Matrix metalloproteinases and their inhibitors in canine mammary tumors

<p>Abstract</p> <p>Background</p> <p>Malignant canine mammary tumors represent 50% of all neoplasms in female dogs. Matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs) are thought to be involved in tumor progression, and they are also as...

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Main Authors: Bradaschia Alice, Aricò Arianna, Garbisa Spiridione, Granato Anna, Zancanella Vanessa, Lopparelli Rosa, Castagnaro Massimo, Vascellari Marta, Morello Emanuela, Giantin Mery, Aresu Luca, Mutinelli Franco, Dacasto Mauro
Format: Article
Language:English
Published: BMC 2011-07-01
Series:BMC Veterinary Research
Online Access:http://www.biomedcentral.com/1746-6148/7/33
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author Bradaschia Alice
Aricò Arianna
Garbisa Spiridione
Granato Anna
Zancanella Vanessa
Lopparelli Rosa
Castagnaro Massimo
Vascellari Marta
Morello Emanuela
Giantin Mery
Aresu Luca
Mutinelli Franco
Dacasto Mauro
author_facet Bradaschia Alice
Aricò Arianna
Garbisa Spiridione
Granato Anna
Zancanella Vanessa
Lopparelli Rosa
Castagnaro Massimo
Vascellari Marta
Morello Emanuela
Giantin Mery
Aresu Luca
Mutinelli Franco
Dacasto Mauro
author_sort Bradaschia Alice
collection DOAJ
description <p>Abstract</p> <p>Background</p> <p>Malignant canine mammary tumors represent 50% of all neoplasms in female dogs. Matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs) are thought to be involved in tumor progression, and they are also associated with the reactive stroma, which provides structural and vascular support for tumor growth.</p> <p>Results</p> <p>MMP-2, MMP-9 and MT1-MMP were expressed at both the mRNA and protein levels in tumor samples. MMP-2 and MMP-9 immunohistochemical reactions were evident both in the epithelial tumor cells and in the stromal compartment to varying degrees; in particular, the intensity of the MMP-2 staining was stronger in the stromal fibroblasts close to epithelial tumor cells in simple carcinomas than in adenomas. These data were supported by gelatin-zymography; bands for the active form of MMP-2 were found in 94% of carcinoma samples, compared with 17% of benign tumor samples. The gene expression and immunohistochemical results for MT1-MMP were comparable to those for MMP-2. The immunoreactivity for MMP-13 and TIMP-2 was lower in carcinomas than in adenomas, confirming the mRNA data for MMP-13 and the other MMP inhibitors that were evaluated. The active form of MMP-9, but not the active form of MMP-2, was identified in the plasma of all of the tested dogs.</p> <p>Conclusions</p> <p>Our findings suggest that MMP-9, MMP-2 and MT1-MMP, which are synthesized by epithelial cancer cells and cancer-associated fibroblasts, play an important role in malignant canine mammary tumors. The reduction of MMP-13 and TIMP-2 could also be a significant step in malignant transformation. MMP-2 and MT1-MMP could be further evaluated as future biomarkers for predicting the progression and prognosis of canine mammary tumors.</p>
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spelling doaj.art-df1f8bd44cf34d55a15a39f35ad75c5c2022-12-21T23:31:53ZengBMCBMC Veterinary Research1746-61482011-07-01713310.1186/1746-6148-7-33Matrix metalloproteinases and their inhibitors in canine mammary tumorsBradaschia AliceAricò AriannaGarbisa SpiridioneGranato AnnaZancanella VanessaLopparelli RosaCastagnaro MassimoVascellari MartaMorello EmanuelaGiantin MeryAresu LucaMutinelli FrancoDacasto Mauro<p>Abstract</p> <p>Background</p> <p>Malignant canine mammary tumors represent 50% of all neoplasms in female dogs. Matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs) are thought to be involved in tumor progression, and they are also associated with the reactive stroma, which provides structural and vascular support for tumor growth.</p> <p>Results</p> <p>MMP-2, MMP-9 and MT1-MMP were expressed at both the mRNA and protein levels in tumor samples. MMP-2 and MMP-9 immunohistochemical reactions were evident both in the epithelial tumor cells and in the stromal compartment to varying degrees; in particular, the intensity of the MMP-2 staining was stronger in the stromal fibroblasts close to epithelial tumor cells in simple carcinomas than in adenomas. These data were supported by gelatin-zymography; bands for the active form of MMP-2 were found in 94% of carcinoma samples, compared with 17% of benign tumor samples. The gene expression and immunohistochemical results for MT1-MMP were comparable to those for MMP-2. The immunoreactivity for MMP-13 and TIMP-2 was lower in carcinomas than in adenomas, confirming the mRNA data for MMP-13 and the other MMP inhibitors that were evaluated. The active form of MMP-9, but not the active form of MMP-2, was identified in the plasma of all of the tested dogs.</p> <p>Conclusions</p> <p>Our findings suggest that MMP-9, MMP-2 and MT1-MMP, which are synthesized by epithelial cancer cells and cancer-associated fibroblasts, play an important role in malignant canine mammary tumors. The reduction of MMP-13 and TIMP-2 could also be a significant step in malignant transformation. MMP-2 and MT1-MMP could be further evaluated as future biomarkers for predicting the progression and prognosis of canine mammary tumors.</p>http://www.biomedcentral.com/1746-6148/7/33
spellingShingle Bradaschia Alice
Aricò Arianna
Garbisa Spiridione
Granato Anna
Zancanella Vanessa
Lopparelli Rosa
Castagnaro Massimo
Vascellari Marta
Morello Emanuela
Giantin Mery
Aresu Luca
Mutinelli Franco
Dacasto Mauro
Matrix metalloproteinases and their inhibitors in canine mammary tumors
BMC Veterinary Research
title Matrix metalloproteinases and their inhibitors in canine mammary tumors
title_full Matrix metalloproteinases and their inhibitors in canine mammary tumors
title_fullStr Matrix metalloproteinases and their inhibitors in canine mammary tumors
title_full_unstemmed Matrix metalloproteinases and their inhibitors in canine mammary tumors
title_short Matrix metalloproteinases and their inhibitors in canine mammary tumors
title_sort matrix metalloproteinases and their inhibitors in canine mammary tumors
url http://www.biomedcentral.com/1746-6148/7/33
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