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Association of the MMP7 –181A>G promoter polymorphism with early onset of chronic obstructive pulmonary disease

the extracellular matrix and cell-surface proteins to regulate wound healing, physiological angiogenesis and immune response [ 8 ]. Matrix metalloproteinases can activate and increase the bioavailability of a variety of non matrix proteins, including cytokines, chemokines, recep-tors and antimicrobial peptides [ 5 , 9 ]. Matrilysin 1 (MMP-7), unlike many MMPs, is expressed by non injured, non inflamed mucosal epithelia in most adult human tissues (7). Besides extracellular matrix (ECM) components, MMP-7 processes cell surface molecules such as pro-defensin, Fas

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Single nucleotide polymorphisms in genes MACC1, RAD18, MMP7 and SDF-1a as prognostic factors in resectable colorectal cancer

and disease dissemination: SDF-1a (stromal derived factor 1 alpha) located on chromosome 10, MMP7 located on chromosome 11, RAD18 located on chromosome 3, and MACC1 (metastasis associated in colorectal cancer 1) located on chromosome 7. 19 – 22 The aim of our study was to evaluate the role of SNPs in selected genes as prognostic markers in resectable CRC. Patients and methods We have conducted a study, regarding the role of selected SNPs in resectable CRC. In total, 163 consecutive patients treated surgically at University Medical Centre in Maribor

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Influence of Polyphenol Extract from Evening Primrose (Oenothera Paradoxa) Seeds on Proliferation of Caco-2 Cells and on Expression, Synthesis and Activity of Matrix Metalloproteinases and Their Inhibitors

Abstract

Evening primrose (Oenothera paradoxa Hudziok) seeds are a rich source of not only a valuable oil containing an essential fatty acid - ᵧ-linolenic acid (GLA) - but also polyphenols which can be obtained from the biomass remaining after oil pressing. The aim of our studies was to evaluate the influence of a polyphenol extract from defatted seeds of evening primrose on human colorectal adenocarcinoma Caco-2 cell proliferation and matrix metalloproteinases (MMPs) synthesis and activity. To assess the effect of evening primrose extract on Caco-2 cell proliferation, crystal violet staining and sulforhodamine B (SRB) assays were used whereas mRNA expression and activity of MMPs were evaluated by RT-PCR and gelatin zymography.

The results revealed that the examined polyphenol extract had little influence on Caco-2 proliferation, but effectively in a time- and dose-dependent manner inhibited MMP-1, MMP-7, MMP-9 and MMP-14 mRNA synthesis induced by TNF-α and TPA. Additionally, zymographic analysis revealed that after 24 h, the polyphenol extract at a concentration of 50 μmol/L GAE caused a 10-fold reduction in MMP-9 synthesis. Moreover, this extract might be a potent inhibitor of MMP activity. The results showed that polyphenol extract from evening primrose inhibited PBMC-derived MMP-2 and MMP-9 enzymatic activity in dose-dependent manner. The obtained results indicate that the polyphenol extract from evening primrose seeds could be an inhibitor of proteases involved in tumor progression and metastasis.

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Risk of peritoneal dissemination in stomach cancer

, Lai HS, Jeng YM, Chen CI, Chang KJ, et al. Connective tissue growth factor inhibits gastric cancer peritoneal metastasis by blocking integrin alpha3beta1-dependent adhesion. Gastric Cancer. 2015;18(3):504-15. 12. Yonemura Y, Endou Y, Fujita H, Fushida S, Bandou E, Taniguchi K, et al. Role of MMP-7 in the formation of peritoneal dissemination in gastric cancer. Gastric Cancer. 2000;3(2):63-70. 13. Javle M, Smyth EC, Chau I. Ramucirumab: successfully targeting angiogenesis in gastric cancer. Clin Cancer Res. 2014;20(23):5875-81. 14. Sugarbaker TA CD

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Differences in plasma TIMP-1 levels between healthy people and patients with rectal cancer stage II or III

References Pesta M, Topolcan O, Holubec L, Rupert K, Cerna M, Holubec L, et al. Clinicopathological assesment and quantitative estimation of the matrix metalloproteinases MMP-2 and MMP-7 and the inhibitors TIMP-1 and TIMP-2 in colorectal carcinoma tissue samples. Anticancer Res 2007; 27: 1863-8. Li M, Yamamoto H, Adachi Y, Maruyama Y, Shinomura Y. Role of matrix metaloproteinase-7 (matrilysin) in human cancer invasion, apoptosis, growth and angiogenesis. Exp Biol Med 2006; 231: 20

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The correlation between the levels of tissue inhibitor of metalloproteinases 1 in plasma and tumour response and survival after preoperative radiochemotherapy in patients with rectal cancer

, Oblak I, Anderluh F. Cetuximab in preoperative treatment of rectal cancer - term outcome of the XERT trial. Radiol Oncol 2012; 46: 252-7. 4. Pesta M, Topolcan O, Holubec L Jr, Rupert K, Cerna M, Holubec LS, et al. Clinicopathological assesment and quantitative estimation of the matrix metalloproteinases MMP-2 and MMP-7 and the inhibitors TIMP-1 and TIMP-2 in colorectal carcinoma tissue samples. Anticancer Res 2007; 27: 1863-7. 5. Li M, Yamamoto H, Adachi Y, Maruyama Y, Shinomura Y. Role of matrix metaloproteinase-7 (matrilysin

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Urine biomarkers in renal allograft

differentiation. And the activation of the Tim-3–Galectin-9 pathway attenuates cytotoxicity and prolongs the survival of organ allografts in mice.[ 24 ] Matrix Metalloproteinase-7 Matrilysin, also known as matrix metalloproteinase-7 (MMP-7), is an enzyme in humans that is encoded by the MMP7 gene. Levels of circulating MMPs and TIMPs fluctuate in SLE, and increased MMP-2, MMP-3, MMP-7, TIMP-1 and TIMP-2 probably reflect an aggravated inflammatory process, whereas lower concentrations of MMP-9 can result from the accumulation of MMPs in the inflamed blood vessels and

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Myeloperoxidase: New Roles for an Old Molecule

, Heinecke JW. Hypochlorous acid oxygenates the cysteine switch domain of promatrilysin (MMP-7). A mechanism for matrix metalloproteinase activation and atherosclerotic plaque rupture by myeloperoxidase. J Biol Chem 2001; 276: 41279-87. Sugiyama S, Okada Y, Sukhova GK, Virmani R, Heinecke JW, Libby P. Macrophage myeloperoxidase regulation by granulocyte macrophage colony-stimulating factor in human atherosclerosis and implications in acute coronary syndromes. Am J Pathol 2001; 158: 879-91. Baldus S, Eiserich JP, Mani A

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