Morphologic Differentiation of HL-60 Cells Is Associated with Appearance of RPTPβ and Induction of Helicobacter pyloriVacA Sensitivity

Padilla, Philip Ian; Wada, Akihiro; Yahiro, Kinnosuke; Kimura, Miyuki; Niidome, Takuro; Aoyagi, Haruhiko; Kumatori, Atsushi; Anami, Masanobu; Hayashi, Tomoyoshi; Fujisawa, Jun; Saito, Haruo; Moss, Joel; Hirayama, Toshiya

doi:10.1074/jbc.275.20.15200

Cited by 75 publications

(69 citation statements)

References 38 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Several cell-surface receptors for VacA have been reported, including two receptor protein tyrosine phosphatases (RPTP-␣ and -␤) (16,(32)(33)(34), the epidermal growth factor receptor (35), and heparan sulfate (36). VacA also localizes to lipid raft domains on the surface of mammalian cells (12,37,38).…”

mentioning

confidence: 99%

Functional Properties of the p33 and p55 Domains of the Helicobacter pylori Vacuolating Cytotoxin

Torres¹,

Ivie²,

McClain

et al. 2005

Journal of Biological Chemistry

View full text Add to dashboard Cite

Helicobacter pylori secretes an 88-kDa vacuolating cytotoxin (VacA) that may contribute to the pathogenesis of peptic ulcer disease and gastric cancer. VacA cytotoxic activity requires assembly of VacA monomers into oligomeric structures, formation of anion-selective membrane channels, and entry of VacA into host cells. In this study, we analyzed the functional properties of recombinant VacA fragments corresponding to two putative VacA domains (designated p33 and p55). Immunoprecipitation experiments indicated that these two domains can interact with each other to form protein complexes. In comparison to the individual VacA domains, a mixture of the p33 and p55 proteins exhibited markedly enhanced binding to the plasma membrane of mammalian cells. Furthermore, internalization of the VacA domains was detected when cells were incubated with the p33/p55 mixture but not when the p33 and p55 proteins were tested individually. Incubation of cells with the p33/p55 mixture resulted in cell vacuolation, whereas the individual domains lacked detectable cytotoxic activity. Interestingly, sequential addition of p55 followed by p33 resulted in VacA internalization and cell vacuolation, whereas sequential addition in the reverse order was ineffective. These results indicate that both the p33 and p55 domains contribute to the binding and internalization of VacA and that both domains are required for vacuolating cytotoxic activity. Reconstitution of toxin activity from two separate domains, as described here for VacA, has rarely been described for pore-forming bacterial toxins, which suggests that VacA is a pore-forming toxin with unique structural properties.

show abstract

mentioning

confidence: 99%

Functional Properties of the p33 and p55 Domains of the Helicobacter pylori Vacuolating Cytotoxin

Torres¹,

Ivie²,

McClain

et al. 2005

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…Recently, we established that RPTP␤ functions as a receptor for VacA (24,29,31,32) and that RPTP␤, expressed in gastric tissue, is responsible for gastric injury caused by VacA (9). Notably, as there was no difference in vacuole development between wild-type mice and RPTP␤-deficient mice, we concluded that RPTP␤ is not essential either for the internalization of VacA or for vacuolation in gastric epithelial cells.…”

Section: Discussionmentioning

confidence: 86%

“…Transfection was performed as described previously (24,29,31,32) with the following modifications. In brief, cells were seeded in 24-well culture plates (0.5 or 1.0 ϫ 10 5 cells in 1 ml of DMEM per well), incubated at 37°C for 24 h, and rinsed with phosphate-buffered saline (PBS).…”

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Essential Domain of Receptor Tyrosine Phosphatase β (RPTPβ) for Interaction with Helicobacter pylori Vacuolating Cytotoxin

Yahiro

Wada

Yamasaki

et al. 2004

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

“…[12][13][14][15] However, little is known about the treatment effect of PMA on the release of leukemia cells from the BM after undergoing such differentiation therapy. 16 Therefore, the adhesion and migration of leukemia cells treated with and without PMA to a mimic ECM environment were investigated in this study.…”

mentioning

confidence: 99%

Nanomechanical measurement of adhesion and migration of leukemia cells with phorbol 12-myristate 13-acetate treatment

Zhou¹,

Tong³

et al. 2016

IJN

View full text Add to dashboard Cite

Morphologic Differentiation of HL-60 Cells Is Associated with Appearance of RPTPβ and Induction of Helicobacter pyloriVacA Sensitivity

Cited by 75 publications

References 38 publications

Functional Properties of the p33 and p55 Domains of the Helicobacter pylori Vacuolating Cytotoxin

Functional Properties of the p33 and p55 Domains of the Helicobacter pylori Vacuolating Cytotoxin

Essential Domain of Receptor Tyrosine Phosphatase β (RPTPβ) for Interaction with Helicobacter pylori Vacuolating Cytotoxin

Nanomechanical measurement of adhesion and migration of leukemia cells with phorbol 12-myristate 13-acetate treatment

Contact Info

Product

Resources

About