[Matrix metalloproteinases and their tissue inhibitors in malignancies of the female genital tract].
Benjamin Piura, Alex Rabinovich, Mahmoud Huleihel
Abstract
Benjamin Piura, Alex Rabinovich, Mahmoud Huleihel
Abstract
The matrix metalloproteinases (MMPs) are a family of proteolytic enzymes, which are capable of degradation of the proteins composing the extracellular matrix and basement membrane. Their proteolytic activity depends on their binding to metal Zinc and is controlled by tissue inhibitors of MMP (TIMPs). Degradation of the extracellular matrix and basement membrane is an important component of the process of tumor invasiveness, progression, angiogenesis and metastatic spread. Since MMPs may serve as markers of tumor behavior and as predictors of survival and since synthetic inhibitors of MMP may have a place in the treatment of cancer, researching MMPs and their tissue inhibitors in malignant diseases has attracted growing attention. Studies on MMPs and their tissue inhibitors in malignancies of the female genital tract have shown the following: 1) In ovarian carcinoma and cervical carcinoma, over-expression of MMP-2 and MMP-9 is associated with invasiveness, metastatic spread and poor prognosis; 2) In endometrial carcinoma, MMP-7 (matrilysin) is the main MMP associated with invasiveness, metastatic spread and poor prognosis; 3) In cervical intra-epithelial neoplasia (CIN), measuring MMP-2 can assist in identifying high-risk for progression CIN I and CIN II; 4). In vulvar squamous cell carcinoma, over-expression of MMP-13 is associated with invasiveness, metastatic spread and poor prognosis. It is speculated that using synthetic drugs that inhibit MMPs in combination with conventional chemotherapy may contribute to the improvement of treatment results in cancer patients.
OpenAlex reports 6 citations for this work. Citation counts describe recorded attention and do not establish research quality.
A contribution statement is not available in the OpenAlex record.
Method details are not available in the OpenAlex metadata.
Findings are not separately available in the OpenAlex metadata.
Limitations are not available in the OpenAlex metadata.
Application details are not available in the OpenAlex metadata.
The matrix metalloproteinases (MMPs) are a family of proteolytic enzymes, which are capable of degradation of the proteins composing the extracellular matrix and basement membrane. Their proteolytic activity depends on their binding to metal Zinc and is controlled by tissue inhibitors of MMP (TIMPs). Degradation of the extracellular matrix and basement membrane is an important component of the process of tumor invasiveness, progression, angiogenesis and metastatic spread. Since MMPs may serve as markers of tumor behavior and as predictors of survival and since synthetic inhibitors of MMP may have a place in the treatment of cancer, researching MMPs and their tissue inhibitors in malignant diseases has attracted growing attention. Studies on MMPs and their tissue inhibitors in malignancies of the female genital tract have shown the following: 1) In ovarian carcinoma and cervical carcinoma, over-expression of MMP-2 and MMP-9 is associated with invasiveness, metastatic spread and poor prognosis; 2) In endometrial carcinoma, MMP-7 (matrilysin) is the main MMP associated with invasiveness, metastatic spread and poor prognosis; 3) In cervical intra-epithelial neoplasia (CIN), measuring MMP-2 can assist in identifying high-risk for progression CIN I and CIN II; 4). In vulvar squamous cell carcinoma, over-expression of MMP-13 is associated with invasiveness, metastatic spread and poor prognosis. It is speculated that using synthetic drugs that inhibit MMPs in combination with conventional chemotherapy may contribute to the improvement of treatment results in cancer patients.
Key concepts: Matrix metalloproteinase, Basement membrane, Medicine, Angiogenesis, Extracellular matrix, Proteolytic enzymes, Matrix metalloproteinase inhibitor, Cancer research