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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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