Epidermal Growth Factor Inhibits Helicobacter pylori Lipopolysaccharide-Induced Apoptosis of Primary Cultures of Gastric Pit Cells

2001 ◽  
pp. 43-46
Author(s):  
Tsukasa Kawahara ◽  
Shigetada Teshima ◽  
Kyoichi Kishi ◽  
Kazuhito Rokutan
Keyword(s):  
Helicobacter Pylori ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Primary Cultures ◽  
Pit Cells ◽  
Epidermal Growth ◽  
Induced Apoptosis

Apoptosis in human cultured trophoblasts is enhanced by hypoxia and diminished by epidermal growth factor

2000 ◽  
Vol 278 (5) ◽  
pp. C982-C988 ◽  
Author(s):  
Roni Levy ◽  
Steven D. Smith ◽  
Kala Chandler ◽  
Yoel Sadovsky ◽  
D. Michael Nelson
Keyword(s):  
Cell Differentiation ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Fetal Growth ◽  
Fetal Growth Restriction ◽  
Caspase Inhibitor ◽  
Trophoblast Differentiation ◽  
Epidermal Growth ◽  
Induced Apoptosis

Preeclampsia and fetal growth restriction are associated with placental hypoperfusion and villous hypoxia. The villous response to this environment includes diminished trophoblast differentiation and enhanced apoptosis. We tested the hypothesis that hypoxia induces apoptosis in cultured trophoblasts, and that epidermal growth factor (EGF), an enhancer of trophoblast differentiation, diminishes hypoxia-induced apoptosis. Trophoblasts isolated from placentas of term-uncomplicated human pregnancies were cultured up to 72 h in standard ([Formula: see text]= 120 mmHg) or hypoxic ([Formula: see text] < 15 mmHg) conditions. Exposure to hypoxia for 24 h markedly enhanced trophoblast apoptosis as determined by DNA laddering, internucleosomal in situ DNA fragmentation, and histomorphology, as well as by the reversibility of the apoptotic process with a caspase inhibitor. Apoptosis was accompanied by increased expression of p53 and Bax and decreased expression of Bcl-2. Addition of EGF to cultured trophoblasts or exposure of more differentiated trophoblasts to hypoxia significantly lowered the level of apoptosis. We conclude that hypoxia enhances apoptosis in cultured trophoblasts by a mechanism that involves an increase in p53 and Bax expression. EGF and enhancement of cell differentiation protect against hypoxic-induced apoptosis.

Eradication of Helicobacter Pylori Normalizes Elevated Mucosal Levels of Epidermal Growth Factor and Its Receptor

1999 ◽  
Vol 94 (10) ◽  
pp. 2885-2889 ◽  
Author(s):  
Walter J Coyle ◽  
Robert E Sedlack ◽  
Richard Nemec ◽  
Richard Peterson ◽  
Thomas Duntemann ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Epidermal Growth

Renal tubular cells are potential targets for epidermal growth factor

1988 ◽  
Vol 255 (6) ◽  
pp. F1191-F1196 ◽  
Author(s):  
P. R. Goodyer ◽  
Z. Kachra ◽  
C. Bell ◽  
R. Rozen
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Cell Line ◽  
Binding Sites ◽  
Collecting Duct ◽  
Primary Cultures ◽  
Kidney Cortex ◽  
Tubular Cells ◽  
Renal Tubular Cells ◽  
Epidermal Growth

Epidermal growth factor (EGF) is a potent polypeptide mitogen with various receptor-mediated growth effects on cells from the skin, breast, and gastrointestinal tract. Recent studies indicate that EGF is produced in the kidney and is excreted in the urine, but the biological significance of renal EGF is uncertain. We demonstrate in vitro mitogenicity of EGF for LLC-PK1 cells, a tubular epithelial cell line derived from pig kidney cortex. Furthermore, when subconfluent monolayers of LLC-PK1 cells are exposed to EGF for 24 h, sodium-dependent phosphate transport is stimulated (209-410% of control). These cells possess EGF-specific high-affinity binding sites at their surface (Kd 300-700 pM) but cannot synthesize the growth factor. EGF binding sites are not a peculiarity of the LLC-PK1 cell line, since similar sites are present on MDCK cells (derived from dog kidney distal tubule or collecting duct), primary cultures of mouse proximal tubular cells, and freshly prepared membrane fractions from mouse kidney. Cortical basolateral membranes are highly enriched in EGF binding sites, whereas EGF binding by brush-border membrane fractions is minimal and is compatible with contamination.

Serum and Gastric Luminal Epidermal Growth Factor in Helicobacter Pylori?Associated Gastritis and Peptic Ulcer Disease

Helicobacter ◽  
1996 ◽  
Vol 1 (4) ◽  
pp. 219-226 ◽  
Author(s):  
Damien A. F. Lynch ◽  
Nicholas P. Mapstone ◽  
Fraser Lewis ◽  
Judith Pentith ◽  
Anthony T. R. Axon ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Peptic Ulcer ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Peptic Ulcer Disease ◽  
Ulcer Disease ◽  
Epidermal Growth
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