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http://purl.uniprot.org/citations/25848906http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25848906http://www.w3.org/2000/01/rdf-schema#comment"

Introduction

Matrix metalloproteinase-8 (MMP-8; neutrophil collagenase) is an important regulator of innate immunity that has oncosuppressive actions in numerous tumor types.

Methods

We have intercrossed Mmp8-null mice with the Polyoma virus middle T oncogene-driven (MMTV-PyMT) mouse model of mammary cancer to explore the effects of loss of MMP-8 on the incidence and progression of mammary carcinomas.

Results

In this aggressive mouse model of breast cancer, loss of MMP-8 accelerated tumor onset even further, such that 90% of MMTV-PyMT; Mmp8-null female mice were tumor-bearing at the time of weaning. Throughout the 14 weeks of the model, tumor burden increased in homozygous Mmp8-null mice compared to Mmp8-wild-type and -heterozygote animals. Likewise, lung metastasis dramatically increased in the MMTV-PyMT; Mmp8-null mice. Immunohistochemistry revealed that tumors in wild-type, Mmp8-heterozygotes and -null animals had similar vascular density at 8 weeks, but at 10 weeks Mmp8-wild-type tumors had a lower vascularity than their heterozygote and null counterparts. No differences in macrophage infiltration were apparent throughout primary tumor development, though at 10 weeks a drop in neutrophil infiltrates was observed in Mmp8-wild-type tumors. Using quantitative real-time RT-PCR, we tracked the expression of the entire Mmp and Timp gene families, observing a significant decrease in Mmp3 expression in Mmp8-null tumors compared to wild-type and heterozygotes throughout the time course of the model, which was confirmed at the protein level.

Conclusions

These findings provide novel insight into the suppressive action of MMP-8 on mammary tumorigenesis and metastasis, and indicate that the loss of MMP-8 likely has pleiotropic effects on innate immunity and angiogenesis that are reflected in changes in the protease web."xsd:string
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http://purl.uniprot.org/citations/25848906http://purl.uniprot.org/core/author"Edwards D.R."xsd:string
http://purl.uniprot.org/citations/25848906http://purl.uniprot.org/core/author"Robinson S.D."xsd:string
http://purl.uniprot.org/citations/25848906http://purl.uniprot.org/core/author"Gutierrez-Fernandez A."xsd:string
http://purl.uniprot.org/citations/25848906http://purl.uniprot.org/core/author"Decock J."xsd:string
http://purl.uniprot.org/citations/25848906http://purl.uniprot.org/core/author"Hendrickx W."xsd:string
http://purl.uniprot.org/citations/25848906http://purl.uniprot.org/core/author"Thirkettle S."xsd:string
http://purl.uniprot.org/citations/25848906http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/25848906http://purl.uniprot.org/core/name"Breast Cancer Res"xsd:string
http://purl.uniprot.org/citations/25848906http://purl.uniprot.org/core/pages"38"xsd:string
http://purl.uniprot.org/citations/25848906http://purl.uniprot.org/core/title"Pleiotropic functions of the tumor- and metastasis-suppressing matrix metalloproteinase-8 in mammary cancer in MMTV-PyMT transgenic mice."xsd:string
http://purl.uniprot.org/citations/25848906http://purl.uniprot.org/core/volume"17"xsd:string
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