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J Biol Chem, Vol. 275, Issue 5, 3629-3636, February 4, 2000
From the Helicobacter pylori infection of the
gastric mucosa is accompanied by an activated histamine metabolism.
Histamine plays a central role in the regulation of gastric acid
secretion and is involved in the pathogenesis of gastroduodenal
ulcerations. Histidine decarboxylase (HDC) is the rate-limiting enzyme
for histamine production, and its activity is regulated through
transcriptional mechanisms. The present study investigated the effect
of H. pylori infection on the transcriptional activity of
the human HDC (hHDC) promoter in a gastric epithelial cell line (AGS)
and analyzed the underlying molecular mechanisms. Our studies
demonstrate that H. pylori infection potently
transactivated the hHDC promoter. The H. pylori-responsive
element of the hHDC gene was mapped to the sequence +1 to +27 base
pairs, which shows no homology to known cis-acting elements
and also functions as a gastrin-responsive element. H. pylori regulates the activity of this element via a Raf-1/MEK/ERK
pathway, which was activated in a Ras-independent manner. Furthermore,
we found that H. pylori-induced transactivation of the hHDC
promoter was independent of the cag pathogenicity island
and the vacuolating cytotoxin A gene and therefore may be exerted
through (a) new virulence factor(s). A better understanding of H. pylori-directed hHDC transcription can provide novel insights into the molecular mechanisms of H. pylori-dependent gene regulation in gastric
epithelial cells and may lead to new therapeutic approaches.
Helicobacter pylori Activates the Histidine
Decarboxylase Promoter through a Mitogen-activated Protein Kinase
Pathway Independent of Pathogenicity Island-encoded Virulence
Factors*
§,
,,, and
Max-Planck-Institut für
Infektionsbiologie, Abteilung Molekulare Biologie, Berlin, the
¶ Medizinische Klink mit Schwerpunkt Gastroenterologie und
Hepatologie, Universitätsklinikum Charité, Campus
Virchow-Klinikum, Humboldt Universität Berlin, the Max von
Pettenkofer Institut für Medizinische Mikrobiologie und Hygiene,
Abteilung Bakteriologie, 80336 München, Germany, and the
** Gastrointestinal Unit and Department of Medicine, Massachusetts
General Hospital and Harvard Medical School,
Boston, Massachusetts, 02114
*
This study was supported in part by Deutsche
Forschungsgemeinschaft Grants NA 292/6-1 (to M. N.) and HO 1288/6-1
(to M. H.), by Fonds der Chemischen Industrie grants (to M. N. and
T. F. M.), and by Verum Stiftung and Mildred Scheel Stiftung grants
(to B. W.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Max-Planck-Institut
für Infektionsbiologie, Abteilung Molekulare Biologie,
Monbijoustrasse 2, 10117 Berlin, Germany. Tel.: 49-30-28460-410; Fax:
49-30-28460-401; E-mail: naumann@mpiib-berlin.mpg.de.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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