Zymographic Detection And Clinical Correlations Of Cysteine Cathepsin And Matrix Metalloproteinase In Human Breast Cancer Tissue

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Breast cancer is the most frequent cause of cancer death in women in less developed countriesrnincluding Ethiopia. Cellular proteases thought to increase the likelihood of cancer invasion andrnmetastasis by degrading components of extracellular matrix. These proteases could be used asrntumor markers for early diagnosis, monitoring the prognosis or targeting therapeutics drugs.rnObjective: To investigate zymographic detection and clinical correlations of cysteine cathepsinsrnand matrix metalloproteinase in human breast cancer tissuernMethodology: Hospital based cross-sectional study was conducted from January 2015 to Junern2015. Thirty six women with breast cancer, who underwent mastectomy for first time werernrecruited from surgery department of Menelik II Hospital, Saint Paul’s Millennium MedicalrnCollege and Zewditu Memorial Hospital. Both tumor and normal tissues were harvested from thernsame patient within 10 minute after surgery. The tissue was processed and metastatic proteasernactivity was evaluated by measuring functional enzymatic activity of cathepsin K, cathepsin L, andrnmatrix metalloproteinase-2 and matrix metalloproteinase-9 using zymography and quantified byrndensitometry.rnResult: Normal and tumor tissue specimens were tested for functional cathepsins and matrixrnmetalloproteinases activities. Mean cathepsin K activity was significantly higher in tumor tissuernspecimens than the activity detected in normal breast tissue specimens (n = 36, p < 0.001), meanrncathepsin L activity was also significantly higher in tumor tissue than normal tissue specimens (nrn= 36, P < 0.001). Furthermore, mean matrix metalloproteinase-2 and -9 activities in tumor breastrntissue was significantly higher in tumor tissue than normal tissue (P < 0.05).rnConclusion: Our result showed different pattern of protease activity expression between normalrnand tumor tissue using zymography. It shows increased protease activity in tumor tissue comparedrnto normal tissue sample. Therefore, tissue proteases could be used together with histopathologicalrntechnique to discriminate the putative subgroup of patients within the same clinical category.rnKey words: Breast cancer, cathepsin K, cathepsin L, matrix metalloproteinase-9, matrixrnmetalloproteinase-2

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Zymographic Detection And Clinical Correlations Of Cysteine Cathepsin And Matrix Metalloproteinase In Human Breast Cancer Tissue

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