Metalloproteinases in Ovarian Cancer.

extracellular matrix matrix metalloproteinase mesenchymal mesothelial cells ovarian cancer peritoneum proteases proteolysis

Journal

International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791

Informations de publication

Date de publication:
26 Mar 2021
Historique:
received: 17 02 2021
revised: 21 03 2021
accepted: 25 03 2021
entrez: 3 4 2021
pubmed: 4 4 2021
medline: 21 4 2021
Statut: epublish

Résumé

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.

Identifiants

pubmed: 33810259
pii: ijms22073403
doi: 10.3390/ijms22073403
pmc: PMC8036623
pii:
doi:

Substances chimiques

Matrix Metalloproteinases EC 3.4.24.-

Types de publication

Journal Article Review

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : NIH HHS
ID : UO1CA236797
Pays : United States
Organisme : NIH HHS
ID : RO1CA109545
Pays : United States
Organisme : NIH HHS
ID : F99AG068527
Pays : United States
Organisme : NCI NIH HHS
ID : U01 CA236979
Pays : United States
Organisme : NCI NIH HHS
ID : R01 CA109545
Pays : United States

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Auteurs

Preston 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.

Ethan 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.

Elizabeth 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.

M Sharon 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.

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