EFEMP1 promotes ovarian cancer cell growth, invasion and metastasis via activated the AKT pathway

Yin, Xiuxiu; Fang, Shuang; Wang, Mei; Wang, Qiang; Fang, Rui; Chen, Jie

doi:10.18632/oncotarget.10296

Cited by 28 publications

(28 citation statements)

References 30 publications

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“…Recent studies have yielded conflicting results about the function of fibulin-3 in tumor biology, showing that affinity or anti-tumor biological activity upon up- or downregulated expression depends on the type of cancer. In ovarian cancer 7 , 8 , osteosarcoma 9 , pancreatic cancer 10 , and glioblastoma 11 , fibulin-3 up-regulation was associated with poor prognosis because of malignant cell growth and invasion. On the other hand, downregulation of fibulin-3 in liver cancer 12 , 13 , gastric carcinoma 14 , lung carcinoma 15 , 16 , endometrial cancer 17 , and nasopharyngeal cancer 18 , was able to suppress cancer cell growth and metastasis.…”

Section: Introductionmentioning

confidence: 99%

RETRACTED ARTICLE: Fibulin-3 knockdown inhibits cervical cancer cell growth and metastasis in vitro and in vivo

Li¹,

Chen²,

Liu³

et al. 2018

Sci Rep

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To explore the function of fibulin-3 in cervical carcinoma malignant cell growth and metastasis, fibulin-3 expression in normal cervical tissue, cervical intraepithelial neoplasia (CIN), and cervical carcinoma were evaluated by immunohistochemistry. Quantitative real-time-polymerase chain reaction, western blotting, and immunocytochemistry were performed to assess the expression of fibulin-3 at mRNA and protein levels in different invasive clone sublines. Fibulin-3 shRNA and fibulin-3 cDNA were used to transfect the strongly and weakly invasive clone sublines. Using in vitro and in vivo functional assays, we investigated the effects of down-regulating and up-regulating fibulin-3 expression on the proliferation and invasion of different clone sublines. Epithelial mesenchymal transition (EMT) and its signaling pathways PI3K/AKT and ERK were studied carefully in lentiviral transfection systems. Fibulin-3 was upregulated in cervical carcinoma, and its overexpression was significantly related with malignant phenotype and poor prognosis of cervical carcinoma. Fibulin-3 promoted cervical cancer cell invasive capabilities by eliciting EMT and activating the PI3K-Akt-mTOR signal transduction pathway. Fibulin-3 could facilitate the process of cervical cancer development. The results presented here will help develop novel prognostic factors and possible therapeutic options for patients with cervical cancer.

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Section: Introductionmentioning

confidence: 99%

RETRACTED ARTICLE: Fibulin-3 knockdown inhibits cervical cancer cell growth and metastasis in vitro and in vivo

Li¹,

Chen²,

Liu³

et al. 2018

Sci Rep

Self Cite

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“…In addition, carbonic anhydrase 9 (CA9) and angiopoietin‐related protein 4 (ANGPTL4), proteins known to respond to tumor hypoxia (Sedlakova et al , ; Carbone et al , ), showed 13‐ and 3.6‐fold increases, respectively, in tumor tissue (Fig D and Appendix Table S1). Finally, EGF‐containing fibulin‐like extracellular matrix protein 1 (EFEMP1), which binds to epidermal growth factor receptor (EGFR) to promote tumor growth, invasion, and metastasis (Yin et al , ), showed a threefold increase across seven O‐linked glycosylation sites in tumor tissue (Fig D and Appendix Table S1). By contrast, both IGHA1 and MUC1, known O‐linked glycoproteins, showed no detectable change between normal and tumor tissue indicating that the changes in O‐linked glycoproteins observed in tumor tissue are highly selective.…”

Section: Resultsmentioning

confidence: 99%

Mapping the O‐glycoproteome using site‐specific extraction of O‐linked glycopeptides (EXoO)

Yang

et al. 2018

Molecular Systems Biology

128

181

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Protein glycosylation is one of the most abundant post‐translational modifications. However, detailed analysis of O‐linked glycosylation, a major type of protein glycosylation, has been severely impeded by the scarcity of suitable methodologies. Here, a chemoenzymatic method is introduced for the site‐specific extraction of O‐linked glycopeptides (EXoO), which enabled the mapping of over 3,000 O‐linked glycosylation sites and definition of their glycans on over 1,000 proteins in human kidney tissues, T cells, and serum. This large‐scale localization of O‐linked glycosylation sites demonstrated that EXoO is an effective method for defining the site‐specific O‐linked glycoproteome in different types of sample. Detailed structural analysis of the sites identified revealed conserved motifs and topological orientations facing extracellular space, the cell surface, the lumen of the Golgi, and the endoplasmic reticulum (ER). EXoO was also able to reveal significant differences in the O‐linked glycoproteome of tumor and normal kidney tissues pointing to its broader use in clinical diagnostics and therapeutics.

