c‐Cbl regulates glioma invasion through matrix metalloproteinase 2

Lee, Ho-Jin; Tsygankov, Alexander Y.

doi:10.1002/jcb.22839

Cited by 17 publications

(19 citation statements)

References 46 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…For example, RING finger protein 5 (RNF5) has been shown to inhibit cell motility by targeting cytoskeletal protein paxillin ubiquitination and altered localization (41). In contrast, RNF13 and RNF55 (also known as proto-oncogene c-Cbl) promote pancreatic cancer and glioma invasion by enhancing the activity of extracellular matrix metallopeptidase-9 (MMP-9) and MMP-2, respectively (42,43), which are required for degrading structural extracellular matrix proteins to promote invasion and metastasis (44). Similarly, RNF45 (also known as tumor autocrine motility factor receptor or gp78) promote sarcoma metastasis by targeting the metastasis suppressor KAI1 for degradation (45).…”

Section: Discussionmentioning

confidence: 99%

Metastasis-associated Protein 1 Drives Tumor Cell Migration and Invasion through Transcriptional Repression of RING Finger Protein 144A

Marzook

Nair

et al. 2012

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background:The mechanistic role of MTA1 in tumor aggressiveness is yet to be deciphered. Results: RNF144A is a direct target of transcriptional repression by MTA1 and inhibits migration and invasion. Conclusion: Transcriptional repression of RNF144A by MTA1 confers a migratory and invasive phenotype of cancer cells. Significance: This study provides novel mechanistic insights into regulation of tumor progression by MTA1.

show abstract

Section: Discussionmentioning

confidence: 99%

Metastasis-associated Protein 1 Drives Tumor Cell Migration and Invasion through Transcriptional Repression of RING Finger Protein 144A

Marzook

Nair

et al. 2012

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…As an example, we can refer to EMMPRIN, a class of glycoprotein secreted by tumor cells, which stimulates MMP-2 expression by fibroblasts (Biswas et al, 2010). Nonetheless, factors accounting for the unbalanced regulation of the enzyme are continuously identified; this is the case of the L1CAM adhesion molecule in a model of lung metastasis and of an E3 uniquitin ligase (c-Cbl) (Hauser et al, 2011;Lee and Tsygankov, 2010;Song et al, 2010).…”

Section: Biological Aspectsmentioning

confidence: 99%

Human matrix metalloproteinases: An ubiquitarian class of enzymes involved in several pathological processes

Sbardella

Fasciglione

Gioia

et al. 2012

Molecular Aspects of Medicine

209

212

View full text Add to dashboard Cite

a b s t r a c tHuman matrix metalloproteinases (MMPs) belong to the M10 family of the MA clan of endopeptidases. They are ubiquitarian enzymes, structurally characterized by an active site where a Zn 2+ atom, coordinated by three histidines, plays the catalytic role, assisted by a glutamic acid as a general base. Various MMPs display different domain composition, which is very important for macromolecular substrates recognition. Substrate specificity is very different among MMPs, being often associated to their cellular compartmentalization and/or cellular type where they are expressed. An extensive review of the different MMPs structural and functional features is integrated with their pathological role in several types of diseases, spanning from cancer to cardiovascular diseases and to neurodegeneration. It emerges a very complex and crucial role played by these enzymes in many physiological and pathological processes.

show abstract

“…Because CBL is well known to promote tumor proliferation and invasion [18, 19], we examined if miR-124-3p would modulate CBL to influence the proliferation and invasion of breast cancer cells. We designed a siRNA sequence targeting CBL ORF to knockdown CBL and constructed a plasmid expressing the full-length CBL ORF to overexpress CBL without the miR-124-responsive 3’-UTR.…”

Section: Resultsmentioning

confidence: 99%

miR-124-3p functions as a tumor suppressor in breast cancer by targeting CBL

Chen

et al. 2016

BMC Cancer

View full text Add to dashboard Cite

BackgroundThe origin and development of breast cancer remain complex and obscure. Recently, microRNA (miRNA) has been identified as an important regulator of the initiation and progression of breast cancer, and some studies have shown the essential role of miR-124-3p as a tumor suppressor in breast tumorigenesis. However, the detailed role of miR-124-3p in breast cancer remains poorly understood.MethodsQuantitative RT-PCR and western blotting assays were used to measure miR-124-3p and CBL expression levels in breast cancer tissues, respectively. Luciferase reporter assay was employed to validate the direct targeting of CBL by miR-124-3p. Cell proliferation and invasion assays were performed to analyze the biological functions of miR-124-3p and CBL in breast cancer cells.ResultsIn the present study, we found that miR-124-3p was consistently downregulated in breast cancer tissues. Moreover, we showed that miR-124-3p significantly suppressed the proliferation and invasion of breast cancer cells. In addition, we investigated the molecular mechanism through which miR-124-3p contributes to breast cancer tumorigenesis and identified CBL (Cbl proto-oncogene, E3 ubiquitin protein ligase) as a direct target gene of miR-124-3p. Moreover, we found that ectopic expression of CBL can attenuate the inhibitory effect of miR-124-3p on cell proliferation and invasion in breast cancer cells.ConclusionsThis study identified a new regulatory axis in which miR-124-3p and CBL regulate the proliferation and invasion of breast cancer cells.Electronic supplementary materialThe online version of this article (doi:10.1186/s12885-016-2862-4) contains supplementary material, which is available to authorized users.

show abstract

c‐Cbl regulates glioma invasion through matrix metalloproteinase 2

Cited by 17 publications

References 46 publications

Metastasis-associated Protein 1 Drives Tumor Cell Migration and Invasion through Transcriptional Repression of RING Finger Protein 144A

Metastasis-associated Protein 1 Drives Tumor Cell Migration and Invasion through Transcriptional Repression of RING Finger Protein 144A

Human matrix metalloproteinases: An ubiquitarian class of enzymes involved in several pathological processes

miR-124-3p functions as a tumor suppressor in breast cancer by targeting CBL

Contact Info

Product

Resources

About