Abstract | BACKGROUND: RESULTS: Our results show that P(122-131) inhibits in vitro adhesion, anchorage-independent proliferation, and migration of DU145 and LNCaP cells, which express pleiotrophin and its receptor RPTPβ/ζ. In addition, P(122-131) inhibits angiogenesis in vivo, as determined by the chicken embryo CAM assay. Investigation of the transduction mechanisms revealed that P(122-131) reduces the phosphorylation levels of Src, Pten, Fak, and Erk1/2. Finally, P(122-131) not only interacts with RPTPβ/ζ, but also interferes with other pleiotrophin receptors, as demonstrated by selective knockdown of pleiotrophin or RPTPβ/ζ expression with the RNAi technology. CONCLUSIONS: In conclusion, our results demonstrate that P(122-131) inhibits biological activities that are related to the induction of a transformed phenotype in PCa cells, by interacing with RPTPβ/ζ and interfering with other pleiotrophin receptors. Cumulatively, these results indicate that P(122-131) may be a potential anticancer agent, and they warrant further study of this peptide.
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Authors | Zoi Diamantopoulou, Oya Bermek, Apostolos Polykratis, Yamina Hamma-Kourbali, Jean Delbé, José Courty, Panagiotis Katsoris |
Journal | Molecular cancer
(Mol Cancer)
Vol. 9
Pg. 224
(Aug 25 2010)
ISSN: 1476-4598 [Electronic] England |
PMID | 20738847
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Carrier Proteins
- Cytokines
- Peptide Fragments
- pleiotrophin
- Receptor-Like Protein Tyrosine Phosphatases, Class 5
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Topics |
- Carrier Proteins
(chemistry)
- Cell Adhesion
(drug effects)
- Cell Line, Tumor
- Cell Proliferation
(drug effects)
- Cytokines
(chemistry)
- Humans
- Peptide Fragments
(pharmacology)
- Receptor-Like Protein Tyrosine Phosphatases, Class 5
(metabolism)
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