JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Padilla, P. I.
Right arrow Articles by Hirayama, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Padilla, P. I.
Right arrow Articles by Hirayama, T.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J Biol Chem, Vol. 275, Issue 20, 15200-15206, May 19, 2000

Morphologic Differentiation of HL-60 Cells Is Associated with Appearance of RPTPbeta and Induction of Helicobacter pylori VacA Sensitivity*

Philip Ian PadillaDagger , Akihiro WadaDagger , Kinnosuke YahiroDagger §, Miyuki KimuraDagger §, Takuro Niidome§, Haruhiko Aoyagi§, Atsushi Kumatori, Masanobu Anami||, Tomoyoshi Hayashi||, Jun-ichi Fujisawa**, Haruo SaitoDagger Dagger , Joel Moss§§, and Toshiya HirayamaDagger ¶¶

From the Dagger  Department of Bacteriology, Institute of Tropical Medicine, Nagasaki University, § Department of Applied Chemistry, Faculty of Engineering, Nagasaki University,  Department of Biochemistry, Institute of Tropical Medicine, Nagasaki University, Nagasaki 8528523, Japan, the || Department of Pathology, Nagasaki University Hospital, Nagasaki 8528501, Japan, the ** Department of Microbiology, Kansai Medical University, Moriguchi 5708506, Japan, the Dagger Dagger  Department of Tumor Immunology, Dana-Farber Cancer Institute, Boston, Massachusetts 02115, and the §§ Pulmonary-Critical Care Medicine Branch, NHKBI, National Institutes of Health, Bethesda, Maryland 20892

Phorbol 12-myristate 13-acetate (PMA) induces differentiation of human leukemic HL-60 cells into cells with macrophage-like characteristics and enhances the susceptibility of HL-60 cells to the Helicobacter pylori VacA toxin (de Bernard, M., Moschioni., M., Papini, E., Telford, J. L., Rappuoli, R., and Montecucco, C. (1998) FEBS Lett. 436, 218-222). We examined the mechanism by which HL-60 cells acquire sensitivity to VacA, in particular, looking for expression of RPTPbeta , a VacA-binding protein postulated to be the VacA receptor (Yahiro, K., Niidome, T., Kimura, M., Hatakeyama, T., Aoyagi, H., Kurazono, H., Imagawa, K., Wada, A., Moss, J., and Hirayama, T. (1999) J. Biol. Chem. 274, 36693-36699). PMA induced expression of RPTPbeta mRNA and protein as determined by RNase protection assay and indirect immunofluorescence studies, respectively. Vitamin D3 and interferon-gamma , which stimulate differentiation of HL-60 cells into monocyte-like cells, also induced VacA sensitivity and expression of RPTPbeta mRNA, whereas 1.2% Me2SO and retinoic acid, which stimulated the maturation of HL-60 into granulocyte-like cells, did not. RPTPbeta antisense oligonucleotide inhibited induction of VacA sensitivity and expression of RPTPbeta . Double immunostaining studies also indicated that newly expressed RPTPbeta colocalized with VacA in PMA-treated HL-60 cells. In agreement with these data, BHK-21 cells, which are insensitive to VacA, when transfected with the RPTPbeta cDNA, acquired VacA sensitivity. All data are consistent with the conclusion that acquisition of VacA sensitivity by PMA-treated HL-60 cells results from induction of RPTPbeta , a protein that functions as the VacA receptor.

* This work was supported by grants-in-aid for Scientific Research and for International Scientific Research (Joint Research) from the Ministry of Education, Science, and Culture of Japan, and funds from the Ohyama Health Foundation.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¶¶ To whom correspondence should be addressed: Dept. of Bacteriology, Inst. of Tropical Medicine, Nagasaki University, Nagasaki 852, Japan. Tel.: 81-95-849-7831; Fax: 81-95-849-7805; E-mail:hirayama@net.nagasaki-u.ac.jp.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Infect. Immun.Home page
M. Nakayama, J. Hisatsune, E. Yamasaki, Y. Nishi, A. Wada, H. Kurazono, J. Sap, K. Yahiro, J. Moss, and T. Hirayama
Clustering of Helicobacter pylori VacA in Lipid Rafts, Mediated by Its Receptor, Receptor-Like Protein Tyrosine Phosphatase {beta}, Is Required for Intoxication in AZ-521 Cells
Infect. Immun., December 1, 2006; 74(12): 6571 - 6580.
[Abstract] [Full Text] [PDF]

