| Investigation on chemotactic drug targeting (chemotaxis and adhesion) inducer effect of GnRH-III derivatives in Tetrahymena and human leukemia cell line. | |
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MedLine Citation:
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PMID: 23208929 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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GnRH-III has been shown to exert a cytotoxic effect on the GnRH-R positive tumor cells. The chemotactic drug targeting (CDT) represents a new way for drug delivery approach based on selective chemoattractant guided targeting. The major goal of the present work was to develop and investigate various GnRH-III derivatives as potential targeting moieties for CDT. The cell physiological effects (chemotaxis, adhesion, and signaling) induced by three native GnRHs (hGnRH-I, cGnRH-II, and lGnRH-III) and nine GnRH-III derivatives were evaluated in two model cells (Tetrahymena pyriformis and Mono Mac 6 human monocytes). According to our results, the native GnRH-III elicited the highest chemoattractant and adhesion inducer activities of all synthesized peptides in micromolar concentrations in monocytes. With respect to chemoattraction, dimeric derivatives linked by a disulfide bridge ([GnRH-III(C)](2) ) proved to be efficient in both model cells; furthermore, acetylation of the linker region ([GnRH-III(Ac-C)](2) ) could slightly improve the chemotactic and adhesion effects in monocytes. The length of the peptide and the type of N-terminal amino acid could also determine the chemotactic and adhesion modulation potency of each fragment. The application of the chemoattractant GnRH-III derivatives was accompanied by a significant activation of phosphatidylinositol 3-kinase in both model cells. In summary, our work on low-level differentiated model cells of tumors has proved that GnRH-III and some of its synthetic derivatives are promising candidates to be applied in CDT: these compounds might act both as carrier, delivery unit, and antitumor agents. Copyright © 2012 European Peptide Society and John Wiley & Sons, Ltd. |
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Authors:
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Eszter Lajkó; Ildikó Szabó; Katalin Andódy; András Pungor; Gábor Mező; László Kőhidai |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2012-12-4 |
Journal Detail:
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Title: Journal of peptide science : an official publication of the European Peptide Society Volume: - ISSN: 1099-1387 ISO Abbreviation: J. Pept. Sci. Publication Date: 2012 Dec |
Date Detail:
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Created Date: 2012-12-4 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9506309 Medline TA: J Pept Sci Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Copyright Information:
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Copyright © 2012 European Peptide Society and John Wiley & Sons, Ltd. |
Affiliation:
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Department of Genetics Cell and Immunobiology, Semmelweis University, Nagyvárad tér. 4, H-1089, Budapest, Hungary. |
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