1. Inhibition of gastric mucin synthesis by Helicobacter pylori
James C. Byrd, Christopher K. Yunker, Qin–Sheng Xu, Lawrence R. Sternberg, Robert S. Bresalier 
Gastroenterology 
Volume 118, Issue 6, Pages (June 2000)
DOI: /S (00)70360-X
Copyright © 2000 American Gastroenterological Association Terms and Conditions

2. Fig. 1
Effect of H. pylori on mucin synthesis in KATO III cells. Cells were labeled for 22 hours with [3H]glucosamine in the presence or absence of H. pylori, and the soluble intracellular fraction and dialyzed medium were analyzed by chromatography on Superose 6. Incorporation of [3H]glucosamine into the void volume (bar) was taken as a measure of mucin synthesis. (A) Soluble intracellular fraction from KATO III cells labeled in the presence (■) or absence (2) of 1 OD600 H. pylori. (B) Medium from cells labeled in the presence (■) or absence (2) of 1 OD600 H. pylori.
Gastroenterology  , DOI: ( /S (00)70360-X)
Copyright © 2000 American Gastroenterological Association Terms and Conditions

3. Fig. 2
Effect of H. pylori on mucin synthesis in 823 gastric cells. Labeled glycoproteins were analyzed as in Figure 1 (A) Soluble intracellular fraction from 823 cells labeled in the presence (■) or absence (2) of 1 OD600 H. pylori. (B) Medium from 823 cells labeled in the presence (■) or absence (2) of 1 OD600 H. pylori.
Gastroenterology  , DOI: ( /S (00)70360-X)
Copyright © 2000 American Gastroenterological Association Terms and Conditions

4. Fig. 3
Inhibition of mucin synthesis by subfractions of H. pylori. Intact H. pylori were lysed by sonication, and the lysates were centrifuged for 60 minutes at 100,000g. KATO III cells were metabolically labeled with [3H]glucosamine in the presence of intact H. pylori (■), H. pylori lysate (▨), the 100,000g pellet (2), or the 100,000g supernatant (●). Mucin in the soluble intracellular fraction was quantitated by size exclusion chromatography on Superose 6 columns and expressed as percent of control (mean ± SEM, n ≥ 3). *P < 0.05, §P < compared with controls.
Gastroenterology  , DOI: ( /S (00)70360-X)
Copyright © 2000 American Gastroenterological Association Terms and Conditions

5. Fig. 4
Time course and reversibility of inhibition of mucin synthesis. (A) KATO III cells, pretreated for 0, 24, or 48 hours with 1 OD600 H. pylori and labeled for 4 hours in the presence of 1 OD600 H. pylori. The x-axis represents total time of exposure to H. pylori. Control represents labeling in the absence of H. pylori. (B) KATO III cells were pretreated for 24 hours with 1 OD600 H. pylori, incubated 0-6 days without H. pylori, and labeled for 4 hours in the absence of H. pylori. Total mucin in the soluble intracellular fractions is expressed as percent of the control, untreated KATO III cells (mean ± SEM; n ≥ 3).
Gastroenterology  , DOI: ( /S (00)70360-X)
Copyright © 2000 American Gastroenterological Association Terms and Conditions

6. Fig. 5
Pulse-chase analysis of mucin in KATO III. Cells were metabolically labeled for 22 hours with [3H]glucosamine, then incubated in the presence or absence of H. pylori in medium without [3H]glucosamine for a further 24 hours. Labeled glycoproteins in medium and soluble intracellular fractions were analyzed by size-exclusion chromatography on Superose 6 columns. Solid bars show void volume containing mucin. (A) Soluble intracellular fraction from the pulse-labeled cells. (B) The soluble intracellular fraction (shaded area) and dialyzed medium (unshaded area) from cells after a 24-hour chase in the absence of H. pylori. (C) The soluble intracellular fraction (shaded area) and dialyzed medium (unshaded area) from cells after a 24-hour chase in the presence of H. pylori (0.3 OD600).
Gastroenterology  , DOI: ( /S (00)70360-X)
Copyright © 2000 American Gastroenterological Association Terms and Conditions

7. Fig. 6
(A) Effect of H. pylori on MUC1 and MUC5AC protein expression in KATO III and 823 gastric epithelial cells. Lysates from 823 and KATO III cells treated for 24 hours with (+) or without (−) 1 OD600 H. pylori were subjected to Western analysis (30 μg/lane). Arrow shows the top of the separating gel; bars show size markers. (Upper panel) MUC5AC-specific monoclonal antibody CLH2. (Lower panel) MUC1-specific monoclonal antibody HMFG2. (B) Effect of H. pylori on expression of control proteins CEA and galectin-3 in KATO III cells. Lysates from KATO III cells treated for 24 hours with (+) or without (−) 1 OD600 H. pylori were subjected to Western analysis (30 μg/lane). Bars show size markers. Rabbit anti-CEA (left), rat monoclonal anti–galectin-3 (right).
Gastroenterology  , DOI: ( /S (00)70360-X)
Copyright © 2000 American Gastroenterological Association Terms and Conditions

8. Fig. 6
(A) Effect of H. pylori on MUC1 and MUC5AC protein expression in KATO III and 823 gastric epithelial cells. Lysates from 823 and KATO III cells treated for 24 hours with (+) or without (−) 1 OD600 H. pylori were subjected to Western analysis (30 μg/lane). Arrow shows the top of the separating gel; bars show size markers. (Upper panel) MUC5AC-specific monoclonal antibody CLH2. (Lower panel) MUC1-specific monoclonal antibody HMFG2. (B) Effect of H. pylori on expression of control proteins CEA and galectin-3 in KATO III cells. Lysates from KATO III cells treated for 24 hours with (+) or without (−) 1 OD600 H. pylori were subjected to Western analysis (30 μg/lane). Bars show size markers. Rabbit anti-CEA (left), rat monoclonal anti–galectin-3 (right).
Gastroenterology  , DOI: ( /S (00)70360-X)
Copyright © 2000 American Gastroenterological Association Terms and Conditions

9. Fig. 7
Time course of inhibition of MUC1 and MUC5AC expression. KATO III cells were treated with 1 OD600 H. pylori for 4-48 hours, and lysates were analyzed for MUC5AC (○) and MUC1 (▵) expression by Western blot analysis. Results are expressed as percent of control KATO III with no H. pylori treatment (mean ± SEM; n = 3).
Gastroenterology  , DOI: ( /S (00)70360-X)
Copyright © 2000 American Gastroenterological Association Terms and Conditions