Invasion of brain tissue by primary glioma: Evidence for the involvement of urokinase-type plasminogen activator as an activator of type iv collagenase

Reith, A.; Rucklidge, Garry J.

doi:10.1016/s0006-291x(05)80814-9

Cited by 55 publications

(28 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…38 Levels of gelatinase A mRNA production correlate with protein activity and expression. 35 Gelatinase A activity as measured by zymography was highest in those cell lines that were most invasive as measured by the Matrigel invasion assay.…”

Section: Abe and Colleaguesmentioning

confidence: 99%

Cytostatic Agents in the Management of Malignant Gliomas

Mikkelsen¹

1998

Cancer Control

View full text Add to dashboard Cite

show abstract

Section: Abe and Colleaguesmentioning

confidence: 99%

Cytostatic Agents in the Management of Malignant Gliomas

Mikkelsen¹

1998

Cancer Control

View full text Add to dashboard Cite

show abstract

“…Matrix metalloproteinases are known to play a crucial role in the invasive nature of a number of neoplasms (Birkedal-Hansen et al, 1993), including malignant gliomas (Reict and Rucklidge, 1992). This family of zinc-dependent endopeptidases includes interstitial collagenases (MMP-l and -8), type IV collagenases/gelatinases (MMP-2 and -9), stromelysins (MMP-3 and -10) and matrilysin (MMP-7) (Nakano et al, 1995).…”

Section: Invasion Of Gliomas and Matrix Metalloproteinasesmentioning

confidence: 99%

“…Degradation of the extracellular matrix is mediated by tumour cell-secreted proteolytic enzymes (Pedersen et al, 1994), such as matrix metalloproteinases (MMPs) (Nakano et al, 1995). Several authors have demonstrated the importance of MMPs in glioma cell invasion (Reict and Rucklidge, 1992;Abe et al, 1994) and have elucidated the structure of the MMP gene family (Birkedal-Hansen et al, 1993). However, to our knowledge, no studies have focused on the modulation of MMP activity by antimicrotubule agents such as EMP.…”

mentioning

confidence: 99%

Suppression of matrix metalloproteinase-2-mediated cell invasion in U87MG, human glioma cells by anti-microtubule agent: in vitro study

Yoshida

Piepmeier²,

Henriksson³

et al. 1998

Br J Cancer

View full text Add to dashboard Cite

Summary Because microtubules are important components of cell motility and intracellular transport, it is reasonable to propose that the depolymerizing effect of an antimicrotubule agent, estramustine, on glioma microtubules would modulate cell invasiveness. To determine whether matrix metalloproteinases, key factors in cell invasion, are affected by exposure to estramustine, a cell proliferation assay, a zymogram, a collagenolysis assay and a haptoinvasion assay were used in this study. The zymogram revealed that an activated (62 kDa) form of matrix metalloproteinase-2 diminished with increasing estramustine concentrations. The collagenolysis assay demonstrated approximately 2.5-to 21-fold lower rates of enzymatic activity suppressed by estramustine in a dose-dependent manner at estramustine concentrations of 1, 5, and 1 0 gM, compared with the control group. On the haptoinvasion assay, no statistically significant difference was seen in the 0.5 gM estramustine group, whereas 1-10 gM estramustine groups revealed significant suppression of invasion from 6 to 24 h in a dose-dependent manner. The results suggest that estramustine suppresses the invasion of U87MG cells in vitro using the decreasing available matrix metalloproteinase-2, an effect caused by the disassembly of microtubules. Suppression of the infiltrative capacity of malignant glioma cells could be of significant value in the treatment of this disease.

show abstract

“…Although cell-associated u-PA appears to be required for the migration of numerous types of cells [8] including U-251 cells [10], our observations coupled with the report of Sitrin and co-workers [29] indicate that the secretion of high levels of u-PA from U-251 cells results in a net plasminogen activation activity in the milieu surrounding these cells. Because u-PA is able to directly activate latent collagenase [37], Reith and Rucklidge [37] have proposed a cyclic model in which these two enzymes could initiate cellular damage, disruption of blood brain barrier, and subsequent release of plasminogen from the damaged vessel. Thus, high levels of rapidly releasable active PAI-1 might be important as a local control mechanism to prevent proteases, which are secreted by the tumor cells themselves, from excessively degrading the surrounding ECM and causing necrosis of the tumors.…”

Section: Secretagogue-induced Secretion Of Pal1 Jrom U-251 Cellsmentioning

confidence: 99%

Human glioma U‐251 cells contain type 1 plasminogen activator inhibitor in a rapidly releasable form

et al. 1996

View full text Add to dashboard Cite

Because recent information suggests that the localized deposition of protease inhibitors is one mechanism by which cells regulate pericellular proteolysis during tissue invasion, the distribution of type 1 plasminogen activator inhibitor (PAl-l) associated with the invasive human glioma cell line U-251 was investigated. Direct and reverse fibrin zymography indicated the presence of urokinase-like plasminogen activator (u-PA) and PAI-1 in U-251 conditioned media and cell lysates. PAI-I antigen was detected immunologically in cytoplasmic granules present within cellular processes of U-251 cells and these organelles could be isolated on Percoll density gradients in a high density band. In contrast, u-PA activity and another secreted protein, amyloid [5-protein precursor, were only present in the low density region of the gradients. Functional analysis of PAI-1 in the granules contained within the high density fractions revealed the presence of active PAl-1. Incubation of U-251 cells with the secretagogue, 8-bromoadenosine 3' :5'-cyclic monophosphate, resulted in a 3-fold increase in the release of PAI-1 in the media conditioned by these cells. These data suggest that the human glioma cell line U-251 contains PAI-I in a rapidly releasable form, which may provide another mechanism by which these tumors could regulate proteolytic activity in a localized manner.

show abstract

Invasion of brain tissue by primary glioma: Evidence for the involvement of urokinase-type plasminogen activator as an activator of type iv collagenase

Cited by 55 publications

References 13 publications

Cytostatic Agents in the Management of Malignant Gliomas

Cytostatic Agents in the Management of Malignant Gliomas

Suppression of matrix metalloproteinase-2-mediated cell invasion in U87MG, human glioma cells by anti-microtubule agent: in vitro study

Human glioma U‐251 cells contain type 1 plasminogen activator inhibitor in a rapidly releasable form

Contact Info

Product

Resources

About