scholarly journals Cell surface nucleolin on developing muscle is a potential ligand for the axonal receptor protein tyrosine phosphatase-σ

FEBS Journal ◽  
2006 ◽  
Vol 273 (20) ◽  
pp. 4668-4681 ◽  
Author(s):  
Daniel E. Alete ◽  
Mark E. Weeks ◽  
Ara G. Hovanession ◽  
Muhamed Hawadle ◽  
Andrew W. Stoker
Keyword(s):  
Cell Surface ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Receptor Protein ◽  
Protein Tyrosine ◽  
Receptor Protein Tyrosine Phosphatase ◽  
Surface Nucleolin ◽  
Cell Surface Nucleolin ◽  
Potential Ligand ◽  
Developing Muscle

scholarly journals The Cell-Specific Phenotype of the Polymorphic vacA Midregion Is Independent of the Appearance of the Cell Surface Receptor Protein Tyrosine Phosphatase β

2006 ◽  
Vol 74 (1) ◽  
pp. 49-55 ◽  
Author(s):  
David A. G. Skibinski ◽  
Christophe Genisset ◽  
Silvia Barone ◽  
John L. Telford
Keyword(s):  
Cell Surface ◽  
Cell Lines ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Cell Surface Receptor ◽  
Receptor Protein ◽  
Protein Tyrosine ◽  
Amino Acid Region ◽  
Receptor Protein Tyrosine Phosphatase ◽  
Surface Receptor

ABSTRACT There are two alleles, m1 and m2, of the midregion of the vacuolating cytotoxin gene (vacA) of Helicobacter pylori which code for toxins with different cell specificities. Here we describe the construction of five chimeric strains in which regions of vacA were exchanged between the two genotypes. By analyzing the toxicity of these strains for HeLa and RK13 cells we have confirmed that a 148-amino-acid region determines the phenotypic differences between the two forms of the protein and that this entire region is important for cytotoxicity. Furthermore, we have used our chimeric strains to investigate whether variations in the midregion of VacA have an effect on phorbol 12-myristate 13-acetate (PMA)-induced VacA sensitivity in HL-60 cells. The PMA-induced VacA sensitivity of HL-60 cells has been previously associated with the appearance of the cell surface receptor protein tyrosine phosphatase beta (RPTPβ). Our data indicate that both the m1 and m2 forms of VacA are able to utilize RPTPβ, and the cell-specific phenotype of the midregion is independent of the presence of RPTPβ. It appears that another as-yet-unidentified receptor exists in HL-60 cells that accounts for the m2 phenotype in this cell line. Also, by studying the effect of PMA on levels of RPTPβ in other cell lines and toxicity of VacA in these cell lines we have shown that RPTPβ does not play a major role in the vacuolation of HeLa cells.

scholarly journals The receptor protein tyrosine phosphatase (RPTP)β/ζ is expressed in different subtypes of human breast cancer

2007 ◽  
Vol 362 (1) ◽  
pp. 5-10 ◽  
Author(s):  
Pablo Perez-Pinera ◽  
Olivia Garcia-Suarez ◽  
Primitiva Menendez-Rodriguez ◽  
J. Mortimer ◽  
Y. Chang ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Protein Tyrosine Phosphatase ◽  
Human Breast Cancer ◽  
Tyrosine Phosphatase ◽  
Receptor Protein ◽  
Human Breast ◽  
Protein Tyrosine ◽  
Receptor Protein Tyrosine Phosphatase

scholarly journals The receptor protein tyrosine phosphatase PTPRJ negatively modulates the CD98hc oncoprotein in lung cancer cells

Oncotarget ◽  
2018 ◽  
Vol 9 (34) ◽  
pp. 23334-23348 ◽  
Author(s):  
Sabrina D’Agostino ◽  
Delia Lanzillotta ◽  
Mariaconcetta Varano ◽  
Cirino Botta ◽  
Antonio Baldrini ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Cancer Cells ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Lung Cancer Cells ◽  
Receptor Protein ◽  
Protein Tyrosine ◽  
Receptor Protein Tyrosine Phosphatase

scholarly journals Promoting Receptor Protein Tyrosine Phosphatase Activity by Targeting Transmembrane Domain Interactions

2021 ◽  
Vol 35 (S1) ◽  
Author(s):  
Damien Thévenin ◽  
Eden Sikorski ◽  
Jacqueline Gerritsen ◽  
Forest White ◽  
Matthew Lazzara
Keyword(s):  
Phosphatase Activity ◽  
Protein Tyrosine Phosphatase ◽  
Transmembrane Domain ◽  
Tyrosine Phosphatase ◽  
Receptor Protein ◽  
Protein Tyrosine ◽  
Receptor Protein Tyrosine Phosphatase ◽  
Domain Interactions

scholarly journals Expression of the Receptor Protein-tyrosine Phosphatase, PTPμ, Restores E-cadherin-dependent Adhesion in Human Prostate Carcinoma Cells

2002 ◽  
Vol 277 (13) ◽  
pp. 11165-11173 ◽  
Author(s):  
Carina B. Hellberg ◽  
Susan M. Burden-Gulley ◽  
Gregory E. Pietz ◽  
Susann M. Brady-Kalnay
Keyword(s):  
Prostate Carcinoma ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Carcinoma Cells ◽  
Human Prostate ◽  
Receptor Protein ◽  
Protein Tyrosine ◽  
Receptor Protein Tyrosine Phosphatase ◽  
Human Prostate Carcinoma ◽  
E Cadherin

scholarly journals Receptor protein tyrosine phosphatase alpha activates pp60c-src and is involved in neuronal differentiation.

1993 ◽  
Vol 12 (10) ◽  
pp. 3789-3798 ◽  
Author(s):  
J. den Hertog ◽  
C.E. Pals ◽  
M.P. Peppelenbosch ◽  
L.G. Tertoolen ◽  
S.W. de Laat ◽  
...  
Keyword(s):  
Neuronal Differentiation ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Receptor Protein ◽  
Protein Tyrosine ◽  
Receptor Protein Tyrosine Phosphatase

scholarly journals Receptor protein tyrosine phosphatase σ binds to neurons in the adult mouse brain

2014 ◽  
Vol 255 ◽  
pp. 12-18 ◽  
Author(s):  
Jae-Hyuk Yi ◽  
Yasuhiro Katagiri ◽  
Panpan Yu ◽  
Jacob Lourie ◽  
Nathanael J. Bangayan ◽  
...  
Keyword(s):  
Mouse Brain ◽  
Protein Tyrosine Phosphatase ◽  
Adult Mouse ◽  
Tyrosine Phosphatase ◽  
Receptor Protein ◽  
Adult Mouse Brain ◽  
Protein Tyrosine ◽  
Receptor Protein Tyrosine Phosphatase
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