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The Antitumor Peptide CIGB-552 Increases COMMD1 and Inhibits Growth of Human Lung Cancer Cells.
Fernández Massó, Julio R; Oliva Argüelles, Brizaida; Tejeda, Yelaine; Astrada, Soledad; Garay, Hilda; Reyes, Osvaldo; Delgado-Roche, Livan; Bollati-Fogolín, Mariela; Vallespí, Maribel G.
Afiliação
  • Fernández Massó JR; Department of Genomic, Center for Genetic Engineering and Biotechnology, Cubanacan, P.O. Box 6162, 10600 Havana, Cuba.
J Amino Acids ; 2013: 251398, 2013.
Article em En | MEDLINE | ID: mdl-23401744
We have demonstrated that the peptide L-2 designed from an alanine scanning of the Limulus-derived LALF32-51 region is a potential candidate for the anticancer therapy and its cell-penetrating capacity is an associated useful property. By the modification in the primary structure of L-2, a second-generation peptide (CIGB-552) was developed. However, the molecular mechanism underlying its cytotoxic activity remains partially unknown. In this study, it was shown that CIGB-552 increases the levels of COMMD1, a protein involved in copper homeostasis, sodium transport, and the NF-κB signaling pathway. We found that CIGB-552 induces ubiquitination of RelA and inhibits the antiapoptotic activity regulated by NF-κB, whereas the knockdown of COMMD1 blocks this effect. We also found that CIGB-552 decreases the antioxidant capacity and induces the peroxidation of proteins and lipids in the tumor cells. Altogether, this study provides new insights into the mechanism of action of the peptide CIGB-552, which could be relevant in the design of future anticancer therapies.

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Revista: J Amino Acids Ano de publicação: 2013 Tipo de documento: Article País de afiliação: Cuba País de publicação: Egito

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Revista: J Amino Acids Ano de publicação: 2013 Tipo de documento: Article País de afiliação: Cuba País de publicação: Egito