Tumor Necrosis Factor-α Augments Matrix Metalloproteinase-9 Production in Skeletal Muscle Cells through the Activation of Transforming Growth Factor-β-activated Kinase 1 (TAK1)-dependent Signaling Pathway

Srivastava, Apurva K.; Qin, Xu‐Jie; Wedhas, Nia; Arnush, Marc; Linkhart, Thomas A.; Chadwick, Robert B.; Kumar, Ashok

doi:10.1074/jbc.m705329200

Cited by 57 publications

(54 citation statements)

References 63 publications

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“…However, in a similar study involving exercise with restricted blood flow, our laboratory observed that phosphorylation of p38 increased after acute exercise, and that restriction of blood flow had no further effect. p38 regulates MMP-9 transcription in various cell lines, including C 2 C 12 cells (25,30). This indirect evidence constitutes further proof against metabolic stress as a major regulatory stimulus responsible for the exercise-induced increase in MMP-9 observed in the present study.…”

Section: Discussionsupporting

confidence: 61%

Endurance exercise activates matrix metalloproteinases in human skeletal muscle

Rullman¹,

Norrbom²,

Strömberg³

et al. 2009

Journal of Applied Physiology

105

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Section: Discussionsupporting

confidence: 61%

Endurance exercise activates matrix metalloproteinases in human skeletal muscle

Rullman¹,

Norrbom²,

Strömberg³

et al. 2009

Journal of Applied Physiology

105

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“…Although we can exclude the Sp1, HBS, and TBE regulatory elements to be required for CNK1-dependent MT1-MMP promoter activation, there may be additional uncharacterized CNK1-responsive regulatory sites in the entire promoter. MMP-9 expression is driven by NF-κB-and JNK/activator protein-1-dependent mechanisms (39)(40)(41), and in accordance to this, CNK1 regulates both pathways (12,13). Interestingly, activator protein-1 binding sites have been found in various proteases such as MMP-1, MMP-3, MMP-7, MMP-10, MMP-12, and MMP-13 (41), suggesting that CNK1 may be a global regulator of MMP transcription.…”

Section: Discussionmentioning

confidence: 79%

CNK1 Promotes Invasion of Cancer Cells through NF-κB–Dependent Signaling

Fritz

Radziwill

2010

Molecular Cancer Research

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Hallmarks of cancer cells are uncontrolled proliferation, evasion of apoptosis, angiogenesis, cell invasion, and metastasis, which are driven by oncogenic activation of signaling pathways. Herein, we identify the scaffold protein CNK1 as a mediator of oncogenic signaling that promotes invasion in human breast cancer and cervical cancer cells. Downregulation of CNK1 diminishes the invasiveness of cancer cells and correlates with reduced expression of matrix metalloproteinase 9 (MMP-9) and membrane-type 1 MMP (MT1-MMP). Ectopic expression of CNK1 elevates MT1-MMP promoter activity in a NF-κB-dependent manner. Moreover, CNK1 cooperates with the NF-κB pathway, but not with the extracellular signal-regulated protein kinase pathway, to promote cell invasion. Mechanistically, CNK1 regulates the alternative branch of the NF-κB pathway because knockdown of CNK1 interferes with processing of NF-κB2 p100 to p52 and its localization to the nucleus. In agreement with this, the invasion of CNK1-depleted cells is less sensitive to RelB downregulation compared with the invasion of control cells. Moreover, CNK1-dependent MT1-MMP promoter activation is blocked by RelB siRNA. Thus, CNK1 is an essential mediator of an oncogenic pathway involved in invasion of breast and cervical cancer cells and is therefore a putative target for cancer therapy. Mol Cancer Res; 8(3); 395-406. ©2010 AACR.

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“…MMP-9 activation has been shown to be especially associated with tumor progression and invasion, including mammary tumors (26). In previous reports, inflammatory cytokines, growth factors, or phorbol esters were shown to stimulate MMP-9 by activating different intracellular-signaling pathways in breast cancer cells (27)(28)(29). The inhibitory effect of MMP-9 expression is important for the development of a therapeutic experimental model of tumor metastasis.…”

Section: Discussionmentioning

confidence: 99%

Cordycepin inhibits TPA-induced matrix metalloproteinase-9 expression by suppressing the MAPK/AP-1 pathway in MCF-7 human breast cancer cells

Noh

Youn²,

Jung³

et al. 2009

Int J Mol Med

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Abstract. Matrix metalloproteinase-9 (MMP-9), which degrades the extracellular matrix (ECM), plays an important role in breast cancer cell invasion. NF-κB and AP-1 are known to induce MMP-9 expression. We investigated whether cordycepin, an NF-κB or AP-1 inhibitor, can modulate MMP-9 expression and cell invasion in MCF-7 cells. Toxicity of cordycepin was determined by 3-(4,5-dimethyl-thiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay. MMP-9 expression was determined by real-time PCR, Zymography, and Western blot analysis. AP-1 activation was assayed by electrophoretic mobility shift assay (EMSA). MAPK signaling was evaluated by Western blotting with specific p-ERK, and ERK, p-p38, p38, p-JNK, JNK antibodies. Cordycepin suppressed AP-1 activation, but not NF-κB activation in 12-O-tetradecanoylpho-bol-13-acetate (TPA)-treated MCF-7 cells. Cordycepin inhibits TPA-induced MMP-9 expression and cell invasion by suppressing AP-1 activation. Also, cordycepin suppressed the MAPK signaling pathway. Cordycepin is a potent inhibitor of TPA-induced MMP-9 expression and blocks strongly the ability of AP-1 activation via MAPK signaling pathway in MCF-7 cells.

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Tumor Necrosis Factor-α Augments Matrix Metalloproteinase-9 Production in Skeletal Muscle Cells through the Activation of Transforming Growth Factor-β-activated Kinase 1 (TAK1)-dependent Signaling Pathway

Cited by 57 publications

References 63 publications

Endurance exercise activates matrix metalloproteinases in human skeletal muscle

Endurance exercise activates matrix metalloproteinases in human skeletal muscle

CNK1 Promotes Invasion of Cancer Cells through NF-κB–Dependent Signaling

Cordycepin inhibits TPA-induced matrix metalloproteinase-9 expression by suppressing the MAPK/AP-1 pathway in MCF-7 human breast cancer cells

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