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Tytuł pozycji:

Metalloproteinases in Ovarian Cancer.

Tytuł:
Metalloproteinases in Ovarian Cancer.
Autorzy:
Carey P; Harper Cancer Research Institute, University of Notre Dame, South Bend, IN 46617, USA.; Department of Preprofessional Studies, University of Notre Dame, Notre Dame, IN 46556, USA.
Low E; Harper Cancer Research Institute, University of Notre Dame, South Bend, IN 46617, USA.; Department of Chemistry & Biochemistry, University of Notre Dame, Notre Dame, IN 46556, USA.
Harper E; Harper Cancer Research Institute, University of Notre Dame, South Bend, IN 46617, USA.; Department of Chemistry & Biochemistry, University of Notre Dame, Notre Dame, IN 46556, USA.; Integrated Biomedical Sciences Graduate Program, University of Notre Dame, Notre Dame, IN 46556, USA.
Stack MS; Harper Cancer Research Institute, University of Notre Dame, South Bend, IN 46617, USA.; Department of Chemistry & Biochemistry, University of Notre Dame, Notre Dame, IN 46556, USA.
Źródło:
International journal of molecular sciences [Int J Mol Sci] 2021 Mar 26; Vol. 22 (7). Date of Electronic Publication: 2021 Mar 26.
Typ publikacji:
Journal Article; Review
Język:
English
Imprint Name(s):
Original Publication: Basel, Switzerland : MDPI, [2000-
MeSH Terms:
Matrix Metalloproteinases/*metabolism
Ovarian Neoplasms/*metabolism
Animals ; Female ; Gene Expression Regulation, Neoplastic ; Humans ; Matrix Metalloproteinases/genetics ; Ovarian Neoplasms/genetics ; Ovarian Neoplasms/pathology ; Proteolysis ; Tumor Microenvironment
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Grant Information:
UO1CA236797 United States NH NIH HHS; RO1CA109545 United States NH NIH HHS; F99AG068527 United States NH NIH HHS; U01 CA236979 United States CA NCI NIH HHS; R01 CA109545 United States CA NCI NIH HHS
Contributed Indexing:
Keywords: extracellular matrix; matrix metalloproteinase; mesenchymal; mesothelial cells; ovarian cancer; peritoneum; proteases; proteolysis
Substance Nomenclature:
EC 3.4.24.- (Matrix Metalloproteinases)
Entry Date(s):
Date Created: 20210403 Date Completed: 20210420 Latest Revision: 20240331
Update Code:
20240331
PubMed Central ID:
PMC8036623
DOI:
10.3390/ijms22073403
PMID:
33810259
Czasopismo naukowe
Proteases play a crucial role in the progression and metastasis of ovarian cancer. Pericellular protein degradation and fragmentation along with remodeling of the extracellular matrix (ECM) is accomplished by numerous proteases that are present in the ovarian tumor microenvironment. Several proteolytic processes have been linked to cancer progression, particularly those facilitated by the matrix metalloproteinase (MMP) family. These proteases have been linked to enhanced migratory ability, extracellular matrix breakdown, and development of support systems for tumors. Several studies have reported the direct involvement of MMPs with ovarian cancer, as well as their mechanisms of action in the tumor microenvironment. MMPs play a key role in upregulating transcription factors, as well as the breakdown of structural proteins like collagen. Proteolytic mechanisms have been shown to enhance the ability of ovarian cancer cells to migrate and adhere to secondary sites allowing for efficient metastasis. Furthermore, angiogenesis for tumor growth and development of metastatic implants is influenced by upregulation of certain proteases, including MMPs. While proteases are produced normally in vivo, they can be upregulated by cancer-associated mutations, tumor-microenvironment interaction, stress-induced catecholamine production, and age-related pathologies. This review outlines the important role of proteases throughout ovarian cancer progression and metastasis.

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