Cited by 201Protease and Inhibitor MechanismsGlioma Diagnosis and TreatmentPeptidase Inhibition and Analysis

The role of matrix metalloproteinases in glioma invasion

Open access
Nakada, Mitsutoshi·2003·Frontiers in Bioscience

Abstract

The matrix metalloproteinase (MMP) family plays an important role in the degradation of extracellular matrix (ECM) in various physiological and pathological conditions. Accumulated evidence has suggested that MMPs contribute to cancer cell invasion of the surrounding normal tissues and metastasis through the cell-surface ECM degradation. Strong correlations have been reported between elevated MMP levels and tumor cell invasiveness in human gliomas. Among them, attention has been focused on gelatinases (MMP-2 and MMP-9) and membrane type MMPs (MT-MMPs). We discuss here the biological significance of these MMPs in the glioblastoma invasion processes. A better understanding of cell-ECM interactions will help in developing therapeutic strategies to decrease the invasion of gliomas.

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  • Accumulated data suggest MMP levels and activities are significantly elevated in human gliomas, which contributes to glioma cell invasion, metastasis, and angiogenesis through cell surface ECM degradation.

    “Accumulated data suggested that MMP levels and activities are significantly elevated in human gliomas, which contributes to glioma cell invasion of the surrounding normal tissues, metastasis, and angiogenesis through cell surface ECM degradation (21, 45).”

    From MicroRNA 21 Promotes Glioma Invasion by Targeting Matrix Metalloproteinase Regulators (2008) · cites this paper as [45]

    The Abstract and §4.1 link elevated MMP levels in human gliomas to invasiveness, and describe ECM degradation and cell-surface activation. But the Abstract discusses metastasis in cancer generally, not specifically gliomas; §4.2 links MMP-9 to angiogenesis only tentatively and says its activity in invasive glioma tissue is unproven. The copy therefore does not establish significantly elevated MMP activities across human gliomas or the claimed glioma metastasis and angiogenesis mechanism. Page numbers were not supplied. (LLM, conf=0.88)

    Experimental — accuracy not yet measured
  • MMPs can degrade ECM components and therefore play important roles in mediating GBM tumor cell motility and invasion.

    “MMPs can degrade ECM components and therefore play important roles in mediating GBM tumor cell motility and invasion (45).”

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Research works printed but not linked: 2

  1. Rooprai, H. K. & McCormick, D.: Proteases and their inhibitors in human brain tumours: a review. Anticancer Res 17, 4151-4162 (1997)
  2. Dziegielewska, K. M., Saunders, N. R., Schejter, E. J., Zakut, H., Zevin-Sonkin, D., Zisling, R. & Soreq, H.: Synthesis of plasma proteins in fetal, adult, and neoplastic human brain tissue. Dev Biol 115, 93-104 (1986)

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Authors
Nakada, M.
Affiliations
Kanazawa University (JP)
Corresponding author
Nakada, Mitsutoshi
Venue
Frontiers in Bioscience
Publisher
IMR Press
Published
2003
Volume
8
Issue
5
Pages
e261-269
ISSN
  • 1093-4715 (ISSN-L)
  • 1093-9946
OpenAlex
W2049813036
Cited by
201
References
1
Citations by year
2026: 4 · 2025: 6 · 2024: 6 · 2023: 9 · 2022: 7 · 2021: 8 · 2020: 10 · 2019: 12 · 2018: 11 · 2017: 6 · 2016: 10 · 2015: 14 · 2014: 10 · 2013: 16 · 2012: 10
FWCI
0.51
Type
journal article
Language
en
Open access
Locations
  • Frontiers in bioscience (publishedVersion)
  • PubMed (publishedVersion)
Funders
Japan Society for the Promotion of Science (14770707)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
  • Health Sciences › Medicine › Genetics › Glioma Diagnosis and Treatment
  • Health Sciences › Medicine › Oncology › Peptidase Inhibition and Analysis
Keywords
matrix metalloproteinases, glioma invasion, glioblastoma, extracellular matrix degradation, gelatinase, MMP-2, MMP-9, membrane-type MMPs, cell-matrix interactions, tumor invasion, metastasis
MeSH terms
Animals, Glioma, Humans, Neoplasm Invasiveness, Matrix Metalloproteinases

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