Autocrine regulation of matrix metalloproteinase-9 gene expression and secretion by tumor necrosis factor-α (TNF-α) in NB4 leukemic cells: specific involvement of TNF receptor type 1

Ismair, MG; Ries, Christian; Lottspeich, F.; Zang, Chuanbing; Kolb, H. J.; Pe, Petrides

doi:10.1038/sj.leu.2401042

Cited by 34 publications

(25 citation statements)

References 20 publications

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“…In our study, we used THP-1 monocytic cells, characterized by constitutive release of MMP-9, as a model system to examine the role of MAPK in MMP-9 gene expression. We found that continuous secretion of MMP-9 in these cells was mediated by autocrine TNF-a stimulation via TNF-R1, consistent with previous results obtained in HL-60 and NB4 leukemic cells (Ries et al, 1994;Ismair et al, 1998). The importance of released TNF-a in this context was also shown by others using the unspecific metalloproteinase inhibitor Marimastat (Robinson et al, 2002).…”

Section: Discussionsupporting

confidence: 92%

“…As we have demonstrated here, inhibition of the ERK1/2 pathway in THP-1 leukemic cells caused a marked decrease in continuous MMP-9 production, which was maintained by endogenous TNF-a. Likewise, we investigated HL-60 and NB4 leukemic cells, which are also known to secrete MMP-9, by autocrine stimulation with TNF-a (Ries et al, 1994;Ismair et al, 1998). In agreement with our findings in THP-1 cells, blockage of MEK1/2 activity also downregulated constitutive MMP-9 production in both HL-60 and NB4 cells (data not shown in the results section to avoid redundancy).…”

Section: Discussionsupporting

confidence: 85%

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Modulation of autocrine TNF-α-stimulated matrix metalloproteinase 9 (MMP-9) expression by mitogen-activated protein kinases in THP-1 monocytic cells

Heidinger

Kolb

Krell

et al. 2006

Biological Chemistry

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Matrix metalloproteinase 9 (MMP-9) is implicated in various physiological processes by its ability to degrade the extracellular matrix (ECM) and process multiple regulatory proteins. Normally, MMP-9 expression is tightly controlled in cells. Sustained or enhanced MMP-9 secretion, however, has been demonstrated to contribute to the pathophysiology of numerous diseases, including arthritis and tumor progression, rendering this enzyme a major target for clinical interventions. Here we show that constitutive MMP-9 secretion was abrogated in THP-1 monocytic leukemia cells by addition of neutralizing antibodies against tumor necrosis factor a (TNF-a) or TNF receptor type 1 (TNF-R1), as well as by inhibition of TNFa converting enzyme (TACE). This indicates that MMP-9 production in these cells is maintained by autocrine stimulation, with TNF-a acting via TNF-R1. To investigate the intracellular signaling routes involved in MMP-9 gene transcription, cells were treated with different inhibitors of major mitogen-activated protein kinase (MAPK) pathways. Interruption of the extracellular signalregulated kinase pathway 1/2 (ERK1/2) using PD98059 significantly downregulated constitutive MMP-9 release. In contrast, blockage of p38 kinase activity by addition of SB203580 or SB202190, as well as inhibition of cJun N-terminal kinase (JNK) using L-JNK-I1, clearly augmented MMP-9 expression and secretion by an upregulation of ERK1/2 phosphorylation. Moreover, exogenously added TNF-a augmented MMP-9 synthesis and secretion in THP-1 cells via enhancement of ERK1/ 2 activity. Taken together, our results indicate that ERK1/ 2 activity plays a pivotal role in TNF-a-induced MMP-9 production and demonstrate its negative modulation by p38 and JNK activity. These findings suggest ERK1/2 rather than p38 and JNK as a reasonable target to specifically block MMP-9 expression using MAPK inhibitors in therapeutic applications.

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Section: Discussionsupporting

confidence: 92%

Section: Discussionsupporting

confidence: 85%

Modulation of autocrine TNF-α-stimulated matrix metalloproteinase 9 (MMP-9) expression by mitogen-activated protein kinases in THP-1 monocytic cells

Heidinger

Kolb

Krell

et al. 2006

Biological Chemistry

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“…MMP-9 is typically expressed at low levels or not at all in tumor cells, but its expression can be rapidly induced by a variety of cytokines (Huang et al, 1998;Ismair et al, 1998;Kondapaka et al, 1997), phorbolester (Toth et al, 1997) and cell -cell interactions (Aoudjit et al, 1998). Moreover, MMP-9 has been widely implicated in tumor invasion and metastasis (Bernhard et al, 1990(Bernhard et al, , 1994, and in the promotion of tumor cell survival (Yu and Stamenkovic, 1999;Yu and Stamenkovic, 2000).…”

Section: Resultsmentioning

confidence: 99%

Matrix metalloproteinase 9 (MMP-9/gelatinase B) proteolytically cleaves ICAM-1 and participates in tumor cell resistance to natural killer cell-mediated cytotoxicity

et al. 2002

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Shedding of intercellular adhesion molecule 1 (ICAM-1) is believed to play a role in tumor cell resistance to cellmediated cytotoxicity. However, the mechanism whereby ICAM-1 is shed from the surface of tumor cells remains unclear. In this study, we have addressed the possibility that matrix metalloproteinases are implicated in ICAM-1 shedding. Our observations suggest a functional relationship between ICAM-1 and matrix metalloproteinase 9 (MMP-9) whereby ICAM-1 provides a cell surface docking mechanism for proMMP-9, which, upon activation, proteolytically cleaves the extracellular domain of ICAM-1 leading to its release from the cell surface. MMP-9-dependent shedding of ICAM-1 is found to augment tumor cell resistance to natural killer (NK) cell-mediated cytotoxicity. Taken together, our observations propose a mechanism for ICAM-1 shedding from the cell surface and provide support for MMP involvement in tumor cell evasion of immune surveillance.

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“…Variable expression levels of MMP-2 and -9 could be detected in conditioned media of myeloid cell lines [177][178][179][180][181][182][183]. The capability of penetrating matrigel in an invasion assay by KG-1 could be partially blocked by TIMP-2 and an MMP-2 antibody, but not by an MMP-9 antibody, indicating that in vitro invasion largely depends on MMP-2 activity [181].…”

Section: Acute Myeloid Leukemia (Aml)mentioning

confidence: 99%

The possible role of matrix metalloproteinase (MMP)-2 and MMP-9 in cancer, e.g. acute leukemia

Klein

Vellenga

Fraaije

et al. 2004

Critical Reviews in Oncology/Hematology

309

170

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Autocrine regulation of matrix metalloproteinase-9 gene expression and secretion by tumor necrosis factor-α (TNF-α) in NB4 leukemic cells: specific involvement of TNF receptor type 1

Cited by 34 publications

References 20 publications

Modulation of autocrine TNF-α-stimulated matrix metalloproteinase 9 (MMP-9) expression by mitogen-activated protein kinases in THP-1 monocytic cells

Modulation of autocrine TNF-α-stimulated matrix metalloproteinase 9 (MMP-9) expression by mitogen-activated protein kinases in THP-1 monocytic cells

Matrix metalloproteinase 9 (MMP-9/gelatinase B) proteolytically cleaves ICAM-1 and participates in tumor cell resistance to natural killer cell-mediated cytotoxicity

The possible role of matrix metalloproteinase (MMP)-2 and MMP-9 in cancer, e.g. acute leukemia

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