Dual Effect of Serum Amyloid A on the Invasiveness of Glioma Cells
Evidence sustains a role for the acute-phase protein serum amyloid A (SAA) in carcinogenesis and metastasis, and the protein has been suggested as a marker for tumor progression. Nevertheless, the demonstration of a direct activity of SAA on tumor cells is still incipient. We have investigated the e...
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2013-01-01
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Series: | Mediators of Inflammation |
Online Access: | http://dx.doi.org/10.1155/2013/509089 |
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author | Franciele Hinterholz Knebel Renata Chaves Albuquerque Renato Ramos Massaro Silvya Stuchi Maria-Engler Ana Campa |
author_facet | Franciele Hinterholz Knebel Renata Chaves Albuquerque Renato Ramos Massaro Silvya Stuchi Maria-Engler Ana Campa |
author_sort | Franciele Hinterholz Knebel |
collection | DOAJ |
description | Evidence sustains a role for the acute-phase protein serum amyloid A (SAA) in carcinogenesis and metastasis, and the protein has been suggested as a marker for tumor progression. Nevertheless, the demonstration of a direct activity of SAA on tumor cells is still incipient. We have investigated the effect of human recombinant SAA (rSAA) on two human glioma cell lines, A172 and T98G. rSAA stimulated the [3H]-thymidine incorporation of both lines, but had dual effects on migration and invasiveness which varied according to the cell line. In T98G, the rSAA increased migration and invasion behaviors whereas in A172 it decreased these behaviors. These findings agree with the effect triggered by rSAA on matrix metalloproteinases (MMPs) activities measured in a gelatinolytic assay. rSAA inhibited activity of both MMPs in A172 cells while increasing them in T98G cells. rSAA also affected the production of compounds present in the tumor microenvironment that orchestrate tumor progression, such as IL-8, the production of reactive oxygen species (ROS) and nitric oxide (NO). We also observed that both lines expressed all three of the isoforms of SAA: SAA1, SAA2, and SAA4. These data suggest that some tumor cells are responsive to SAA and, in these cases, SAA may have a role in cancer progression that varies according to the cell type. |
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institution | Kabale University |
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language | English |
publishDate | 2013-01-01 |
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series | Mediators of Inflammation |
spelling | doaj-art-3fb3c713ba44466f93ace49b396bbca32025-02-03T06:07:49ZengWileyMediators of Inflammation0962-93511466-18612013-01-01201310.1155/2013/509089509089Dual Effect of Serum Amyloid A on the Invasiveness of Glioma CellsFranciele Hinterholz Knebel0Renata Chaves Albuquerque1Renato Ramos Massaro2Silvya Stuchi Maria-Engler3Ana Campa4Departamento de Análises Clínicas e Toxicológicas, Faculdade de Ciências Farmacêuticas, Universidade de São Paulo, Avenida Prof. Lineu Prestes, 580 Cidade Universitária, 05508-000 São Paulo, SP, BrazilDepartamento de Análises Clínicas e Toxicológicas, Faculdade de Ciências Farmacêuticas, Universidade de São Paulo, Avenida Prof. Lineu Prestes, 580 Cidade Universitária, 05508-000 São Paulo, SP, BrazilDepartamento de Análises Clínicas e Toxicológicas, Faculdade de Ciências Farmacêuticas, Universidade de São Paulo, Avenida Prof. Lineu Prestes, 580 Cidade Universitária, 05508-000 São Paulo, SP, BrazilDepartamento de Análises Clínicas e Toxicológicas, Faculdade de Ciências Farmacêuticas, Universidade de São Paulo, Avenida Prof. Lineu Prestes, 580 Cidade Universitária, 05508-000 São Paulo, SP, BrazilDepartamento de Análises Clínicas e Toxicológicas, Faculdade de Ciências Farmacêuticas, Universidade de São Paulo, Avenida Prof. Lineu Prestes, 580 Cidade Universitária, 05508-000 São Paulo, SP, BrazilEvidence sustains a role for the acute-phase protein serum amyloid A (SAA) in carcinogenesis and metastasis, and the protein has been suggested as a marker for tumor progression. Nevertheless, the demonstration of a direct activity of SAA on tumor cells is still incipient. We have investigated the effect of human recombinant SAA (rSAA) on two human glioma cell lines, A172 and T98G. rSAA stimulated the [3H]-thymidine incorporation of both lines, but had dual effects on migration and invasiveness which varied according to the cell line. In T98G, the rSAA increased migration and invasion behaviors whereas in A172 it decreased these behaviors. These findings agree with the effect triggered by rSAA on matrix metalloproteinases (MMPs) activities measured in a gelatinolytic assay. rSAA inhibited activity of both MMPs in A172 cells while increasing them in T98G cells. rSAA also affected the production of compounds present in the tumor microenvironment that orchestrate tumor progression, such as IL-8, the production of reactive oxygen species (ROS) and nitric oxide (NO). We also observed that both lines expressed all three of the isoforms of SAA: SAA1, SAA2, and SAA4. These data suggest that some tumor cells are responsive to SAA and, in these cases, SAA may have a role in cancer progression that varies according to the cell type.http://dx.doi.org/10.1155/2013/509089 |
spellingShingle | Franciele Hinterholz Knebel Renata Chaves Albuquerque Renato Ramos Massaro Silvya Stuchi Maria-Engler Ana Campa Dual Effect of Serum Amyloid A on the Invasiveness of Glioma Cells Mediators of Inflammation |
title | Dual Effect of Serum Amyloid A on the Invasiveness of Glioma Cells |
title_full | Dual Effect of Serum Amyloid A on the Invasiveness of Glioma Cells |
title_fullStr | Dual Effect of Serum Amyloid A on the Invasiveness of Glioma Cells |
title_full_unstemmed | Dual Effect of Serum Amyloid A on the Invasiveness of Glioma Cells |
title_short | Dual Effect of Serum Amyloid A on the Invasiveness of Glioma Cells |
title_sort | dual effect of serum amyloid a on the invasiveness of glioma cells |
url | http://dx.doi.org/10.1155/2013/509089 |
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