Cysteine Cathepsins and Matrix Metalloproteases Among Breast Cancer Patients
Solomon Tsegaye,1 Mohammed Mehdi,2 Wajana L Labisso,3 Daniel Seifu Melka2 1Department of Biochemistry, College of Health Sciences, Assela University, Addis Ababa, Ethiopia; 2Department of Biochemistry, College of Health Sciences, Addis Ababa University, Addis Ababa, Ethiopia; 3Department of Patholog...
Guardado en:
Autores principales: | , , , |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Dove Medical Press
2021
|
Materias: | |
Acceso en línea: | https://doaj.org/article/dcaeae46394c4bee96ca2b6eed61ead3 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
id |
oai:doaj.org-article:dcaeae46394c4bee96ca2b6eed61ead3 |
---|---|
record_format |
dspace |
spelling |
oai:doaj.org-article:dcaeae46394c4bee96ca2b6eed61ead32021-12-02T14:41:57ZCysteine Cathepsins and Matrix Metalloproteases Among Breast Cancer Patients1179-1314https://doaj.org/article/dcaeae46394c4bee96ca2b6eed61ead32021-05-01T00:00:00Zhttps://www.dovepress.com/cysteine-cathepsins-and-matrix-metalloproteases-among-breast-cancer-pa-peer-reviewed-fulltext-article-BCTThttps://doaj.org/toc/1179-1314Solomon Tsegaye,1 Mohammed Mehdi,2 Wajana L Labisso,3 Daniel Seifu Melka2 1Department of Biochemistry, College of Health Sciences, Assela University, Addis Ababa, Ethiopia; 2Department of Biochemistry, College of Health Sciences, Addis Ababa University, Addis Ababa, Ethiopia; 3Department of Pathology, College of Health Sciences, Addis Ababa University, Addis Ababa, EthiopiaCorrespondence: Mohammed MehdiDepartment of Biochemistry, College of Health Sciences, Addis Ababa University, P.o.box: 9086, Addis Ababa, EthiopiaTel +251910066838Email mohammed.mehdi@aau.edu.etBackground: Cellular proteases are thought to increase the likelihood of cancer cell infiltration and metastasis by degrading constituents of the extracellular matrix (ECM). Measuring activities of these proteases may be used as tumor markers for early diagnosis, prognosis, and as a possible target for treatment plan.Objective: The aim of the current study is to evaluate cysteine cathepsins (CTSK and CTSL) and matrix metalloproteases-2 (MMP-2) and 9 (MMP-9) activities in human breast tumor tissue.Methods: A comparative cross-sectional study plan was devised to study the enzymatic activities ofCTSK and CTSL andMMP-2 and MMP-9 via zymographic detection method. Sites of tissue sample collection were St Paul’s Millennium Medical College, Menelik II Hospital and Zewditu Memorial Hospital, Addis Ababa, Ethiopia. A total of 36 breast cancer patients were recruited and tissue samples were collected for the study.Results: Activities of CTSK and CTSL were significantly elevated in cancerous tissue than the adjacent normal non-cancerous breast tissue of the same patients (n = 36, p ≤ 0.05). Also, activities ofMMP-2 and MMP-9 were increased significantly in tumor tissues than normal tissues (n = 36, P ≤ 0.05).Conclusion: It is found that there are different patterns of protease enzymatic activity expression between normal and tumor tissue using zymography. Compared with normal tissue samples, the protease enzymatic activity in cancerous tissue is higher. Thus, tissue proteases can be used in conjunction with histological techniques to identify patients in the same clinical group.Keywords: breast cancer, cathepsin K; CTSK, cathepsin L; CTSL, matrix metalloprotinease-9; MMP-9, matrix metalloprotinease-2; MMP-2Tsegaye SMehdi MLako WLMelka DSDove Medical Pressarticlebreast cancercathepsin kcathepsin lmmp-9mmp-2Neoplasms. Tumors. Oncology. Including cancer and carcinogensRC254-282ENBreast Cancer: Targets and Therapy, Vol Volume 13, Pp 271-283 (2021) |
institution |
DOAJ |
collection |
DOAJ |
language |
EN |
topic |
breast cancer cathepsin k cathepsin l mmp-9 mmp-2 Neoplasms. Tumors. Oncology. Including cancer and carcinogens RC254-282 |
