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dc.contributor.author Dos Santos, Célia
dc.contributor.author Hamadat, Sabah
dc.contributor.author Le Saux, Karen
dc.contributor.author Newton, Clara
dc.contributor.author Mazouni, Meriem
dc.contributor.author Zargarian, Loussiné
dc.contributor.author Miro-Padovani, Mickael
dc.contributor.author Zadigue, Patricia
dc.contributor.author Delbé, Jean
dc.contributor.author Hamma-Kourbali, Yamina
dc.contributor.author Amiche, Mohamed
dc.date.available 2018-04-10T13:35:44Z
dc.date.issued 2017-08
dc.identifier.citation Dos Santos, Célia; Hamadat, Sabah; Le Saux, Karen; Newton, Clara; Mazouni, Meriem; et al.; Studies of the antitumor mechanism of action of dermaseptin B2, a multifunctional cationic antimicrobial peptide, reveal a partial implication of cell surface glycosaminoglycans; Public Library of Science; Plos One; 12; 8; 8-2017
dc.identifier.issn 1932-6203
dc.identifier.uri http://hdl.handle.net/11336/41470
dc.description.abstract Dermaseptin-B2 (DRS-B2) is a multifunctional cationic antimicrobial peptide (CAP) isolated from frog skin secretion. We previously reported that DRS-B2 possesses anticancer and antiangiogenic activities in vitro and in vivo. In the present study, we evaluated the antiproliferative activity of DRS-B2 on numerous tumor cell lines, its cell internalization and studies of its molecular partners as well as their influences on its structure. Confocal microscopy using ([Alexa594]-(Cys0)-DRS-B2) shows that in sensitive human tumor cells (PC3), DRS-B2 seems to accumulate rapidly at the cytoplasmic membranes and enters the cytoplasm and the nucleus, while in less sensitive tumor cells (U87MG), DRS-B2 is found packed in vesicles at the cell membrane. Furthermore FACS analysis shows that PC3 cells viability decreases after DRS-B2 treatment while U87 MG seems to be unaffected. However, "pull down" experiments performed with total protein pools from PC3 or U87MG cells and the comparison between the antiproliferative effect of DRS-B2 and its synthetic analog containing all Damino acids suggest the absence of a stereo-selective protein receptor. Pretreatment of PC3 cells with sodium chlorate, decreases the antiproliferative activity of DRS-B2. This activity is partially restored after addition of exogenous chondroitin sulfate C (CS-C). Moreover, we demonstrate that at nanomolar concentrations CS-C potentiates the antiproliferative effect of DRS-B2. These results highlight the partial implication of glycosaminoglycans in the mechanism of antiproliferative action of DRS-B2. Structural analysis of DRS-B2 by circular dichroism in the presence of increasing concentration of CS-C shows that DRS-B2 adopts anα-helical structure. Finally, structure-activity-relationship studies suggest a key role of the W residue in position 3 of the DRS-B2 sequence for its antiproliferative activity.<br /><br />
dc.format application/pdf
dc.language.iso eng
dc.publisher Public Library of Science
dc.rights info:eu-repo/semantics/openAccess
dc.rights.uri https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject DERMASEPTIN B2
dc.subject ANTITUMORAL ACTIVITY
dc.subject GLYCOSAMINOGLYCANS
dc.subject.classification Otras Ciencias Biológicas
dc.subject.classification Ciencias Biológicas
dc.subject.classification CIENCIAS NATURALES Y EXACTAS
dc.title Studies of the antitumor mechanism of action of dermaseptin B2, a multifunctional cationic antimicrobial peptide, reveal a partial implication of cell surface glycosaminoglycans
dc.type info:eu-repo/semantics/article
dc.type info:ar-repo/semantics/artículo
dc.type info:eu-repo/semantics/publishedVersion
dc.date.updated 2018-04-06T13:42:53Z
dc.journal.volume 12
dc.journal.number 8
dc.journal.pais Estados Unidos
dc.journal.ciudad San Francisco
dc.description.fil Fil: Dos Santos, Célia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Centre National de la Recherche Scientifique; Francia
dc.description.fil Fil: Hamadat, Sabah. Centre National de la Recherche Scientifique; Francia. University Paris Est Creteil; Francia
dc.description.fil Fil: Le Saux, Karen. University Paris Est Creteil; Francia
dc.description.fil Fil: Newton, Clara. Centre National de la Recherche Scientifique; Francia. University Paris Est Creteil; Francia
dc.description.fil Fil: Mazouni, Meriem. Centre National de la Recherche Scientifique; Francia. University Paris Est Creteil; Francia
dc.description.fil Fil: Zargarian, Loussiné. Centre National de la Recherche Scientifique; Francia
dc.description.fil Fil: Miro-Padovani, Mickael. University Paris Est Creteil; Francia
dc.description.fil Fil: Zadigue, Patricia. University Paris Est Creteil; Francia
dc.description.fil Fil: Delbé, Jean. University Paris Est Creteil; Francia
dc.description.fil Fil: Hamma-Kourbali, Yamina. University Paris Est Creteil; Francia
dc.description.fil Fil: Amiche, Mohamed. University Paris Est Creteil; Francia
dc.journal.title Plos One
dc.relation.alternativeid info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1371/journal.pone.0182926
dc.relation.alternativeid info:eu-repo/semantics/altIdentifier/url/http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0182926
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info:eu-repo/semantics/openAccess Excepto donde se diga explícitamente, este item se publica bajo la siguiente descripción: Creative Commons Attribution-NonCommercial-ShareAlike 2.5 Unported (CC BY-NC-SA 2.5)