Home page
 Infect. Immun.Home page
D. A. G. Skibinski, C. Genisset, S. Barone, and J. L. Telford
The Cell-Specific Phenotype of the Polymorphic vacA Midregion Is Independent of the Appearance of the Cell Surface Receptor Protein Tyrosine Phosphatase {beta}
Infect. Immun., January 1, 2006; 74(1): 49 - 55.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
V. J. Torres, S. E. Ivie, M. S. McClain, and T. L. Cover
Functional Properties of the p33 and p55 Domains of the Helicobacter pylori Vacuolating Cytotoxin
J. Biol. Chem., June 3, 2005; 280(22): 21107 - 21114.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. Yahiro, A. Wada, E. Yamasaki, M. Nakayama, Y. Nishi, J. Hisatsune, N. Morinaga, J. Sap, M. Noda, J. Moss, et al.
Essential Domain of Receptor Tyrosine Phosphatase {beta} (RPTP{beta}) for Interaction with Helicobacter pylori Vacuolating Cytotoxin
J. Biol. Chem., December 3, 2004; 279(49): 51013 - 51021.
[Abstract] [Full Text] [PDF]

Home page
 Microbiol. Mol. Biol. Rev.Home page
I. R. Henderson, F. Navarro-Garcia, M. Desvaux, R. C. Fernandez, and D. Ala'Aldeen
Type V Protein Secretion Pathway: the Autotransporter Story
Microbiol. Mol. Biol. Rev., December 1, 2004; 68(4): 692 - 744.
[Abstract] [Full Text] [PDF]

Home page
 J BiochemHome page
A. Wada, E. Yamasaki, and T. Hirayama
Helicobacter pylori Vacuolating Cytotoxin, VacA, Is Responsible for Gastric Ulceration
J. Biochem., December 1, 2004; 136(6): 741 - 746.
[Abstract] [Full Text] [PDF]

Home page
 JEMHome page
M. Boncristiano, S. R. Paccani, S. Barone, C. Ulivieri, L. Patrussi, D. Ilver, A. Amedei, M. M. D'Elios, J. L. Telford, and C. T. Baldari
The Helicobacter pylori Vacuolating Toxin Inhibits T Cell Activation by Two Independent Mechanisms
J. Exp. Med., December 15, 2003; 198(12): 1887 - 1897.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. Yahiro, A. Wada, M. Nakayama, T. Kimura, K.-i. Ogushi, T. Niidome, H. Aoyagi, K.-i. Yoshino, K. Yonezawa, J. Moss, et al.
Protein-tyrosine Phosphatase {alpha}, RPTP{alpha}, Is a Helicobacter pylori VacA Receptor
J. Biol. Chem., May 23, 2003; 278(21): 19183 - 19189.
[Abstract] [Full Text] [PDF]

Home page
 Infect. Immun.Home page
H. K. Patel, D. C. Willhite, R. M. Patel, D. Ye, C. L. Williams, E. M. Torres, K. B. Marty, R. A. MacDonald, and S. R. Blanke
Plasma Membrane Cholesterol Modulates Cellular Vacuolation Induced by the Helicobacter pylori Vacuolating Cytotoxin
Infect. Immun., August 1, 2002; 70(8): 4112 - 4123.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Gastrointest. Liver Physiol.Home page
L. Debellis, E. Papini, R. Caroppo, C. Montecucco, and S. Curci
Helicobacter pylori cytotoxin VacA increases alkaline secretion in gastric epithelial cells
Am J Physiol Gastrointest Liver Physiol, December 1, 2001; 281(6): G1440 - G1448.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
V. Ricci, A. Galmiche, A. Doye, V. Necchi, E. Solcia, and P. Boquet
High Cell Sensitivity to Helicobacter pylori VacA Toxin Depends on a GPI-anchored Protein and is not Blocked by Inhibition of the Clathrin-mediated Pathway of Endocytosis
Mol. Biol. Cell, November 1, 2000; 11(11): 3897 - 3909.
[Abstract] [Full Text]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2000 by the American Society for Biochemistry and Molecular Biology.