Curcumin suppresses phorbol ester-induced matrix metalloproteinase-9 expression by inhibiting the PKC to MAPK signaling pathways in human astroglioma cells

Woo, Moon Sook; Jung, Soo Hyun; Kim, So Young; Hyun, Jin Won; Ko, Kwang Ho; Kim, Won Ki; Kim, Hee Sun

doi:10.1016/j.bbrc.2005.07.174

Cited by 163 publications

(107 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Activation of these kinases causes variable cellular responses depending upon cell type. Some studies have shown that curcumin represses or promotes ERK, JNK and p38 activation, while others have found no effect of curcumin on ERK, JNK and p38 activation (13)(14)(15)(30)(31)(32). These findings indicated a dual role for MAPK in the cellular response that appeared to be specific to the type of cell and apoptotic stimulus studied.…”

Section: Discussionmentioning

confidence: 96%

Curcumin induces apoptosis in human lung adenocarcinoma A549 cells through a reactive oxygen species-dependent mitochondrial signaling pathway

Chen

Wang²,

Xu³

et al. 2009

Oncol Rep

View full text Add to dashboard Cite

Abstract.Several studies have shown that curcumin can induce apoptosis and inhibit growth in human A549 lung adenocarcinoma cells. However, the mechanism is not completely understood yet. The present study was designed to investigate the effects of curcumin on A549 cells to better understand its apoptosis and apoptosis-related factors in vitro. The apoptosis induction, intracellular reactive oxygen species (ROS) and mitochondrial membrane potential (MMP) were examined by confocal fluorescence microscope and flow cytometry. The MAPK protein expression was examined by Western blot analysis. After treatment with curcumin, apoptosis were observed. Curcumin-induced apoptosis was accompanied by an increase of intracellular ROS level and a loss of MMP. In addition, induction of apoptosis was also accompanied by sustained phosphorylation and activation of JNK, p38 and ERK. However, pretreatment with MAPK inhibitors had no effect upon curcumin-induced apoptosis. GSH and NAC, an anti-oxidant agent, blocked the curcumin-induced ROS production, MMP loss and rescued cells from curcumininduced apoptosis. Our results indicated that curcumin induced apoptosis in A549 cells through a reactive oxygen speciesdependent mitochondrial signaling pathway and independent of MAPK signaling pathway.

show abstract

Section: Discussionmentioning

confidence: 96%

Curcumin induces apoptosis in human lung adenocarcinoma A549 cells through a reactive oxygen species-dependent mitochondrial signaling pathway

Chen

Wang²,

Xu³

et al. 2009

Oncol Rep

View full text Add to dashboard Cite

show abstract

“…AP-1, which belongs to the bZIP group of DNA-binding proteins, associates to form a variety of homo-and heterodimers through a combination of signaling events, leading to increased activity of proteins that directly potentiate Jun and Fos family members or activate transcription factors that regulate c-jun and c-fos expression. (18,(36)(37)(38)(39). NF-κB comprises a family of inducible transcription factors which regulate host inflammatory and immune responses (40).…”

Section: Discussionmentioning

confidence: 99%

“…MMP-2, on the other hand, is usually expressed constitutively (14,15). Cytokine and TPA treatments can induce MMP-9 expression via activation of transcription factors such as nuclear factor-κB (NF-κB) and activator protein-1 (AP-1) (16)(17)(18).…”

Section: Introductionmentioning

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

View full text Add to dashboard Cite

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.

show abstract

“…Phorbol 12-myristate 13-acetate (PMA) was previously described to induce MMP-9 expression in normal and tumoral astrocytes, through activation of the Protein Kinase C pathway (Arai et al, 2003;Woo et al, 2005). We performed gelatin zymography (GZ) to determine whether PMA increases the MMP-9 expression and/or activity in LN229 astrocytoma cells.…”

Section: Mmp-9 Secreted By Ln229 Astrocytoma Cells Induces Igfbp2 Promentioning

confidence: 99%

Matrix metalloproteinase‐9 interplays with the IGFBP2–IGFII complex to promote cell growth and motility in astrocytomas

Rorive

Berton

D’Haene

et al. 2008

Glia

View full text Add to dashboard Cite

Insulin-like growth factor II (IGFII) acts as a potent mitogen for several tumor types and has been reported to positively influence astrocytoma cell growth and motility. In the central nervous system, IGFII bioavailability is mainly modulated by insulin-like growth factor binding protein 2 (IGFBP2), which sequestrates IGFII and therefore prevents its interaction with the type-1 IGF receptor (IGF-IR). Proteolysis of IGFBP2 is the predominant mechanism recognized to reduce the binding affinity of IGFBP2 for IGFII, thus favoring dissociation of IGFII from the IGFBP2-IGFII complex. It is known that certain proteases involved in astrocytoma malignancy, such as matrix metalloproteinase-7 (MMP-7), plasmin, and cathepsin D, are able to proteolyze IGFBP2 in vitro. The present study aims to investigate whether other proteases expressed by astrocytomas, specifically MMP-2, MMP-9, and membrane-type 1 matrix metalloprotease (MT1-MMP), are able to proteolyze the IGFBP2-IGFII complex. Our results show the following: (i) MMP-9 proteolyzes the IGFBP2-IGFII complex in vitro, while MMP-2 and MT1-MMP do not; (ii) this MMP-9-induced IGFBP2-IGFII complex proteolysis releases free IGFII, which contributes to enhance the motility and the growth of LN229 astrocytoma cells. Furthermore, this study also highlights that the formation of the IGFBP2-IGFII complex inhibits IGFBP2's cell motility promoting effect by reducing the pool of free IGFBP2. In conclusion, MMP-9-induced IGFBP2 proteolysis may be regarded as an important post-translational event involved in astrocytoma aggressiveness. These new findings support drug targeting of MMP-9 as an interesting approach in the treatment of astrocytoma. V V C

show abstract

Curcumin suppresses phorbol ester-induced matrix metalloproteinase-9 expression by inhibiting the PKC to MAPK signaling pathways in human astroglioma cells

Cited by 163 publications

References 20 publications

Curcumin induces apoptosis in human lung adenocarcinoma A549 cells through a reactive oxygen species-dependent mitochondrial signaling pathway

Curcumin induces apoptosis in human lung adenocarcinoma A549 cells through a reactive oxygen species-dependent mitochondrial signaling pathway

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

Matrix metalloproteinase‐9 interplays with the IGFBP2–IGFII complex to promote cell growth and motility in astrocytomas

Contact Info

Product

Resources

About