Proteomic analysis of cell cycle arrest and differentiation induction caused by ATPR, a derivative of all‐trans retinoic acid, in human gastric cancer SGC‐7901 cells

Qin, Xia; Zhao, Yingli; Wang, Jiali; Qiao, Wenhao; Zhang, Dongling; Yin, Hong; Xu, Donghui; Chen, Feihu

doi:10.1002/prca.201600099

Cited by 20 publications

(21 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Subcellular expression analysis showed that filamin A was transferred from the cytoplasm to the nucleus after ATPR treatment and showed a significantly high nucleus to cytoplasm ratio for 14‐3‐3ε and filamin A in the ATPR group, which suggested that ATPR was able to regulate the subcellular localization of filamin A (Figure A). According to our previous study, ATPR also regulates the subcellular localization of 14‐3‐3ε and promotes its transfer to the nucleus . As the binding of 14‐3‐3ε to filamin A decreases after ATPR treatment, 14‐3‐3ε was speculated to promote the transfer of filamin A from the cytoplasm to the nucleus.…”

Section: Resultsmentioning

confidence: 88%

“…In our previous study, ATPR was shown to induce G 0 /G 1 phase arrest in gastric cancer cells by downregulating the total expression of 14‐3‐3ε and inducing its nuclear location . To further explore the role of ATPR and 14‐3‐3ε on the cell cycle in gastric cancer, a targeted proteomics approach was used to identify the 14‐3‐3ε‐binding proteins in ATPR group and the vehicle group.…”

Section: Resultsmentioning

confidence: 99%

“…Each 4‐μg sample was loaded and separated on a C18 column (10 cm × 100 μm) using a nano‐liquid chromatograph (Dionex, Thermo Fisher). The separation procedure refers to our previous experimental conditions . The liquid phase‐separated peptide was introduced into a Q‐Exactive tandem mass spectrometer (ThermoFisher Scientific, San Jose, CA) equipped with an ESI ionization source.…”

Section: Methodsmentioning

confidence: 99%

“…For overexpression of 14‐3‐3ε, SGC‐7901 cells were maintained in 1 mL of complete medium with 5 mg/mL Polybrene per well and were treated with 3 × 10 6 TU/mL 14‐3‐3ε gene‐lentiviral particles overnight, and three wells were transduced with empty lentiviral particles as the control . For knockdown of 14‐3‐3ε or filamin A, all sequences of siRNAs are shown in Table .…”

Section: Methodsmentioning

confidence: 99%

“…The separation procedure refers to our previous experimental conditions. 12 The liquid phase-separated peptide was introduced into a Q-Exactive tandem mass spectrometer (ThermoFisher Scientific, San Jose, CA) equipped with an ESI ionization source.…”

Section: In-gel Enzymatic Digestion and Mass Spectrometry Analysismentioning

confidence: 99%

See 4 more Smart Citations

ATPR‐induced G₀/G₁ phase arrest in gastric cancer cells by regulating the binding of 14‐3‐3ε and filamin A

Zhao

Fang

et al. 2018

Cancer Medicine

Self Cite

View full text Add to dashboard Cite

Abstract4‐amino‐2‐trifluoromethyl‐phenyl retinate (ATPR) was able to induce the G0/G1 phase arrest in gastric cancer SGC‐7901 cells by downregulating 14‐3‐3ε. However, the mechanisms underlying this effect have not been fully elucidated. Because 14‐3‐3ε functions as a molecular chaperone on cell cycle regulation, the interaction between 14‐3‐3ε and the target proteins is worth an in‐depth study. In this study, the use of targeting proteomics identified 352 14‐3‐3ε‐binding proteins in SGC‐7901 cells. Analysis of gene ontology (GO) was performed using PANTHER to annotate the biological processes, protein classes, and pathways of these proteins. In 25 cell cycle‐related proteins, filamin A was reduced following ATPR treatment, and this change was validated by immunoprecipitation. The cell cycle was arrested at the G0/G1 phase following ATPR treatment or filamin A silencing in SGC‐7901 cells. Furthermore, subcellular expression analysis showed that 14‐3‐3ε and filamin A were transferred from the cytoplasm to the nucleus after ATPR treatment. On the other hand, overexpression of 14‐3‐3ε, in SGC‐7901 cells, resulted in an increase in the total cellular level of filamin A and an increase in the subcellular localization of filamin A in the cytoplasm. ATPR treatment of the 14‐3‐3ε overexpression cells decreased the total level of filamin A and redistributed filamin A protein from the cytoplasm to the nucleus. Immunohistochemical analysis showed that the expression levels of 14‐3‐3ε and filamin A in gastric cancer tissues were significantly higher, with a predominant localization in the cytoplasm, compared to the levels in matched tissues. Taken together, our results suggest that ATPR can induce nuclear localization of filamin A by reducing the binding of 14‐3‐3ε and filamin A, which may be the mechanism of ATPR‐induced G0/G1 phase arrest.

show abstract

Section: Resultsmentioning

confidence: 88%

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: In-gel Enzymatic Digestion and Mass Spectrometry Analysismentioning

confidence: 99%

See 3 more Smart Citations

ATPR‐induced G₀/G₁ phase arrest in gastric cancer cells by regulating the binding of 14‐3‐3ε and filamin A

