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. Copyright 2003 American Cancer Society.
BACKGROUND: The humanmatrix 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. Copyright 2003 American Cancer Society.
Authors: Petra Horka; Karin Malickova; Radka Jarosova; Ivana Janatkova; Tomas Zima; Marta Kalousova Journal: J Assist Reprod Genet Date: 2012-09-28 Impact factor: 3.412
Authors: V O Bister; M T Salmela; M L Karjalainen-Lindsberg; J Uria; J Lohi; P Puolakkainen; C Lopez-Otin; U Saarialho-Kere Journal: Dig Dis Sci Date: 2004-04 Impact factor: 3.199