spellingShingle |
breast cancer cathepsin k cathepsin l mmp-9 mmp-2 Neoplasms. Tumors. Oncology. Including cancer and carcinogens RC254-282 Tsegaye S Mehdi M Lako WL Melka DS Cysteine Cathepsins and Matrix Metalloproteases Among Breast Cancer Patients |
description |
Solomon Tsegaye,1 Mohammed Mehdi,2 Wajana L Labisso,3 Daniel Seifu Melka2 1Department of Biochemistry, College of Health Sciences, Assela University, Addis Ababa, Ethiopia; 2Department of Biochemistry, College of Health Sciences, Addis Ababa University, Addis Ababa, Ethiopia; 3Department of Pathology, College of Health Sciences, Addis Ababa University, Addis Ababa, EthiopiaCorrespondence: Mohammed MehdiDepartment of Biochemistry, College of Health Sciences, Addis Ababa University, P.o.box: 9086, Addis Ababa, EthiopiaTel +251910066838Email mohammed.mehdi@aau.edu.etBackground: Cellular proteases are thought to increase the likelihood of cancer cell infiltration and metastasis by degrading constituents of the extracellular matrix (ECM). Measuring activities of these proteases may be used as tumor markers for early diagnosis, prognosis, and as a possible target for treatment plan.Objective: The aim of the current study is to evaluate cysteine cathepsins (CTSK and CTSL) and matrix metalloproteases-2 (MMP-2) and 9 (MMP-9) activities in human breast tumor tissue.Methods: A comparative cross-sectional study plan was devised to study the enzymatic activities ofCTSK and CTSL andMMP-2 and MMP-9 via zymographic detection method. Sites of tissue sample collection were St Paul’s Millennium Medical College, Menelik II Hospital and Zewditu Memorial Hospital, Addis Ababa, Ethiopia. A total of 36 breast cancer patients were recruited and tissue samples were collected for the study.Results: Activities of CTSK and CTSL were significantly elevated in cancerous tissue than the adjacent normal non-cancerous breast tissue of the same patients (n = 36, p ≤ 0.05). Also, activities ofMMP-2 and MMP-9 were increased significantly in tumor tissues than normal tissues (n = 36, P ≤ 0.05).Conclusion: It is found that there are different patterns of protease enzymatic activity expression between normal and tumor tissue using zymography. Compared with normal tissue samples, the protease enzymatic activity in cancerous tissue is higher. Thus, tissue proteases can be used in conjunction with histological techniques to identify patients in the same clinical group.Keywords: breast cancer, cathepsin K; CTSK, cathepsin L; CTSL, matrix metalloprotinease-9; MMP-9, matrix metalloprotinease-2; MMP-2 |
format |
article |
author |
Tsegaye S Mehdi M Lako WL Melka DS |
author_facet |
Tsegaye S Mehdi M Lako WL Melka DS |
author_sort |
Tsegaye S |
title |
Cysteine Cathepsins and Matrix Metalloproteases Among Breast Cancer Patients |
title_short |
Cysteine Cathepsins and Matrix Metalloproteases Among Breast Cancer Patients |
title_full |
Cysteine Cathepsins and Matrix Metalloproteases Among Breast Cancer Patients |
title_fullStr |
Cysteine Cathepsins and Matrix Metalloproteases Among Breast Cancer Patients |
title_full_unstemmed |
Cysteine Cathepsins and Matrix Metalloproteases Among Breast Cancer Patients |
title_sort |
cysteine cathepsins and matrix metalloproteases among breast cancer patients |
publisher |
Dove Medical Press |
publishDate |
2021 |
url |
https://doaj.org/article/dcaeae46394c4bee96ca2b6eed61ead3 |
work_keys_str_mv |
AT tsegayes cysteinecathepsinsandmatrixmetalloproteasesamongbreastcancerpatients AT mehdim cysteinecathepsinsandmatrixmetalloproteasesamongbreastcancerpatients AT lakowl cysteinecathepsinsandmatrixmetalloproteasesamongbreastcancerpatients AT melkads cysteinecathepsinsandmatrixmetalloproteasesamongbreastcancerpatients |
_version_ |
1718389840798547968 |