Helicobacter pylori induces mono-(adenosine 5'-diphosphate)-ribosylation in human gastric adenocarcinoma

  • Authors:
    • Takashi Akai
    • Yoshihiro Nabeya
    • Kinnosuke Yahiro
    • Naoko Morinaga
    • Kanae Mitsuhashi
    • Masahito Inoue
    • Akio Sakamoto
    • Takenori Ochiai
    • Masatoshi Noda
  • View Affiliations

  • Published online on: October 1, 2006     https://doi.org/10.3892/ijo.29.4.965
  • Pages: 965-972
Metrics: Total Views: 0 (Spandidos Publications: | PMC Statistics: )
Total PDF Downloads: 0 (Spandidos Publications: | PMC Statistics: )


Abstract

Mono-(adenosine 5'-diphosphate) (ADP)-ribosylation, which transfers an ADP-ribose from nicotinamide adenine dinucleotide (NAD) to an acceptor protein, is an important post-translational modification of cellular proteins. Several bacterial toxins are known to possess the mono-ADP-ribosyltransferase activity to catalyze this reaction as a possible pathogenic factor. Therefore, the aim of this study was to examine whether H. pylori may also induce mono-ADP-ribosylation in a human gastric mucosal protein in association with gastric cancer development. Tumorous and adjacent non-tumorous mucosal tissue specimens were obtained from the surgically removed stomachs of 5 patients with gastric adenocarcinoma, and then were homogenized into cytosolic and membranous fractions. Each homogenate or an H. pylori extract was assayed for mono-ADP-ribosylation with [adenylate-32P]-NAD and 3-aminobenzamide, a potent inhibitor of poly-ADP-ribosylation. The radiolabeled proteins were separated by sodium dodecylsulfate-polyacrylamide gel electrophoresis followed by radio-image analysis. In the extracts from H. pylori, a strain-dependent, endogenous radiolabeling of 70-kDa protein was detected. An assay of the membranous fractions from 5 gastric adenocarcinomas with the extract of OMH4, a clinical H. pylori isolate, revealed notable radiolabelings of 55- and 45-kDa proteins, which were not found without the OMH4 extract. In contrast, the radiolabelings were minimal in the membranous fractions from respective non-tumorous mucosae, and they were not detected in any of the examined cytosolic fractions. All three radiolabelings of 70-, 55-, and 45-kDa proteins were dependent on NAD, but not on ADP-ribose. Snake venom phosphodiesterase digestion of the 3 radiolabeled proteins released only AMP. We thus found that H. pylori had an enzymatic mono-ADP-ribosyltransferase activity which enabled it to modify the 55- and 45-kDa membranous proteins of human gastric adenocarcinoma, as well as the 70-kDa protein of H. pylori itself. The possible roles underlying our observations on carcinogenesis or development of human gastric carcinoma are yet to be elucidated.

Related Articles

Journal Cover

October 2006
Volume 29 Issue 4

Print ISSN: 1019-6439
Online ISSN:1791-2423

Sign up for eToc alerts

Recommend to Library

Copy and paste a formatted citation
APA
Akai, T., Nabeya, Y., Yahiro, K., Morinaga, N., Mitsuhashi, K., Inoue, M. ... Noda, M. (2006). Helicobacter pylori induces mono-(adenosine 5'-diphosphate)-ribosylation in human gastric adenocarcinoma . International Journal of Oncology, 29, 965-972. https://doi.org/10.3892/ijo.29.4.965
MLA
Akai, T., Nabeya, Y., Yahiro, K., Morinaga, N., Mitsuhashi, K., Inoue, M., Sakamoto, A., Ochiai, T., Noda, M."Helicobacter pylori induces mono-(adenosine 5'-diphosphate)-ribosylation in human gastric adenocarcinoma ". International Journal of Oncology 29.4 (2006): 965-972.
Chicago
Akai, T., Nabeya, Y., Yahiro, K., Morinaga, N., Mitsuhashi, K., Inoue, M., Sakamoto, A., Ochiai, T., Noda, M."Helicobacter pylori induces mono-(adenosine 5'-diphosphate)-ribosylation in human gastric adenocarcinoma ". International Journal of Oncology 29, no. 4 (2006): 965-972. https://doi.org/10.3892/ijo.29.4.965