Expression of matrix metalloproteinases (MMPs) in primary human breast cancer and breast cancer cell lines: New findings and review of the literature

<p>Abstract</p> <p>Background</p> <p>Matrix metalloproteinases (MMPs) are a family of structural and functional related endopeptidases. They play a crucial role in tumor invasion and building of metastatic formations because of their ability to degrade extracellular matrix proteins. Under physiological conditions their activity is precisely regulated in order to prevent tissue disruption. This physiological balance seems to be disrupted in cancer making tumor cells capable of invading the tissue. In breast cancer different expression levels of several MMPs have been found.</p> <p>Methods</p> <p>To fill the gap in our knowledge about MMP expression in breast cancer, we analyzed the expression of all known human MMPs in a panel of twenty-five tissue samples (five normal breast tissues, ten grade 2 (G2) and ten grade 3 (G3) breast cancer tissues). As we found different expression levels for several MMPs in normal breast and breast cancer tissue as well as depending on tumor grade, we additionally analyzed the expression of MMPs in four breast cancer cell lines (MCF-7, MDA-MB-468, BT 20, ZR 75/1) commonly used in research. The results could thus be used as model for further studies on human breast cancer. Expression analysis was performed on mRNA and protein level using semiquantitative RT-PCR, Western blot, immunohistochemistry and immunocytochemistry.</p> <p>Results</p> <p>In summary, we identified several MMPs (MMP-1, -2, -8, -9, -10, -11, -12, -13, -15, -19, -23, -24, -27 and -28) with a stronger expression in breast cancer tissue compared to normal breast tissue. Of those, expression of MMP-8, -10, -12 and -27 is related to tumor grade since it is higher in analyzed G3 compared to G2 tissue samples. In contrast, MMP-7 and MMP-27 mRNA showed a weaker expression in tumor samples compared to healthy tissue. In addition, we demonstrated that the four breast cancer cell lines examined, are constitutively expressing a wide variety of MMPs. Of those, MDA-MB-468 showed the strongest mRNA and protein expression for most of the MMPs analyzed.</p> <p>Conclusion</p> <p>MMP-1, -2, -8, -9, -10, -11, -12, -13, -15, -19, -23, -24, -27 and -28 might thus be associated with breast cancer development and tumor progression. Therefore, these MMPs are proper candidates for further functional analysis of their role in breast cancer.</p

Roles of trifluoroacetic acid, acetic acid and their salts in the synthesis of helical mesoporous materials

Helical mesoporous materials have attracted much attention due to their potential applications in catalysis and chiral recognition. In this paper, we have systematically studied the influence of trifluoroacetic acid, acetic acid and their salts on the synthesis of helical mesoporous materials in the presence of a cationic surfactant cetyltrimethylammonium bromide (CTAB) as a template. Results show that helical mesostructures can be successfully synthesized when CF(3)COO(-) anions were used as additives with an additive/CATB molar ratio (R) range of 0.1-0.375 for the CF(3)COOH/CTAB templating system and a relatively wider R range of 0.1-0.5 for the CF(3)COONa/CTAB templating system, which can be attributed to the influence of pH caused by the acid- or salt-form of additives. The pitch sizes of the helical mesostructures can be finely controlled by varying the additive/CTAB ratio. The results indicate that in order to synthesize helical mesostructures in a broad range of additive/CTAB ratios, the perfluorinated salt with a short fluorocarbon chain should be used. Our synthesis strategy can be used for the fabrication of helical mesostructured porous materials with adjustable pore and helical pitch sizes, which are important in their potential applications