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Nanostructured, Self-Assembling Peptide K5 Blocks TNF-α and PGE(2) Production by Suppression of the AP-1/p38 Pathway
Nanostructured, self-assembling peptides hold promise for a variety of regenerative medical applications such as 3D cell culture systems, accelerated wound healing, and nerve repair. The aim of this study was to determine whether the self-assembling peptide K5 can be applied as a carrier of anti-inf...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Hindawi Publishing Corporation
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3270444/ https://www.ncbi.nlm.nih.gov/pubmed/22315508 http://dx.doi.org/10.1155/2012/489810 |
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author | Yang, Woo Seok Park, Yung Chul Kim, Ji Hye Kim, Hye Ri Yu, Tao Byeon, Se Eun Unsworth, Larry D. Lee, Jaehwi Cho, Jae Youl |
author_facet | Yang, Woo Seok Park, Yung Chul Kim, Ji Hye Kim, Hye Ri Yu, Tao Byeon, Se Eun Unsworth, Larry D. Lee, Jaehwi Cho, Jae Youl |
author_sort | Yang, Woo Seok |
collection | PubMed |
description | Nanostructured, self-assembling peptides hold promise for a variety of regenerative medical applications such as 3D cell culture systems, accelerated wound healing, and nerve repair. The aim of this study was to determine whether the self-assembling peptide K5 can be applied as a carrier of anti-inflammatory drugs. First, we examined whether the K5 self-assembling peptide itself can modulate various cellular inflammatory responses. We found that peptide K5 significantly suppressed the release of tumor-necrosis-factor- (TNF-) α and prostaglandin E(2) (PGE(2)) from RAW264.7 cells and peritoneal macrophages stimulated by lipopolysaccharide (LPS). Similarly, there was inhibition of cyclooxygenase- (COX-) 2 mRNA expression assessed by real-time PCR, indicating that the inhibition is at the transcriptional level. In agreement with this finding, peptide K5 suppressed the translocation of the transcription factors activator protein (AP-1) and c-Jun and inhibited upstream inflammatory effectors including mitogen activated protein kinase (MAPK), p38, and mitogen-activated protein kinase kinase 3/6 (MKK 3/6). Whether this peptide exerts its effects via a transmembrane or cytoplasmic receptor is not clear. However, our data strongly suggest that the nanostructured, self-assembling peptide K5 may possess significant anti-inflammatory activity via suppression of the p38/AP-1 pathway. |
format | Online Article Text |
id | pubmed-3270444 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-32704442012-02-07 Nanostructured, Self-Assembling Peptide K5 Blocks TNF-α and PGE(2) Production by Suppression of the AP-1/p38 Pathway Yang, Woo Seok Park, Yung Chul Kim, Ji Hye Kim, Hye Ri Yu, Tao Byeon, Se Eun Unsworth, Larry D. Lee, Jaehwi Cho, Jae Youl Mediators Inflamm Research Article Nanostructured, self-assembling peptides hold promise for a variety of regenerative medical applications such as 3D cell culture systems, accelerated wound healing, and nerve repair. The aim of this study was to determine whether the self-assembling peptide K5 can be applied as a carrier of anti-inflammatory drugs. First, we examined whether the K5 self-assembling peptide itself can modulate various cellular inflammatory responses. We found that peptide K5 significantly suppressed the release of tumor-necrosis-factor- (TNF-) α and prostaglandin E(2) (PGE(2)) from RAW264.7 cells and peritoneal macrophages stimulated by lipopolysaccharide (LPS). Similarly, there was inhibition of cyclooxygenase- (COX-) 2 mRNA expression assessed by real-time PCR, indicating that the inhibition is at the transcriptional level. In agreement with this finding, peptide K5 suppressed the translocation of the transcription factors activator protein (AP-1) and c-Jun and inhibited upstream inflammatory effectors including mitogen activated protein kinase (MAPK), p38, and mitogen-activated protein kinase kinase 3/6 (MKK 3/6). Whether this peptide exerts its effects via a transmembrane or cytoplasmic receptor is not clear. However, our data strongly suggest that the nanostructured, self-assembling peptide K5 may possess significant anti-inflammatory activity via suppression of the p38/AP-1 pathway. Hindawi Publishing Corporation 2012 2012-01-24 /pmc/articles/PMC3270444/ /pubmed/22315508 http://dx.doi.org/10.1155/2012/489810 Text en Copyright © 2012 Woo Seok Yang et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Yang, Woo Seok Park, Yung Chul Kim, Ji Hye Kim, Hye Ri Yu, Tao Byeon, Se Eun Unsworth, Larry D. Lee, Jaehwi Cho, Jae Youl Nanostructured, Self-Assembling Peptide K5 Blocks TNF-α and PGE(2) Production by Suppression of the AP-1/p38 Pathway |
title | Nanostructured, Self-Assembling Peptide K5 Blocks TNF-α and PGE(2) Production by Suppression of the AP-1/p38 Pathway |
title_full | Nanostructured, Self-Assembling Peptide K5 Blocks TNF-α and PGE(2) Production by Suppression of the AP-1/p38 Pathway |
title_fullStr | Nanostructured, Self-Assembling Peptide K5 Blocks TNF-α and PGE(2) Production by Suppression of the AP-1/p38 Pathway |
title_full_unstemmed | Nanostructured, Self-Assembling Peptide K5 Blocks TNF-α and PGE(2) Production by Suppression of the AP-1/p38 Pathway |
title_short | Nanostructured, Self-Assembling Peptide K5 Blocks TNF-α and PGE(2) Production by Suppression of the AP-1/p38 Pathway |
title_sort | nanostructured, self-assembling peptide k5 blocks tnf-α and pge(2) production by suppression of the ap-1/p38 pathway |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3270444/ https://www.ncbi.nlm.nih.gov/pubmed/22315508 http://dx.doi.org/10.1155/2012/489810 |
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