Zhao

Fang

et al. 2018

Cancer Medicine

Self Cite

View full text Add to dashboard Cite

show abstract

p‐Hydroxylcinnamaldehyde slows the progression of 4NQO‐induced oesophageal tumourigenesis via the RhoA‐MAPK signaling pathway

Zhao

et al. 2018

Molecular Carcinogenesis

View full text Add to dashboard Cite

p-Hydroxylcinnamaldehyde isolated from the Cochinchina momordica seed (CMSP) has been identified to inhibit growth and metastasis in oesophageal squamous cell carcinoma (ESCC) by inducing differentiation. The aim of the present study was to evaluate the effect and underlying mechanism of CMSP on 4-nitroquinoline 1-oxide (4NQO)-induced oesophageal tumourigenesis. In the present study, a mouse model of oesophageal preneoplastic lesions was established by providing 4NQO-containing drinking water to C57BL/6 mice. The effect of CMSP on tumourigenesis induced by the chemical mutagen and the effect of CMSP on immune function were investigated. The results showed that the incidence and pathological stage of atypical hyperplasia in oesophageal tissues were significantly reduced in CMSP-treated mice compared with untreated mice. Immunohistochemistry and pull-down assay results revealed that the expression levels of p-ERK1/2, p-SAPK/JNK, and GTP-RhoA were significantly decreased in the oesophageal tissue of CMSP-treated mice. In addition, the proportions of CD4 T cells, CD8 T cells, and NK cells were increased, while the proportion of CD4 CD25 regulatory T cells (Tregs) was decreased, in the peripheral blood of CMSP-treated mice. These results indicated that CMSP could hamper 4NQO-induced oesophageal tumourigenesis by regulating the RhoA-ERK/JNK signaling pathway and promoting immune system function, thus providing a new potential strategy for treating preneoplastic lesions of the oesophagus.

show abstract

Quantitative Proteomic Profiling of Cerebrospinal Fluid to Identify Candidate Biomarkers for Alzheimer's Disease

Sathe

Renuse

et al. 2019

Proteomics Clinical Apps

View full text Add to dashboard Cite

Purpose Development of novel biomarkers for AD is important for early diagnosis, monitoring disease progression and therapeutic response. The aim of this study was to identify the potential CSF biomarkers for Alzheimer's disease (AD) and evaluate these markers on independent CSF samples using a parallel reaction monitoring mass spectrometry (PRM-MS) assay. Experimental design In this study, we employed high-resolution mass spectrometry and tandem mass tag (TMT) multiplexing technology to identify proteins that might serve as candidate biomarkers for Alzheimer’s disease. Identified potential biomarkers were validated using a parallel reaction monitoring mass spectrometry (PRM-MS) assay. Results We identified 2,327 proteins in the cerebrospinal fluid (CSF) of which 139 were observed to be significantly different in their abundance in the CSF of AD patients versus controls. The proteins whose abundance was altered in AD included a number of known AD marker proteins such as MAPT, NPTX2, SCG2, VGF, GFAP, SST and NCAM1 as well as novel biomarkers such as GSN, PKM and YWHAG. We then sought to validate these findings in a separate set of CSF specimens from AD dementia patients and controls. For the AD group, significant increases were found for YWHAG and PKM, and a significant decrease was observed for VGF by multiplexed targeted parallel reaction monitoring (PRM) experiments. NPTX2 in combination with PKM or with YWHAG led to the best results with AUCs of 0.935 and 0.933, respectively. Conclusions and clinical relevance The identified altered CSF proteins in AD CSF samples will be useful to understand AD pathogenesis.

show abstract

Proteomic analysis of cell cycle arrest and differentiation induction caused by ATPR, a derivative of all‐trans retinoic acid, in human gastric cancer SGC‐7901 cells

Cited by 20 publications

References 30 publications

ATPR‐induced G₀/G₁ phase arrest in gastric cancer cells by regulating the binding of 14‐3‐3ε and filamin A

ATPR‐induced G₀/G₁ phase arrest in gastric cancer cells by regulating the binding of 14‐3‐3ε and filamin A

p‐Hydroxylcinnamaldehyde slows the progression of 4NQO‐induced oesophageal tumourigenesis via the RhoA‐MAPK signaling pathway

Quantitative Proteomic Profiling of Cerebrospinal Fluid to Identify Candidate Biomarkers for Alzheimer's Disease

Contact Info

Product

Resources

About

Proteomic analysis of cell cycle arrest and differentiation induction caused by ATPR, a derivative of all‐trans retinoic acid, in human gastric cancer SGC‐7901 cells

Cited by 20 publications

References 30 publications

ATPR‐induced G0/G1 phase arrest in gastric cancer cells by regulating the binding of 14‐3‐3ε and filamin A

ATPR‐induced G0/G1 phase arrest in gastric cancer cells by regulating the binding of 14‐3‐3ε and filamin A

p‐Hydroxylcinnamaldehyde slows the progression of 4NQO‐induced oesophageal tumourigenesis via the RhoA‐MAPK signaling pathway

Quantitative Proteomic Profiling of Cerebrospinal Fluid to Identify Candidate Biomarkers for Alzheimer's Disease

Contact Info

Product

Resources

About

ATPR‐induced G₀/G₁ phase arrest in gastric cancer cells by regulating the binding of 14‐3‐3ε and filamin A

ATPR‐induced G₀/G₁ phase arrest in gastric cancer cells by regulating the binding of 14‐3‐3ε and filamin A