Secretion of matrix metalloproteinase-2 (72 kD gelatinase/type IV collagenase = gelatinase A) by malignant human glioma cell lines

Implications for the growth and cellular invasion of the extracellular matrix

Takao Nakagawa, Toshihiko Kubota, Masanori Kabuto, Noboru Fujimoto, Yasunori Okada

Research output: Contribution to journalArticle

55 Citations (Scopus)

Abstract

Human glioma cells (T98G and A172 cell lines) were cultured on various extracellular matrix (ECM) components including type I, IV and V collagens, fibronectin, laminin, and reconstituted basement membrane (Matrigel), and the role of matrix metalloproteinases (MMPs) in their growth and invasion was examined. T98G glioma cells grew well on these ECM components and invaded the reconstituted basement membrane. In contrast, A172 glioma cells showed growth inhibition on collagen types IV and V and Matrigel without invasion of the Matrigel. Gelatin zymography and enzyme immunoassays demonstrated that T98G glioma cells, but not A172 cells, secrete a large amount of matrix metallproteinase-2 (MMP-2, 72 kD gelatinase/type IV collagenase = gelatinase A), and this was confirmed by immunoblotting and immunohistochemistry. Of the two different tissue inhibitors of metalloproteinases (TIMP-1 and TIMP-2), T98G cells produced only TIMP-1 during culture on Matrigel, whereas A172 cells secreted both. Although both human recombinant TIMP-1 and TIMP-2 stimulated T98G cell growth slightly on Matrigel, the in vitro invasiveness was significantly reduced by only recombinant TIMP-2. These results suggest that MMP-2 plays an important role in the ECM invasion of T98G human glioma cells in vitro.

Original languageEnglish
Pages (from-to)13-24
Number of pages12
JournalJournal of Neuro-Oncology
Volume28
Issue number1
Publication statusPublished - 1996

Fingerprint

Gelatinases
Matrix Metalloproteinase 2
Collagenases
Glioma
Extracellular Matrix
Cell Line
Tissue Inhibitor of Metalloproteinase-1
Growth
Tissue Inhibitor of Metalloproteinase-2
Collagen Type V
Collagen Type IV
Basement Membrane
Laminin
Gelatin
Collagen Type I
Matrix Metalloproteinases
Immunoenzyme Techniques
Fibronectins
Immunoblotting
Immunohistochemistry

Keywords

  • Extracellular matrix
  • Invasion
  • Malignant glioma
  • Matrix metalloproteinases

ASJC Scopus subject areas

  • Cancer Research
  • Clinical Neurology
  • Oncology
  • Neuroscience(all)

Cite this

Secretion of matrix metalloproteinase-2 (72 kD gelatinase/type IV collagenase = gelatinase A) by malignant human glioma cell lines : Implications for the growth and cellular invasion of the extracellular matrix. / Nakagawa, Takao; Kubota, Toshihiko; Kabuto, Masanori; Fujimoto, Noboru; Okada, Yasunori.

In: Journal of Neuro-Oncology, Vol. 28, No. 1, 1996, p. 13-24.

Research output: Contribution to journalArticle

@article{ff2f5c194b4041f981cc15c74a982306,
title = "Secretion of matrix metalloproteinase-2 (72 kD gelatinase/type IV collagenase = gelatinase A) by malignant human glioma cell lines: Implications for the growth and cellular invasion of the extracellular matrix",
abstract = "Human glioma cells (T98G and A172 cell lines) were cultured on various extracellular matrix (ECM) components including type I, IV and V collagens, fibronectin, laminin, and reconstituted basement membrane (Matrigel), and the role of matrix metalloproteinases (MMPs) in their growth and invasion was examined. T98G glioma cells grew well on these ECM components and invaded the reconstituted basement membrane. In contrast, A172 glioma cells showed growth inhibition on collagen types IV and V and Matrigel without invasion of the Matrigel. Gelatin zymography and enzyme immunoassays demonstrated that T98G glioma cells, but not A172 cells, secrete a large amount of matrix metallproteinase-2 (MMP-2, 72 kD gelatinase/type IV collagenase = gelatinase A), and this was confirmed by immunoblotting and immunohistochemistry. Of the two different tissue inhibitors of metalloproteinases (TIMP-1 and TIMP-2), T98G cells produced only TIMP-1 during culture on Matrigel, whereas A172 cells secreted both. Although both human recombinant TIMP-1 and TIMP-2 stimulated T98G cell growth slightly on Matrigel, the in vitro invasiveness was significantly reduced by only recombinant TIMP-2. These results suggest that MMP-2 plays an important role in the ECM invasion of T98G human glioma cells in vitro.",
keywords = "Extracellular matrix, Invasion, Malignant glioma, Matrix metalloproteinases",
author = "Takao Nakagawa and Toshihiko Kubota and Masanori Kabuto and Noboru Fujimoto and Yasunori Okada",
year = "1996",
language = "English",
volume = "28",
pages = "13--24",
journal = "Journal of Neuro-Oncology",
issn = "0167-594X",
publisher = "Kluwer Academic Publishers",
number = "1",

