Ectodomain shedding of E-cadherin and c-Met is induced by Helicobacter pylori infection.
Helicobacter pylori, a microaerophilic gram-negative bacterium, colonizes the human stomach. About 50% of the world's population is infected, and this infection is considered as the major risk factor for the development of gastric adenocarcinomas in 1% of infected subjects. Carcinogenesis is characterized by the process of epithelial-to-mesenchymal transition (EMT), in the course of which fully differentiated epithelial cells turn into depolarized and migratory cells. Concomitant disruption of adherence junctions (AJ) is facilitated by growth factors like hepatocyte growth factor 1 (HGF-1), but has been also shown to depend on ectodomain shedding of E-cadherin. The aim of this study was to investigate the impact of infection with H. pylori of NCI-N87 gastric epithelial cells on the shedding of E-cadherin and HGF-receptor c-Met. Our results show that infection with H. pylori provokes shedding of the surface proteins c-Met and E-cadherin. Evidence is provided that ADAM10 contributes to the shedding of c-Met and E-cadherin.
Schirrmeister
Wiebke
W
Clinic of Gastroenterology, Hepatology and Infectious Diseases, Otto-von-Guericke-University Magdeburg, Leipziger Str. 44, D-39120 Magdeburg, Germany.
Gnad
Thorsten
T
Wex
Thomas
T
Higashiyama
Shigeki
S
Wolke
Carmen
C
Naumann
Michael
M
Lendeckel
Uwe
U
D051722:ADAM Proteins / Q000235:genetics / Q000378:metabolism; D000072197:ADAM10 Protein; D053829:Amyloid Precursor Protein Secretases / Q000235:genetics / Q000378:metabolism; D015820:Cadherins / Q000378:metabolism*; D002460:Cell Line; D018450:Disease Progression; D004847:Epithelial Cells / Q000378:metabolism* / Q000382:microbiology*; D015870:Gene Expression / Q000235:genetics; D005998:Glycine / Q000031:analogs & derivatives / Q000494:pharmacology; D016481:Helicobacter Infections / Q000378:metabolism* / Q000382:microbiology; D016480:Helicobacter pylori / Q000502:physiology*; D006801:Humans; D006877:Hydroxamic Acids / Q000494:pharmacology; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism; D008666:Metalloendopeptidases / Q000037:antagonists & inhibitors / Q000378:metabolism; D010446:Peptide Fragments / Q000378:metabolism*; D011480:Protease Inhibitors / Q000494:pharmacology; D019859:Proto-Oncogene Proteins c-met / Q000378:metabolism*; D034741:RNA, Small Interfering / Q000235:genetics; D013270:Stomach / Q000166:cytology; D013274:Stomach Neoplasms / Q000378:metabolism / Q000382:microbiology / Q000473:pathology; D014162:Transfection
D015820:Cadherins; D006877:Hydroxamic Acids; C107086:KB R7785; D008565:Membrane Proteins; D010446:Peptide Fragments; D011480:Protease Inhibitors; D034741:RNA, Small Interfering; C099410:TAPI-2; D019859:Proto-Oncogene Proteins c-met; D053829:Amyloid Precursor Protein Secretases; D051722:ADAM Proteins; C411902:ADAM19 protein, human; D008666:Metalloendopeptidases; D000072197:ADAM10 Protein; C491236:ADAM10 protein, human; D005998:Glycine