A Lipocalin-Derived Peptide Modulating Fibroblasts and Extracellular Matrix Proteins
Lipocalin family members have been implicated in development, regeneration, and pathological processes, but their roles are unclear. Interestingly, these proteins are found abundant in the venom of the Lonomia obliqua caterpillar. Lipocalins are β-barrel proteins, which have three conserved motifs i...
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Wiley
2012-01-01
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Series: | Journal of Toxicology |
Online Access: | http://dx.doi.org/10.1155/2012/325250 |
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author | Linda Christian Carrijo-Carvalho Durvanei A. Maria Janaina S. Ventura Kátia L. P. Morais Robson L. Melo Consuelo Junqueira Rodrigues Ana Marisa Chudzinski-Tavassi |
author_facet | Linda Christian Carrijo-Carvalho Durvanei A. Maria Janaina S. Ventura Kátia L. P. Morais Robson L. Melo Consuelo Junqueira Rodrigues Ana Marisa Chudzinski-Tavassi |
author_sort | Linda Christian Carrijo-Carvalho |
collection | DOAJ |
description | Lipocalin family members have been implicated in development, regeneration, and pathological processes, but their roles are unclear. Interestingly, these proteins are found abundant in the venom of the Lonomia obliqua caterpillar. Lipocalins are β-barrel proteins, which have three conserved motifs in their amino acid sequence. One of these motifs was shown to be a sequence signature involved in cell modulation. The aim of this study is to investigate the effects of a synthetic peptide comprising the lipocalin sequence motif in fibroblasts. This peptide suppressed caspase 3 activity and upregulated Bcl-2 and Ki-67, but did not interfere with GPCR calcium mobilization. Fibroblast responses also involved increased expression of proinflammatory mediators. Increase of extracellular matrix proteins, such as collagen, fibronectin, and tenascin, was observed. Increase in collagen content was also observed in vivo. Results indicate that modulation effects displayed by lipocalins through this sequence motif involve cell survival, extracellular matrix remodeling, and cytokine signaling. Such effects can be related to the lipocalin roles in disease, development, and tissue repair. |
format | Article |
id | doaj-art-caacfd716c8f444fbede69b9017ac1f4 |
institution | Kabale University |
issn | 1687-8191 1687-8205 |
language | English |
publishDate | 2012-01-01 |
publisher | Wiley |
record_format | Article |
series | Journal of Toxicology |
spelling | doaj-art-caacfd716c8f444fbede69b9017ac1f42025-02-03T05:45:30ZengWileyJournal of Toxicology1687-81911687-82052012-01-01201210.1155/2012/325250325250A Lipocalin-Derived Peptide Modulating Fibroblasts and Extracellular Matrix ProteinsLinda Christian Carrijo-Carvalho0Durvanei A. Maria1Janaina S. Ventura2Kátia L. P. Morais3Robson L. Melo4Consuelo Junqueira Rodrigues5Ana Marisa Chudzinski-Tavassi6Laboratory of Biochemistry and Biophysics, Butantan Institute, Avenida Vital Brasil 1500, 05503-900 São Paulo, SP, BrazilLaboratory of Biochemistry and Biophysics, Butantan Institute, Avenida Vital Brasil 1500, 05503-900 São Paulo, SP, BrazilLaboratory of Biochemistry and Biophysics, Butantan Institute, Avenida Vital Brasil 1500, 05503-900 São Paulo, SP, BrazilLaboratory of Biochemistry and Biophysics, Butantan Institute, Avenida Vital Brasil 1500, 05503-900 São Paulo, SP, BrazilCenter for Applied Toxinology, Butantan Institute, 05503-900 São Paulo, SP, BrazilDepartment of Orthopedics and Traumatology, Faculty of Medicine, University of São Paulo, 01246-903 São Paulo, SP, BrazilLaboratory of Biochemistry and Biophysics, Butantan Institute, Avenida Vital Brasil 1500, 05503-900 São Paulo, SP, BrazilLipocalin family members have been implicated in development, regeneration, and pathological processes, but their roles are unclear. Interestingly, these proteins are found abundant in the venom of the Lonomia obliqua caterpillar. Lipocalins are β-barrel proteins, which have three conserved motifs in their amino acid sequence. One of these motifs was shown to be a sequence signature involved in cell modulation. The aim of this study is to investigate the effects of a synthetic peptide comprising the lipocalin sequence motif in fibroblasts. This peptide suppressed caspase 3 activity and upregulated Bcl-2 and Ki-67, but did not interfere with GPCR calcium mobilization. Fibroblast responses also involved increased expression of proinflammatory mediators. Increase of extracellular matrix proteins, such as collagen, fibronectin, and tenascin, was observed. Increase in collagen content was also observed in vivo. Results indicate that modulation effects displayed by lipocalins through this sequence motif involve cell survival, extracellular matrix remodeling, and cytokine signaling. Such effects can be related to the lipocalin roles in disease, development, and tissue repair.http://dx.doi.org/10.1155/2012/325250 |
spellingShingle | Linda Christian Carrijo-Carvalho Durvanei A. Maria Janaina S. Ventura Kátia L. P. Morais Robson L. Melo Consuelo Junqueira Rodrigues Ana Marisa Chudzinski-Tavassi A Lipocalin-Derived Peptide Modulating Fibroblasts and Extracellular Matrix Proteins Journal of Toxicology |
title | A Lipocalin-Derived Peptide Modulating Fibroblasts and
Extracellular Matrix Proteins |
title_full | A Lipocalin-Derived Peptide Modulating Fibroblasts and
Extracellular Matrix Proteins |
title_fullStr | A Lipocalin-Derived Peptide Modulating Fibroblasts and
Extracellular Matrix Proteins |
title_full_unstemmed | A Lipocalin-Derived Peptide Modulating Fibroblasts and
Extracellular Matrix Proteins |
title_short | A Lipocalin-Derived Peptide Modulating Fibroblasts and
Extracellular Matrix Proteins |
title_sort | lipocalin derived peptide modulating fibroblasts and extracellular matrix proteins |
url | http://dx.doi.org/10.1155/2012/325250 |
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