}

TY - JOUR

T1 - Secretion of matrix metalloproteinase-2 (72 kD gelatinase/type IV collagenase = gelatinase A) by malignant human glioma cell lines

T2 - Implications for the growth and cellular invasion of the extracellular matrix

AU - Nakagawa, Takao

AU - Kubota, Toshihiko

AU - Kabuto, Masanori

AU - Fujimoto, Noboru

AU - Okada, Yasunori

PY - 1996

Y1 - 1996

N2 - Human glioma cells (T98G and A172 cell lines) were cultured on various extracellular matrix (ECM) components including type I, IV and V collagens, fibronectin, laminin, and reconstituted basement membrane (Matrigel), and the role of matrix metalloproteinases (MMPs) in their growth and invasion was examined. T98G glioma cells grew well on these ECM components and invaded the reconstituted basement membrane. In contrast, A172 glioma cells showed growth inhibition on collagen types IV and V and Matrigel without invasion of the Matrigel. Gelatin zymography and enzyme immunoassays demonstrated that T98G glioma cells, but not A172 cells, secrete a large amount of matrix metallproteinase-2 (MMP-2, 72 kD gelatinase/type IV collagenase = gelatinase A), and this was confirmed by immunoblotting and immunohistochemistry. Of the two different tissue inhibitors of metalloproteinases (TIMP-1 and TIMP-2), T98G cells produced only TIMP-1 during culture on Matrigel, whereas A172 cells secreted both. Although both human recombinant TIMP-1 and TIMP-2 stimulated T98G cell growth slightly on Matrigel, the in vitro invasiveness was significantly reduced by only recombinant TIMP-2. These results suggest that MMP-2 plays an important role in the ECM invasion of T98G human glioma cells in vitro.

AB - Human glioma cells (T98G and A172 cell lines) were cultured on various extracellular matrix (ECM) components including type I, IV and V collagens, fibronectin, laminin, and reconstituted basement membrane (Matrigel), and the role of matrix metalloproteinases (MMPs) in their growth and invasion was examined. T98G glioma cells grew well on these ECM components and invaded the reconstituted basement membrane. In contrast, A172 glioma cells showed growth inhibition on collagen types IV and V and Matrigel without invasion of the Matrigel. Gelatin zymography and enzyme immunoassays demonstrated that T98G glioma cells, but not A172 cells, secrete a large amount of matrix metallproteinase-2 (MMP-2, 72 kD gelatinase/type IV collagenase = gelatinase A), and this was confirmed by immunoblotting and immunohistochemistry. Of the two different tissue inhibitors of metalloproteinases (TIMP-1 and TIMP-2), T98G cells produced only TIMP-1 during culture on Matrigel, whereas A172 cells secreted both. Although both human recombinant TIMP-1 and TIMP-2 stimulated T98G cell growth slightly on Matrigel, the in vitro invasiveness was significantly reduced by only recombinant TIMP-2. These results suggest that MMP-2 plays an important role in the ECM invasion of T98G human glioma cells in vitro.

KW - Extracellular matrix

KW - Invasion

KW - Malignant glioma

KW - Matrix metalloproteinases

UR - http://www.scopus.com/inward/record.url?scp=0029932140&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0029932140&partnerID=8YFLogxK

M3 - Article

VL - 28

SP - 13

EP - 24

JO - Journal of Neuro-Oncology

JF - Journal of Neuro-Oncology

SN - 0167-594X

IS - 1

ER -