TNF-α increases human melanoma cell invasion and migration in vitro: the role of proteolytic enzymes

Katerinaki, E; Evans, Gareth S; Lorigan, Paul; MacNeil, Sheila

doi:10.1038/sj.bjc.6601257

Cited by 75 publications

(62 citation statements)

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“…We also found TNF-a to cause a modest increase in proteolytic activity, which could be blocked effectively using a 2 macroglobulin (Katerinaki et al, 2003), but with no concomitant increase in matrix metalloproteinase 2 or 9 activation or expression. However, the above studies did not consider whether melanoma invasion through fibronectin was attributable specifically to an increase in cell migration or to an increase in invasion.…”

mentioning

confidence: 61%

“…In vitro and in vivo invasion may involve both increased migration and increased proteolytic breakdown of the matrix. Thus, we recently found that while TNF-a did not cause an obvious upregulation of proteolytic activity in HBL cells, the introduction of a broadspectrum protease inhibitor (a 2 macroglobulin) was able to block TNF-a-stimulated cell invasion and cell migration (Katerinaki et al, 2003). In the current study, we compared two methods for measuring cell migration, both based on introducing a 'scratch' to a cultured monolayer of cells (adapted from a method previously reported for keratinocytes (Cha et al, 1996)).…”

Section: Discussionmentioning

confidence: 99%

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Melanoma cell migration is upregulated by tumour necrosis factor-α and suppressed by α-melanocyte-stimulating hormone

et al. 2004

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We reported recently that the inflammatory cytokine tumour necrosis factor a (TNF-a) can upregulate integrin expression, cell attachment and invasion of cells through fibronectin in a human melanoma cell line (HBL). Furthermore, the actions of TNF-a were suppressed by the addition of an anti-inflammatory peptide a-melanocyte-stimulating hormone (a-MSH). In the current study, we extend this work investigating to what extent TNF-a might stimulate melanoma invasion by promoting cell migration and whether a-MSH is also inhibitory. Two human melanoma cell lines were examined in vitro (HBL and C8161) using a scratch migration assay. Analysis using either time-lapse video microscopy or imaging software analysis of migrating 'fronts' of cells revealed that C8161 cells migrated more rapidly than HBL cells. However, when cells were stimulated with TNF-a both cell types responded with a significant increase in migration distance over a 16 -26 h incubation time. a-Melanocyte-stimulating hormone had an inhibitory effect on TNF-astimulated migration for HBL cells, completely blocking migration at 10 À9 M. In contrast, C8161 cells did not respond to a-MSH (as these cells have a loss-of-function melanocortin-1 receptor). However, stable transfection of C8161 cells with the wild-type melanocortin-1 receptor produced cells whose migration was significantly inhibited by a-MSH. In addition, the use of a neutralising antibody to the b 1 -integrin subunit significantly reduced migration in both cell types. This data therefore supports an inflammatory environment promoting melanoma cell migration, and in addition shows that a-MSH can inhibit inflammatory stimulated migration. The data also support a fundamental role of the b 1 -integrin receptor in melanoma cell migration.

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confidence: 61%

Section: Discussionmentioning

confidence: 99%

Melanoma cell migration is upregulated by tumour necrosis factor-α and suppressed by α-melanocyte-stimulating hormone

et al. 2004

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“…IFNÁ may also promote metastatic diffusion of melanoma cells through a down regulation of the processing of tumor antigens (20)(21)(22). TNF· promoted the invasiveness of human melanoma cells through the stimulation of the expression of integrin receptors (23), or cell-bound degradative enzymes (24).…”

Section: Introductionmentioning

confidence: 99%

Cytokine-dependent invasiveness in B16 murine melanoma cells: Role of uPA system and MMP-9

et al. 2006

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Abstract. Proteases are crucial for the spread of cancer cells from a primary tumor to the site of secondary growth. This study examined the ability of IFNÁ and TNF· to stimulate a better invasiveness in B16 murine melanoma cells, and investigated whether this enhanced ability was related to a higher expression of protease activities, such as urokinase plasminogen activator (uPA) and its receptor (uPAR), and matrix metalloproteinases 2 and 9 (MMP-2, MMP-9). We found that murine melanoma cells enhanced their lungcolonizing potential in vivo and invasiveness through Matrigel-coated filters upon costimulation with IFNÁ and TNF·; neither IFNÁ nor TNF· alone, at the dose used in the experiments, was able to elicit a change in the invasive/ metastatic efficiency of melanoma cells. The invasive phenotype of murine melanoma cells stimulated with IFNÁ and TNF· was characterized by an enhanced uPA/uPAR and MMP-9 expression: TNF· promoted MMP-9 mRNA expression and pro-MMP-9 protein secretion, and the costimulation with IFNÁ and TNF· was required to potentiate the expression of mRNA and protein for uPAR, and to induce a redistribution of uPA from the soluble to the cell bodyassociated form. Both monoclonal antibodies, anti-uPAR and anti-MMP-9, caused a significant reduction of invasiveness in IFNÁ/TNF·-stimulated melanoma cells. These results indicate that invasiveness in B16 murine melanoma cells can be regulated in a cytokine-specific fashion and is dependent on the synergism between the uPA/uPAR system and MMP-9.

