Cancer · 2002 · 51 citations · 21 references
Life SciencesMolecular BiologyPathologyCarcinogenesisGene ExpressionNeoplasiaEndometrial CancerExtracellular MatrixTumor MarkersMatrix Metalloproteinase Gene ExpressionMatrix Metalloproteinases
BACKGROUND: The human matrix metalloproteinase (MMP)-26, also called matrilysin-2 or endometase, has been isolated as a matrilysin (MMP-7) homolog. Matrix metalloproteinase-26 was expressed in tissue samples from the placenta and endometrial tumors and its expression may be related to the development of endometrial carcinomas. METHODS: Total RNAs were isolated from 5 endometrial carcinoma cell lines, 36 normal endometrial tissue samples, 4 hyperplasia tissue samples, and from 24 endometrial carcinoma tissue samples. Reverse transcription-polymerase chain reation (RT-PCR) was performed to detect MMP-26 mRNA expression. To identify MMP-26 mRNA localization and protein expression, we performed in situ RT-PCR and immunohistochemistry, respectively. RESULTS: Reverse transcription-polymerase chain reaction analysis revealed that MMP-26 mRNA was expressed in 24 of 36 normal human endometrial tissue samples. However, MMP-26 mRNA expression was not detected in endometrial carcinoma cell lines nor in endometrial carcinoma tissue samples except for one case. Western blot analysis showed similar results. In situ RT-PCR analysis revealed that MMP-26 expression was localized in the epithelial glandular cells but faint expression was observed in the stromal cells. Subsequently, we separated endometrial tissues into epithelial glandular and stromal cells. Using RT-PCR, the purified epithelial glandular cells exhibited MMP-26 mRNA expression but the purified stromal cells did not. Immunohistochemical analyses revealed that MMP-26 protein expression is also limited to endometrial epithelial glandular cells but not to cancer cells. Therefore, MMP-26 expression is limited to normal epithelial glandular cells. CONCLUSIONS: We found a significant difference in MMP-26 expression in normal and malignant endometrial tissue samples, although its function is still unknown. These data suggest that MMP-26 may be a candidate for a new tumor marker for endometrial carcinomas.
21
Matrix Metalloproteinases: Biologic Activity and Clinical Implications
Amy R. Nelson, Barbara Fingleton, Mace L. Rothenberg et al. · Journal of Clinical Oncology · 2000 · 1.6K citations
Medicine, Cancer Biology, Oncology +14
The Stromal Proteinase MMP3/Stromelysin-1 Promotes Mammary Carcinogenesis
Mark D. Sternlicht, André Lochter, Carolyn J. Sympson et al. · Cell · 1999 · 927 citations · Full text
Matrix metalloproteinase–1 is associated with poor prognosis in colorectal cancer
Graeme I. Murray, Margaret E. Duncan, Pauline O'Neil et al. · Nature Medicine · 1996 · 447 citations
Medicine, Cancer Biology, Oncology +11
Matrix metalloproteinase–1 is associated with poor prognosis in colorectal cancer
Graeme I. Murray, Margaret E. Duncan, Pauline O'Neil et al. · Nature Medicine · 1996 · 323 citations
Medicine, Cancer Biology, Oncology +11
Gloria Velasco, Alberto M. Pendás, Antonio Fueyo et al. · Journal of Biological Chemistry · 1999 · 229 citations · Full text