Abstract
VacA, a secretory product of Helicobacter pylori, binds to its cell surface receptor, receptor tyrosine phosphatase (RPTP) β, leading to cytoplasmic vacuolization of gastric epithelial AZ-521 cells. VacA binding to the cell surface and VacA-dependent vacuolization were inhibited by cell culture media containing fetal calf serum (FCS). The high molecular weight fraction of FCS isolated by Superose 12 gel filtration chromatography inhibited VacA binding, whereas only weak effects were observed with other fractions. These data show that the high molecular weight fraction of FCS inhibits VacA action though its ability to block toxin binding to its receptor, RPTPβ, on AZ-521 cells.
| Original language | English |
|---|---|
| Pages (from-to) | 105-107 |
| Number of pages | 3 |
| Journal | Microbiology and Immunology |
| Volume | 47 |
| Issue number | 1 |
| Publication status | Published - 2003 |
| Externally published | Yes |
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Keywords
- Helicobacter pylori
- RPTPβ
- Toxin receptor
- VacA
- Vacuolating cytotoxin
ASJC Scopus subject areas
- Immunology and Microbiology(all)
- Microbiology (medical)
- Microbiology
Cite this
High molecular weight factor in FCS inhibits Helicobacter pylori VacA-binding to its receptor, RPTPß, on AZ-521. / Kimura, Takahiro; Wada, Akihiro; Nakayama, Masaaki; Ogushi, Ken ichi; Nishi, Yoshito; De Guzman, Blanquita B.; Moss, Joel; Hirayama, Toshiya.
In: Microbiology and Immunology, Vol. 47, No. 1, 2003, p. 105-107.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - High molecular weight factor in FCS inhibits Helicobacter pylori VacA-binding to its receptor, RPTPß, on AZ-521
AU - Kimura, Takahiro
AU - Wada, Akihiro
AU - Nakayama, Masaaki
AU - Ogushi, Ken ichi
AU - Nishi, Yoshito
AU - De Guzman, Blanquita B.
AU - Moss, Joel
AU - Hirayama, Toshiya
PY - 2003
Y1 - 2003
N2 - VacA, a secretory product of Helicobacter pylori, binds to its cell surface receptor, receptor tyrosine phosphatase (RPTP) β, leading to cytoplasmic vacuolization of gastric epithelial AZ-521 cells. VacA binding to the cell surface and VacA-dependent vacuolization were inhibited by cell culture media containing fetal calf serum (FCS). The high molecular weight fraction of FCS isolated by Superose 12 gel filtration chromatography inhibited VacA binding, whereas only weak effects were observed with other fractions. These data show that the high molecular weight fraction of FCS inhibits VacA action though its ability to block toxin binding to its receptor, RPTPβ, on AZ-521 cells.
AB - VacA, a secretory product of Helicobacter pylori, binds to its cell surface receptor, receptor tyrosine phosphatase (RPTP) β, leading to cytoplasmic vacuolization of gastric epithelial AZ-521 cells. VacA binding to the cell surface and VacA-dependent vacuolization were inhibited by cell culture media containing fetal calf serum (FCS). The high molecular weight fraction of FCS isolated by Superose 12 gel filtration chromatography inhibited VacA binding, whereas only weak effects were observed with other fractions. These data show that the high molecular weight fraction of FCS inhibits VacA action though its ability to block toxin binding to its receptor, RPTPβ, on AZ-521 cells.
KW - Helicobacter pylori
KW - RPTPβ
KW - Toxin receptor
KW - VacA
KW - Vacuolating cytotoxin
UR - http://www.scopus.com/inward/record.url?scp=0037238984&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0037238984&partnerID=8YFLogxK
M3 - Article
C2 - 12636260
AN - SCOPUS:0037238984
VL - 47
SP - 105
EP - 107
JO - Microbiology and Immunology
JF - Microbiology and Immunology
SN - 0385-5600
IS - 1
ER -