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“…Reports have proved that TNF-a enhances metastatic properties in many cancer cell lines. [34][35][36][37] The in vitro TNF-a stimulation model we have recently developed provides a new way to characterize the importance of signaling molecules in cancer cells for cytokine-induced metastasis. Several signaling pathways related to enhanced metastasis have been studied; however, the contribution of TAK1 to tumor metastasis has never been investigated.…”

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confidence: 99%

TAK1‐mediated stress signaling pathways are essential for TNF‐α‐promoted pulmonary metastasis of murine colon cancer cells

Choo

Sakurai

Koizumi

et al. 2006

Intl Journal of Cancer

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We have recently established a TNF-a-promoted metastasis model, in which the ability to metastasize to the lung was enhanced by stimulation of cultured colon 26 cells with TNF-a before intravenous inoculation. To investigate intracellular events in metastatic cascades of TNF-a-treated cancer cells, we have focused on the stress signaling pathways to c-Jun N-terminal kinase (JNK) and p38. Treatment with a specific inhibitor, SP600125 or SB203580, in vitro suppressed TNF-a-induced migration and pulmonary metastasis. Activation of endogenous TAK1, a mitogen-activated protein kinase (MAP3K) regulating the JNK and p38 MAPK pathways, was induced rapidly by TNF-a, and co-transfection of TAK1 with its activator protein TAB1 stimulated activation of JNK and p38 MAPKs, which led to activation of the transcription factor AP-1. The activation of stress signaling pathways by TAK1 resulted in enhanced migration to fibronectin in vitro and metastasis to the lung in vivo without affecting cell proliferation in vitro and tumor growth in vivo. Moreover, knockdown of endogenous TAK1 using small interfering RNA (siRNA) suppressed the TNF-a-induced JNK/p38 activation, migration and pulmonary metastasis. These results indicate that TAK1-mediated stress signaling pathways in cancer cells are essential for TNF-a-promoted metastasis to the lung. ' 2005 Wiley-Liss, Inc.Key words: TAK1; TNF-a; metastasis; inflammation The theory of a functional relationship between inflammation and cancer is not new. Two millennia ago, the Greek doctor Galen noticed a link between inflammation and cancer, and Virchow hypothesized in 1863 that the origin of cancer was a site of chronic inflammation.1-3 Over the past 10 years, the relationship between inflammation and cancer has become more widely accepted. Inflammatory cells and cytokines found in tumors are more likely to contribute to tumor growth, progression and immunosuppression than they are to mount an effective host anti-tumor response.1-5 Therefore, inflammation is responsible for the development of cancers, in organs such as the liver, esophagus, stomach, large intestine and urinary bladder. The proinflammatory cytokine tumor necrosis factor-a (TNF-a) is a key mediator in inflammation. Despite the name, TNF-a is important in early events in tumorigenesis, regulating a cascade of cytokines, chemokines, adhesion molecules, extracellular proteases and proangiogenic molecules. 1,6 In fact, it has been demonstrated that TNF-a expression is increased in the serum of cancer patients.7,8 TNF-a also plays a critical role in tumor progression. Injection of TNF-a in mice results in an enhancement of metastasis accompanied by tumor cell extravasation with increased expression of adhesion molecules, in which the action of TNF-a is not distinguishable between host cells or cancer cells.9,10 Kitakata et al. demonstrated that the action of TNF-a toward host cells is essential for metastasis using TNF-RI-deficient mice. 11 We have recently established a TNF-a-promoted metastasis model, in which the ability to me...

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TNF-α increases human melanoma cell invasion and migration in vitro: the role of proteolytic enzymes

Cited by 75 publications

References 26 publications

Melanoma cell migration is upregulated by tumour necrosis factor-α and suppressed by α-melanocyte-stimulating hormone

Melanoma cell migration is upregulated by tumour necrosis factor-α and suppressed by α-melanocyte-stimulating hormone

Cytokine-dependent invasiveness in B16 murine melanoma cells: Role of uPA system and MMP-9

TAK1‐mediated stress signaling pathways are essential for TNF‐α‐promoted pulmonary metastasis of murine colon cancer cells

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