Enhanced RNA expression of tissue inhibitor of metalloproteinases-1 (TIMP-1) in human breast cancer
โ Scribed by Hitoshi Yoshiji; Daniel E. Gomez; Unnur P. Thorgeirsson
- Publisher
- John Wiley and Sons
- Year
- 1996
- Tongue
- French
- Weight
- 408 KB
- Volume
- 69
- Category
- Article
- ISSN
- 0020-7136
No coin nor oath required. For personal study only.
โฆ Synopsis
Tissue inhibitor of metalloproteinases-I (TIMP-I) is known to have at least 2 distinct types of activity, i.e., as a regulator of collagenolytic activity, and erythroid potentiating activity (EPA). In this study, we examined the expression of TIMP-I in human mammary carcinomas, non-malignant breast tissues and benign breast tumors. A total of 53 samples were subjected to Northernblot analysis, including 23 of primary breast cancer, 26 of non-malignant breast tissues, and 4 of benign tumors. Of the 53 samples, I0 were paired malignant and non-malignant breasttissue samples from the same patient. TIMP-I RNA expression was significantly higher in the malignant tumor tissues than in the non-malignant counterpart. Similar differences were ob- sewed in the level of TIMP-I protein expression in the paired breast samples examined. Moreover, breast-cancer cell lines secreted larger amounts of TIMP-I in vitro than non-neoplastic breast epithelial lineis. The up-regulation of TIMP-I expression in breast cancer may suggest that TIMP-I has an additional role to that of metalloprcrteinase inhibitor.
๐ SIMILAR VOLUMES
Degradation of the extracellular matrix (ECM) is an essential step in tumour invasion and metastasis. The matrix metalloproteinases (MMPs) each have different substrate specificities within the ECM and are important in its degradation. MMP activity is dependent on the levels of activated MMP and tis
We analyzed blood plasma concentrations of matrix metalloproteinase-1 and -3 (MMP-1; MMP-3), the tissue inhibitor of metalloproteinase-1 (TIMP-1) and the complex MMP-1/ TIMP-1, and looked for any correlation with prostate cancer stage. These components were measured by ELISA tests specific for these
Proteolysis is an essential component of wound healing but, if uncontrolled, it may lead to degradation of the neo-matrix and a delay in wound repair. Despite numerous reports of impaired wound healing associated with increasing age, the control of proteolysis is completely unknown. Tissue inhibitor
Studies from model systems suggest that matrix metalloproteinases (MMPs) are causally involved in tumor progression while tissue inhibitors of MMPs (TIMPs) prevent this progression. Here, we show that concentrations of TIMP-1 are significantly higher in breast carcinomas than in fibroadenomas. In pr