach Diseases
Helicobacter Infections
Tissue
Stomach
Carcinogenesis
Mucous Membrane
Keratin-8
Chaperonin 60
Inflammation
Aldehyde Dehydrogenase
Chloride Channels
Protein Precursors
Cell proliferation
Gastritis

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Baek, H. Y., Lim, J. W., Kim, H., Kim, J. M., Kim, J. S., Jung, H. C., & Kim, K. H. (2004). Oxidative-stress-related proteome changes in Helicobacter pylori-infected human gastric mucosa. Biochemical Journal, 379(2), 291-299. https://doi.org/10.1042/BJ20031208
Baek, Hye Yeon ; Lim, Joo Weon ; Kim, Hyeyoung ; Kim, Jung Mogg ; Kim, Joo Sung ; Jung, Hyun Chae ; Kim, Kyung Hwan. / Oxidative-stress-related proteome changes in Helicobacter pylori-infected human gastric mucosa. In: Biochemical Journal. 2004 ; Vol. 379, No. 2. pp. 291-299.
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Oxidative-stress-related proteome changes in Helicobacter pylori-infected human gastric mucosa. / Baek, Hye Yeon; Lim, Joo Weon; Kim, Hyeyoung; Kim, Jung Mogg; Kim, Joo Sung; Jung, Hyun Chae; Kim, Kyung Hwan.

In: Biochemical Journal, Vol. 379, No. 2, 15.04.2004, p. 291-299.

Research output: Contribution to journalArticle

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T1 - Oxidative-stress-related proteome changes in Helicobacter pylori-infected human gastric mucosa

AU - Baek, Hye Yeon

AU - Lim, Joo Weon

AU - Kim, Hyeyoung

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AU - Jung, Hyun Chae

AU - Kim, Kyung Hwan

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AB - Helicobacter pylori infection leads to gastroduodenal inflammation, peptic ulceration and gastric carcinoma. Proteomic analysis of the human gastric mucosa from the patients with erosive gastritis, peptic ulcer or gastric cancer, which were either infected or not with H. pylori, was used to determine the differentially expressed proteins by H. pylori in the human gastric mucosa in order to investigate the pathogenic mechanism of H. pylori-induced gastric diseases. Prior to the experiment, the expression of the main 18 proteins were identified in the gastric mucosa and used for a proteome map of the human gastric mucosa. Using two-dimensional electrophoresis of the protein isolated from the H. pylori-infected tissues, Coomassie Brilliant Blue staining and computerized analysis of the stained gel, the expression of eight proteins were altered in the H. pylori-infected tissues compared with the non-infected tissues. MS analysis (matrix-assisted laser desorption/ionization-time of flight MS) of the tryptic fragment and a data search allowed the the identification of the four increased proteins (78 kDa glucose-regulated protein precursor, endoplasmin precursor, aldehyde dehydrogenase 2 and L-lactate dehydrogenase B chain) and the four decreased proteins (intracellular chloride channel protein 1, glutathione S-transferase, heat-shock protein 60 and cytokeratin 8) caused by H. pylori infection in the gastric mucosa. These proteins are related to cell proliferation, carcinogenesis, cytoskeletal function and cellular defence mechanism. The common feature is that these proteins are related to oxidative-stress-mediated cell damage. In conclusion, the established gastric mucosal proteome map might be useful for detecting the disease-related protein changes. The H. pylori-induced alterations in protein expression demonstrate the involvement of oxidative stress in the pathogenesis of H. pylori-induced gastric diseases, including inflammation, ulceration and carcinogenesis.

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