Glial cell line-derived neurotrophic factor induces cell migration and matrix metalloproteinase-13 expression in glioma cells

Lu, Dah‐Yuu; Leung, Yuk‐Man; Cheung, Chi-Wai; Chen, Yun‐Ru; Wong, Kar‐Lok

doi:10.1016/j.bcp.2010.06.046

Cited by 76 publications

(64 citation statements)

References 45 publications

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“…MMP-1 expression has been documented to occur in GBM cells (4,21), and increased expression correlates with increased tumor grade (58,71) and tumorigenicity (52), and decreased survival in GBM patients (71). Moreover, increased MMP-13 production in glioma cells in response to various stimuli leads to an increase in migration and invasion (43). Also of note, MMP-13 is a critical player in the activation of other MMPs (39).…”

Section: Discussionmentioning

confidence: 99%

EphrinA1 Is Released in Three Forms from Cancer Cells by Matrix Metalloproteases

Beauchamp

Lively

Mintz

et al. 2012

Molecular and Cellular Biology

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EphrinA1 is a glycosylphosphatidylinositol (GPI)-linked ligand for the EphA2 receptor, which is overexpressed in glioblastoma (GBM), among other cancers. Activation of the receptor by ephrinA1 leads to a suppression of oncogenic properties of GBM cells. We documented that a monomeric functional form of ephrinA1 is released from cancer cells and thus explored the mechanism of ephrinA1 release and the primary protein sequence. We demonstrate here that multiple metalloproteases (MMPs) are able to cleave ephrinA1, most notably MMP-1, -2, -9, and -13. The proteolytic cleavage that releases ephrinA1 occurs at three positions near the C terminus, producing three forms ending in valine-175, histidine-177, or serine-178. Moreover, deletion of amino acids 174 to 181 or 175 to 181 yields ephrinA1 that is still GPI linked but not released by proteolysis, underlining the necessity of amino acids 175 to 181 for release from the membrane. Furthermore, recombinant ephrinA1 ending at residue 175 retains activity toward the EphA2 receptor. These findings suggest a mechanism of release and provide evidence for the existence of several forms of monomeric ephrinA1. Moreover, ephrinA1 should be truncated at a minimum at amino acid 175 in fusions or conjugates with other molecules in order to prevent likely proteolysis within physiological and pathobiological environments.

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Section: Discussionmentioning

confidence: 99%

EphrinA1 Is Released in Three Forms from Cancer Cells by Matrix Metalloproteases

Beauchamp

Lively

Mintz

et al. 2012

Molecular and Cellular Biology

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“…10, A and B). Actually these kinase signalings had been correlated with the increased invasiveness of glioblastoma cells (49,50). For example, the alteration of the IP3K/Akt pathway was reported to regulate the migration and invasion of human glioma cells LN229, T89G, and U-373 through the reduction of MMP-2 and MT1-MMP (43).…”

Section: Discussionmentioning

confidence: 99%

Neurokinin-1 Receptor Directly Mediates Glioma Cell Migration by Up-regulation of Matrix Metalloproteinase-2 (MMP-2) and Membrane Type 1-Matrix Metalloproteinase (MT1-MMP)

Mou

Ya-wei

Zhou

et al. 2013

Journal of Biological Chemistry

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Background: Neurokinin-1 receptor is known to promote tumor cell proliferation. Results: Neurokinin-1 receptor activates ERK, JNK, and Akt through the G q -phospholipase C pathway, up-regulating MMP-2 and MT1-MMP and subsequently enhancing glioma cell migration. Conclusion: Neurokinin-1 receptor mediates glioma cell migration by the up-regulation of MMP-2 and MT1-MMP. Significance: This study shows for the first time that neurokinin-1 receptor is directly involved in tumor cell migration.

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“…Increased levels of GDNF in the urine could serve as a basis for the adjunct diagnosis, monitoring, and treatment of interstitial cystitis in patients with bladder cancer (Okragly et al 1999). Recently, we reported that GDNF increases cell migration and metastasis in gliomas, chondrosarcomas, and oral squamous cell carcinomas (Su et al 2009, Lu et al 2010, Chuang et al 2013. Moreover, it has also been reported that the GDNF expression in colon adenocarcinoma cells may play an important role in the pathogenesis of intestinal ganglioneuromatosis (Qiao et al 2009), where an increased expression of GDNF is associated with diffuse ganglioneuromatosis (Furuta et al 2007).…”

Section: Introductionmentioning

confidence: 93%

“…Previous reports have shown that GDNF also affects the survival of cancer cells and their proliferation in gliomas (Wiesenhofer et al 2000b) and enhances the metastasis ) and invasion potential (Kikuchi 2004, Ito et al 2005, Qiao et al 2009, Lu et al 2010) of pancreatic cancer. GDNF and its receptor are expressed in human cancers such as gliomas (Wiesenhofer et al 2000a).…”

Section: Introductionmentioning

confidence: 98%

GDNF increases cell motility in human colon cancer through VEGF–VEGFR1 interaction

Huang

Chen

Chiu

et al. 2013

Endocrine-Related Cancer

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Glial cell line-derived neurotrophic factor (GDNF), a potent neurotrophic factor, has been shown to affect cancer cell metastasis and invasion. However, the molecular mechanisms underlying GDNF-induced colon cancer cell migration remain unclear. GDNF is found to be positively correlated with malignancy in human colon cancer patients. The migratory activities of two human colon cancer cell lines, HCT116 and SW480, were found to be enhanced in the presence of human GDNF. The expression of vascular endothelial growth factor (VEGF) was also increased in response to GDNF stimulation, along with VEGF mRNA expression and transcriptional activity. The enhancement of GDNF-induced cancer cell migration was antagonized by a VEGF-neutralizing antibody. Our results also showed that the expression of VEGF receptor 1 (VEGFR1) was increased in response to GDNF stimulation, whereas GDNF-induced cancer cell migration was reduced by a VEGFR inhibitor. The GDNF-induced VEGF expression was regulated by the p38 and PI3K/Akt signaling pathways. Treatment with GDNF increased nuclear hypoxia-inducible factor 1 a (HIF1a) accumulation and its transcriptional activity in a time-dependent manner. Moreover, GDNF increased hypoxia responsive element (HRE)-containing VEGF promoter transcriptional activity but not that of the HRE-deletion VEGF promoter construct. Inhibition of HIF1a by a pharmacological inhibitor or dominant-negative mutant reduced the GDNF-induced migratory activity in human colon cancer cells. These results indicate that GDNF enhances the migration of colon cancer cells by increasing VEGF-VEGFR interaction, which is mainly regulated by the p38, PI3K/Akt, and HIF1a signaling pathways.

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Glial cell line-derived neurotrophic factor induces cell migration and matrix metalloproteinase-13 expression in glioma cells

Cited by 76 publications

References 45 publications

EphrinA1 Is Released in Three Forms from Cancer Cells by Matrix Metalloproteases

EphrinA1 Is Released in Three Forms from Cancer Cells by Matrix Metalloproteases

Neurokinin-1 Receptor Directly Mediates Glioma Cell Migration by Up-regulation of Matrix Metalloproteinase-2 (MMP-2) and Membrane Type 1-Matrix Metalloproteinase (MT1-MMP)

GDNF increases cell motility in human colon cancer through VEGF–VEGFR1 interaction

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