High molecular weight factor in FCS inhibits Helicobacter pylori VacA-binding to its receptor, RPTPß, on AZ-521

Takahiro Kimura; Akihiro Wada; Masaaki Nakayama; Ken ichi Ogushi; Yoshito Nishi; Blanquita B. De Guzman; Joel Moss; Toshiya Hirayama

doi:10.1111/j.1348-0421.2003.tb02792.x

High molecular weight factor in FCS inhibits Helicobacter pylori VacA-binding to its receptor, RPTPß, on AZ-521

Takahiro Kimura, Akihiro Wada, Masaaki Nakayama, Ken ichi Ogushi, Yoshito Nishi, Blanquita B. De Guzman, Joel Moss, Toshiya Hirayama

Research output: Contribution to journal › Article › peer-review

5 Citations (Scopus)

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
DOIs	https://doi.org/10.1111/j.1348-0421.2003.tb02792.x
Publication status	Published - 2003
Externally published	Yes

Keywords

Helicobacter pylori
RPTPβ
Toxin receptor
VacA
Vacuolating cytotoxin

ASJC Scopus subject areas

Microbiology
Immunology
Virology

Access to Document

10.1111/j.1348-0421.2003.tb02792.x

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 › peer-review

@article{d8793c8fccba4684981677016196c866,

title = "High molecular weight factor in FCS inhibits Helicobacter pylori VacA-binding to its receptor, RPTP{\ss}, on AZ-521",

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.",

keywords = "Helicobacter pylori, RPTPβ, Toxin receptor, VacA, Vacuolating cytotoxin",

author = "Takahiro Kimura and Akihiro Wada and Masaaki Nakayama and Ogushi, {Ken ichi} and Yoshito Nishi and {De Guzman}, {Blanquita B.} and Joel Moss and Toshiya Hirayama",

year = "2003",

doi = "10.1111/j.1348-0421.2003.tb02792.x",

language = "English",

volume = "47",

pages = "105--107",

journal = "Microbiology and Immunology",

issn = "0385-5600",

publisher = "Center for Academic Publications Japan",

number = "1",

}

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

U2 - 10.1111/j.1348-0421.2003.tb02792.x

DO - 10.1111/j.1348-0421.2003.tb02792.x

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 -

High molecular weight factor in FCS inhibits Helicobacter pylori VacA-binding to its receptor, RPTPß, on AZ-521

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this