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AC‐1001 H3 CDR peptide induces apoptosis and signs of autophagy in vitro and exhibits antimetastatic activity in a syngeneic melanoma model
Antibody‐derived peptides modulate functions of the immune system and are a source of anti‐infective and antitumor substances. Recent studies have shown that they comprise amino acid sequences of immunoglobulin complementarity‐determining regions, but also fragments of constant regions. V(H) CDR3 of...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5011487/ https://www.ncbi.nlm.nih.gov/pubmed/27642552 http://dx.doi.org/10.1002/2211-5463.12080 |
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author | Rabaça, Aline N. Arruda, Denise C. Figueiredo, Carlos R. Massaoka, Mariana H. Farias, Camyla F. Tada, Dayane B. Maia, Vera C. Silva Junior, Pedro I. Girola, Natalia Real, Fernando Mortara, Renato A. Polonelli, Luciano Travassos, Luiz R. |
author_facet | Rabaça, Aline N. Arruda, Denise C. Figueiredo, Carlos R. Massaoka, Mariana H. Farias, Camyla F. Tada, Dayane B. Maia, Vera C. Silva Junior, Pedro I. Girola, Natalia Real, Fernando Mortara, Renato A. Polonelli, Luciano Travassos, Luiz R. |
author_sort | Rabaça, Aline N. |
collection | PubMed |
description | Antibody‐derived peptides modulate functions of the immune system and are a source of anti‐infective and antitumor substances. Recent studies have shown that they comprise amino acid sequences of immunoglobulin complementarity‐determining regions, but also fragments of constant regions. V(H) CDR3 of murine mAb AC‐1001 displays antimetastatic activities using B16F10‐Nex2 murine melanoma cells in a syngeneic model. The peptide was cytotoxic in vitro in murine and human melanoma cells inducing reactive oxygen species (ROS) and apoptosis by the intrinsic pathway. Signs of autophagy were also suggested by the increased expression of LC3/LC3II and Beclin 1 and by ultrastructural evidence. AC‐1001 H3 bound to both G‐ and F‐actin and inhibited tumor cell migration. These results are important evidence of the antitumor activity of Ig CDR‐derived peptides. |
format | Online Article Text |
id | pubmed-5011487 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-50114872016-09-16 AC‐1001 H3 CDR peptide induces apoptosis and signs of autophagy in vitro and exhibits antimetastatic activity in a syngeneic melanoma model Rabaça, Aline N. Arruda, Denise C. Figueiredo, Carlos R. Massaoka, Mariana H. Farias, Camyla F. Tada, Dayane B. Maia, Vera C. Silva Junior, Pedro I. Girola, Natalia Real, Fernando Mortara, Renato A. Polonelli, Luciano Travassos, Luiz R. FEBS Open Bio Research Articles Antibody‐derived peptides modulate functions of the immune system and are a source of anti‐infective and antitumor substances. Recent studies have shown that they comprise amino acid sequences of immunoglobulin complementarity‐determining regions, but also fragments of constant regions. V(H) CDR3 of murine mAb AC‐1001 displays antimetastatic activities using B16F10‐Nex2 murine melanoma cells in a syngeneic model. The peptide was cytotoxic in vitro in murine and human melanoma cells inducing reactive oxygen species (ROS) and apoptosis by the intrinsic pathway. Signs of autophagy were also suggested by the increased expression of LC3/LC3II and Beclin 1 and by ultrastructural evidence. AC‐1001 H3 bound to both G‐ and F‐actin and inhibited tumor cell migration. These results are important evidence of the antitumor activity of Ig CDR‐derived peptides. John Wiley and Sons Inc. 2016-07-15 /pmc/articles/PMC5011487/ /pubmed/27642552 http://dx.doi.org/10.1002/2211-5463.12080 Text en © 2016 The Authors. Published by FEBS Press and John Wiley & Sons Ltd. This is an open access article under the terms of the Creative Commons Attribution (http://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Articles Rabaça, Aline N. Arruda, Denise C. Figueiredo, Carlos R. Massaoka, Mariana H. Farias, Camyla F. Tada, Dayane B. Maia, Vera C. Silva Junior, Pedro I. Girola, Natalia Real, Fernando Mortara, Renato A. Polonelli, Luciano Travassos, Luiz R. AC‐1001 H3 CDR peptide induces apoptosis and signs of autophagy in vitro and exhibits antimetastatic activity in a syngeneic melanoma model |
title |
AC‐1001 H3 CDR peptide induces apoptosis and signs of autophagy in vitro and exhibits antimetastatic activity in a syngeneic melanoma model |
title_full |
AC‐1001 H3 CDR peptide induces apoptosis and signs of autophagy in vitro and exhibits antimetastatic activity in a syngeneic melanoma model |
title_fullStr |
AC‐1001 H3 CDR peptide induces apoptosis and signs of autophagy in vitro and exhibits antimetastatic activity in a syngeneic melanoma model |
title_full_unstemmed |
AC‐1001 H3 CDR peptide induces apoptosis and signs of autophagy in vitro and exhibits antimetastatic activity in a syngeneic melanoma model |
title_short |
AC‐1001 H3 CDR peptide induces apoptosis and signs of autophagy in vitro and exhibits antimetastatic activity in a syngeneic melanoma model |
title_sort | ac‐1001 h3 cdr peptide induces apoptosis and signs of autophagy in vitro and exhibits antimetastatic activity in a syngeneic melanoma model |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5011487/ https://www.ncbi.nlm.nih.gov/pubmed/27642552 http://dx.doi.org/10.1002/2211-5463.12080 |
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