AC-1001 H3 CDR peptide induces apoptosis and signs of autophagy in vitro and exhibits antimetastatic activity in a syngeneic melanoma model
Autor(a) principal: | |
---|---|
Data de Publicação: | 2016 |
Outros Autores: | , , , , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNIFESP |
Texto Completo: | http://dx.doi.org/10.1002/2211-5463.12080 http://repositorio.unifesp.br/handle/11600/51077 |
Resumo: | 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. |
id |
UFSP_c90a5606549128fbb1cd734bf57536af |
---|---|
oai_identifier_str |
oai:repositorio.unifesp.br/:11600/51077 |
network_acronym_str |
UFSP |
network_name_str |
Repositório Institucional da UNIFESP |
repository_id_str |
3465 |
spelling |
AC-1001 H3 CDR peptide induces apoptosis and signs of autophagy in vitro and exhibits antimetastatic activity in a syngeneic melanoma modelapoptosisautophagyimmunoglobulin CDRmelanomapeptidesAntibody-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.Univ Fed Sao Paulo UNIFESP, Unidade Oncol Expt UNONEX, Sao Paulo, SP, BrazilUniv Mogi das Cruzes, Nucleo Integrado Biotecnol, Mogi Das Cruzes, SP, BrazilUniv Fed Sao Paulo UNIFESP, Dept Ciencia & Tecnol, Sao Jose Dos Campos, BrazilRecepta Biopharma, Sao Paulo, BrazilInst Butantan, Lab Especial Toxinol Aplicada, Sao Paulo, BrazilUniv Fed Sao Paulo UNIFESP, Dept Parasitol, Sao Paulo, SP, BrazilUniv Parma, Dept Biomed Biotechnol & Translat Sci, Microbiol & Virol Unit, I-43100 Parma, ItalyUniv Fed Sao Paulo UNIFESP, Unidade Oncol Expt UNONEX, Sao Paulo, SP, BrazilUniv Fed Sao Paulo UNIFESP, Dept Ciencia & Tecnol, Sao Jose Dos Campos, BrazilUniv Fed Sao Paulo UNIFESP, Dept Parasitol, Sao Paulo, SP, BrazilWeb of ScienceFundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP) [2010/16447-6, 51423-0]Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq)FAPESP:2010/16447-651423-0Wiley2019-07-22T15:46:46Z2019-07-22T15:46:46Z2016info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion885-901http://dx.doi.org/10.1002/2211-5463.12080Febs Open Bio. Hoboken, v. 6, n. 9, p. 885-901, 2016.10.1002/2211-5463.12080WOS000383618300002.pdf2211-5463http://repositorio.unifesp.br/handle/11600/51077WOS:000383618300002enginfo:eu-repo/semantics/openAccessRabaca, Aline N. [UNIFESP]Arruda, Denise C. [UNIFESP]Figueiredo, Carlos R. [UNIFESP]Massaoka, Mariana H. [UNIFESP]Farias, Camyla F. [UNIFESP]Tada, Dayane B. [UNIFESP]Maia, Vera C.Silva Junior, Pedro I.Girola, Natalia [UNIFESP]Real, Fernando [UNIFESP]Mortara, Renato A. [UNIFESP]Polonelli, LucianoTravassos, Luiz R. [UNIFESP]reponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESP2021-09-29T09:32:03Zoai:repositorio.unifesp.br/:11600/51077Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestbiblioteca.csp@unifesp.bropendoar:34652021-09-29T09:32:03Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
dc.title.none.fl_str_mv |
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 |
spellingShingle |
AC-1001 H3 CDR peptide induces apoptosis and signs of autophagy in vitro and exhibits antimetastatic activity in a syngeneic melanoma model Rabaca, Aline N. [UNIFESP] apoptosis autophagy immunoglobulin CDR melanoma peptides |
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_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_sort |
AC-1001 H3 CDR peptide induces apoptosis and signs of autophagy in vitro and exhibits antimetastatic activity in a syngeneic melanoma model |
author |
Rabaca, Aline N. [UNIFESP] |
author_facet |
Rabaca, Aline N. [UNIFESP] Arruda, Denise C. [UNIFESP] Figueiredo, Carlos R. [UNIFESP] Massaoka, Mariana H. [UNIFESP] Farias, Camyla F. [UNIFESP] Tada, Dayane B. [UNIFESP] Maia, Vera C. Silva Junior, Pedro I. Girola, Natalia [UNIFESP] Real, Fernando [UNIFESP] Mortara, Renato A. [UNIFESP] Polonelli, Luciano Travassos, Luiz R. [UNIFESP] |
author_role |
author |
author2 |
Arruda, Denise C. [UNIFESP] Figueiredo, Carlos R. [UNIFESP] Massaoka, Mariana H. [UNIFESP] Farias, Camyla F. [UNIFESP] Tada, Dayane B. [UNIFESP] Maia, Vera C. Silva Junior, Pedro I. Girola, Natalia [UNIFESP] Real, Fernando [UNIFESP] Mortara, Renato A. [UNIFESP] Polonelli, Luciano Travassos, Luiz R. [UNIFESP] |
author2_role |
author author author author author author author author author author author author |
dc.contributor.author.fl_str_mv |
Rabaca, Aline N. [UNIFESP] Arruda, Denise C. [UNIFESP] Figueiredo, Carlos R. [UNIFESP] Massaoka, Mariana H. [UNIFESP] Farias, Camyla F. [UNIFESP] Tada, Dayane B. [UNIFESP] Maia, Vera C. Silva Junior, Pedro I. Girola, Natalia [UNIFESP] Real, Fernando [UNIFESP] Mortara, Renato A. [UNIFESP] Polonelli, Luciano Travassos, Luiz R. [UNIFESP] |
dc.subject.por.fl_str_mv |
apoptosis autophagy immunoglobulin CDR melanoma peptides |
topic |
apoptosis autophagy immunoglobulin CDR melanoma peptides |
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. |
publishDate |
2016 |
dc.date.none.fl_str_mv |
2016 2019-07-22T15:46:46Z 2019-07-22T15:46:46Z |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1002/2211-5463.12080 Febs Open Bio. Hoboken, v. 6, n. 9, p. 885-901, 2016. 10.1002/2211-5463.12080 WOS000383618300002.pdf 2211-5463 http://repositorio.unifesp.br/handle/11600/51077 WOS:000383618300002 |
url |
http://dx.doi.org/10.1002/2211-5463.12080 http://repositorio.unifesp.br/handle/11600/51077 |
identifier_str_mv |
Febs Open Bio. Hoboken, v. 6, n. 9, p. 885-901, 2016. 10.1002/2211-5463.12080 WOS000383618300002.pdf 2211-5463 WOS:000383618300002 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
885-901 |
dc.publisher.none.fl_str_mv |
Wiley |
publisher.none.fl_str_mv |
Wiley |
dc.source.none.fl_str_mv |
reponame:Repositório Institucional da UNIFESP instname:Universidade Federal de São Paulo (UNIFESP) instacron:UNIFESP |
instname_str |
Universidade Federal de São Paulo (UNIFESP) |
instacron_str |
UNIFESP |
institution |
UNIFESP |
reponame_str |
Repositório Institucional da UNIFESP |
collection |
Repositório Institucional da UNIFESP |
repository.name.fl_str_mv |
Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP) |
repository.mail.fl_str_mv |
biblioteca.csp@unifesp.br |
_version_ |
1814268434161074176 |