Zymographic Detection and Clinical Correlations of Cysteine Cathepsin and Matrix Metalloproteinase in Human Breast Cancer Tissue
| dc.contributor.advisor | Kibret, Belayhun (PhD) | |
| dc.contributor.author | Tsegaye, Solomon | |
| dc.date.accessioned | 2018-06-24T17:57:33Z | |
| dc.date.accessioned | 2023-11-29T04:18:19Z | |
| dc.date.available | 2018-06-24T17:57:33Z | |
| dc.date.available | 2023-11-29T04:18:19Z | |
| dc.date.issued | 2016-06 | |
| dc.description.abstract | Breast cancer is the most frequent cause of cancer death in women in less developed countries including Ethiopia. Cellular proteases thought to increase the likelihood of cancer invasion and metastasis by degrading components of extracellular matrix. These proteases could be used as tumor markers for early diagnosis, monitoring the prognosis or targeting therapeutics drugs. Objective: To investigate zymographic detection and clinical correlations of cysteine cathepsins and matrix metalloproteinase in human breast cancer tissue Methodology: Hospital based cross-sectional study was conducted from January 2015 to June 2015. Thirty six women with breast cancer, who underwent mastectomy for first time were recruited from surgery department of Menelik II Hospital, Saint Paul’s Millennium Medical College and Zewditu Memorial Hospital. Both tumor and normal tissues were harvested from the same patient within 10 minute after surgery. The tissue was processed and metastatic protease activity was evaluated by measuring functional enzymatic activity of cathepsin K, cathepsin L, and matrix metalloproteinase-2 and matrix metalloproteinase-9 using zymography and quantified by densitometry. Result: Normal and tumor tissue specimens were tested for functional cathepsins and matrix metalloproteinases activities. Mean cathepsin K activity was significantly higher in tumor tissue specimens than the activity detected in normal breast tissue specimens (n = 36, p < 0.001), mean cathepsin L activity was also significantly higher in tumor tissue than normal tissue specimens (n = 36, P < 0.001). Furthermore, mean matrix metalloproteinase-2 and -9 activities in tumor breast tissue was significantly higher in tumor tissue than normal tissue (P < 0.05). Conclusion: Our result showed different pattern of protease activity expression between normal and tumor tissue using zymography. It shows increased protease activity in tumor tissue compared to normal tissue sample. Therefore, tissue proteases could be used together with histopathological technique to discriminate the putative subgroup of patients within the same clinical category. Key words: Breast cancer, cathepsin K, cathepsin L, matrix metalloproteinase-9, matrix metalloproteinase-2 | en_US |
| dc.identifier.uri | http://etd.aau.edu.et/handle/123456789/2995 | |
| dc.language.iso | en | en_US |
| dc.publisher | Addis Ababa University | en_US |
| dc.subject | Breast cancer; Cathepsin K; Cathepsin L; Matrix metalloproteinase-9; Matrix metalloproteinase-2 | en_US |
| dc.title | Zymographic Detection and Clinical Correlations of Cysteine Cathepsin and Matrix Metalloproteinase in Human Breast Cancer Tissue | en_US |
| dc.type | Thesis | en_US |