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“…Through previous studies, we found that EFEMP1 was involved in the regulation of many biological processes in carcinoma, suggesting that EFEMP1 may play an important role in the development of HCC. When the transcription of EFEMP1 was inhibited, how did it cause phenotypic changes in HCC cells, and by what kind of signaling pathway to affect HCC?…”

Section: Resultsmentioning

confidence: 96%

Epidermal growth factor‐containing fibulin‐like extracellular matrix protein 1 (EFEMP1) suppressed the growth of hepatocellular carcinoma cells by promoting Semaphorin 3B(SEMA3B)

Duan

Jiang

et al. 2019

Cancer Medicine

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Aim Epidermal growth factor‐containing fibulin‐like extracellular matrix protein 1(EFEMP1) has been found to be involved in the occurrence and development of many cancers. The relationship between EFEMP1 and the development of hepatocellular carcinoma (HCC) and the molecular mechanism are not fully understood. Methods Real‐time polymerase chain reaction (PCR) and tissue microarray were used to detect the expression of EFEMP1 in HCC cell lines and tissue. Methylation‐specific PCR assay was used to measure the methylation level of EFEMP1 in HCC cell lines and tissue. To study the function of EFEMP1 on cell function, Huh7 and HepG2 were infected with lentiviral particles expressing EFEMP1. MTT assay and colony formation assay were used to examine the effect of EFEMP1 on cell proliferation. Annexin‐VAPC/7‐AAD double were used to detect the effect of EFEMP1 on cell apoptosis. To further detect the effect of EFEMP1 on the development of HCC in vivo, we performed the tumor formation experiment in nude mice. Gene chip was used to detect the expression profile of Huh7 and HepG2 overexpressing EFEMP1. To further screen out the differences, GO analysis and pathway analysis were performed. To study the effects of SEMA3B, specific siRNA was used to inhibit the expression of SEMA3B. Chi‐squared test and rank sum test were used to analyze the relationship between EFEMP1 expression and HCC clinical characteristic. Results The study found that the expression of EFEMP1 was significantly decreased in HCC cell lines and HCC tissues. The expression level of EFEMP1 was related to the TNM (the extent of the tumor, the extent of spread to the lymph nodes, the presence of metastasis) stage and the prognosis of patients with HCC. The decrease of protein expression suggested that the patient prognosis was worse, and the protein level of EFEMP1 may be an independent factor in the prognosis of HCC patients. Promoter methylation may be one of the reasons for EFEMP1 inhibition. EFEMP1 could inhibit the proliferation of HCC cells and promoted the apoptosis of HCC cells to regulate the development of HCC. And EFEMP1 promoted the apoptosis of HCC cells mainly through the mitochondrial apoptosis pathway. EFEMP1 may inhibit the proliferation of HCC cells through the SEMA3B gene in the Axon guidance pathway. Conclusion In summary, our research revealed the regulation of EFEMP1 on cell proliferation and apoptosis in HCC. EFEMP1 may suppress the growth of HCC cells by promoting SEMA3B.

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EFEMP1 promotes ovarian cancer cell growth, invasion and metastasis via activated the AKT pathway

Cited by 28 publications

References 30 publications

RETRACTED ARTICLE: Fibulin-3 knockdown inhibits cervical cancer cell growth and metastasis in vitro and in vivo

RETRACTED ARTICLE: Fibulin-3 knockdown inhibits cervical cancer cell growth and metastasis in vitro and in vivo

Mapping the O‐glycoproteome using site‐specific extraction of O‐linked glycopeptides (EXoO)

Epidermal growth factor‐containing fibulin‐like extracellular matrix protein 1 (EFEMP1) suppressed the growth of hepatocellular carcinoma cells by promoting Semaphorin 3B(SEMA3B)

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