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
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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.

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October 2006
Volume 29 Issue 4

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

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Spandidos Publications style
Akai T, Nabeya Y, Yahiro K, Morinaga N, Mitsuhashi K, Inoue M, Sakamoto A, Ochiai T and Noda M: Helicobacter pylori induces mono-(adenosine 5'-diphosphate)-ribosylation in human gastric adenocarcinoma . Int J Oncol 29: 965-972, 2006.
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