Nanchang, China
Nanchang, China

Time filter

Source Type

Yang X.,Jiangxi Tumor Hospital | Zhang Y.,CAS Wuhan Institute of Hydrobiology | Zhang Y.,CAS Wuhan Institute of Virology | Zhang L.,Nanjing Southeast University | And 3 more authors.
Acta Biochimica et Biophysica Sinica | Year: 2014

The normal cellular prion protein, PrPC is a highly conserved and widely expressed cell surface glycoprotein in all mammals. The expression of PrP is pivotal in the pathogenesis of prion diseases; however, the normal physiological functions of PrPC remain incompletely understood. Based on the studies in cell models, a plethora of functions have been attributed to PrPC. In this paper, we reviewed the potential roles that PrP C plays in cell physiology and focused on its contribution to tumorigenesis. © 2014 The Author 2014.


PubMed | Nanjing Southeast University, CAS Wuhan Institute of Virology, Jiangxi Tumor Hospital, University of Chinese Academy of Sciences and 3 more.
Type: Journal Article | Journal: The Journal of biological chemistry | Year: 2016

The normal cellular prion protein (PrP) is a glycosylphosphatidylinositol (GPI)-anchored cell surface glycoprotein. However, in pancreatic ductal adenocarcinoma cell lines, such as BxPC-3, PrP exists as a pro-PrP retaining its glycosylphosphatidylinositol (GPI) peptide signaling sequence. Here, we report the identification of another pancreatic ductal adenocarcinoma cell line, AsPC-1, which expresses a mature GPI-anchored PrP. Comparison of the 24 genes involved in the GPI anchor modification pathway between AsPC-1 and BxPC-3 revealed 15 of the 24 genes, including PGAP1 and PIG-F, were down-regulated in the latter cells. We also identified six missense mutations in DPM2, PIG-C, PIG-N, and PIG-P alongside eight silent mutations. When BxPC-3 cells were fused with Chinese hamster ovary (CHO) cells, which lack endogenous PrP, pro-PrP was successfully converted into mature GPI-anchored PrP. Expression of the individual gene, such as PGAP1, PIG-F, or PIG-C, into BxPC-3 cells does not result in phosphoinositide-specific phospholipase C sensitivity of PrP. However, when PIG-F but not PIG-P is expressed in PGAP1-expressing BxPC-3 cells, PrP on the surface of the cells becomes phosphoinositide-specific phospholipase C-sensitive. Thus, low expression of PIG-F and PGAP1 is the major factor contributing to the accumulation of pro-PrP. More importantly, BxPC-3 cells expressing GPI-anchored PrP migrate much slower than BxPC-3 cells bearing pro-PrP. In addition, GPI-anchored PrP-bearing AsPC-1 cells also migrate slower than pro-PrP bearing BxPC-3 cells, although both cells express filamin A. Knocking out PRNP in BxPC-3 cell drastically reduces its migration. Collectively, these results show that multiple gene irregularity in BxPC-3 cells is responsible for the formation of pro-PrP, and binding of pro-PrP to filamin A contributes to enhanced tumor cell motility.


PubMed | Surgery Academy, Shanghai JiaoTong University, Yaan Peoples Hospital, Shanghai University and Jiangxi Tumor Hospital
Type: | Journal: BioMed research international | Year: 2014

Colorectal tumorigenesis is ascribed to the activity of Wnt signaling pathway in a ligand-independent manner mainly through APC and CTNNB1 gene mutations and in a ligand-dependent manner through low expression of Wnt inhibitors such as WNT inhibitory factor 1 (WIF1) and secreted frizzled related protein 1 (SFRP1). In this study we found that WIF1 protein expression was increased and SFRP1 was decreased significantly in CRC tissue versus normal tissue, and high expression of WIF1 was associated with big tumor diameters and deep invasion, and loss of SFRP1 expression was associated with the left lesion site, deep invasion, and high TNM stage. Among the four expression patterns (WIF+/SFRP1+, WIF+/SFRP1-, WIF-/SFRP1+, and WIF-/SFRP1-) only coexpression of WIF1 and SFRP1 (WIF+/SFRP1+) was associated with favorable overall survival, together with low TNM stage, as an independent prognostic factor as shown in a multivariate survival model. The results indicated that WIF1 seemed to play an oncogenic role, while SFRP1 seemed to play an oncosuppressive role although both of them are secreted Wnt antagonists. Coexpression of SFRP1 and WIF1, rather than SFRP1 or WIF1 alone, could be used, together with low TNM stage, as a prognostic predictor of favorable outcomes in CRC.


Fu Q.,Nanchang University | Fu Q.,Jiangxi Provincial Peoples Hospital | Zhou X.,Nanchang University | Dong Y.,Jiangxi Tumor Hospital | And 4 more authors.
PLoS ONE | Year: 2016

The purpose of this study was to characterize the inhibitory modulation of cocaine- and amphetamine-regulated transcript (CART) peptides, particularly with respect to the function of the D3 dopamine receptor (D3R), which is activated by its interaction with phosphorylated CaMKIIα (pCaMKIIα) in the nucleus accumbens (NAc). After repeated oral administration of caffeine (30 mg/kg) for five days, microinjection of CART peptide (0.08 μM/0.5 μl/hemisphere) into the NAc affected locomotor behavior. The pCaMKIIα-D3R interaction, D3R phosphorylation and cAMP/PKA/phosphorylated CREB (pCREB) signaling pathway activity were measured in NAc tissues, and Ca2+ influx and pCaMKIIα levels were measured in cultured NAc neurons. We found that CART attenuated the caffeine-mediated enhancement of depolarization-induced Ca2+ influx and CaMKIIα phosphorylation in cultured NAc neurons. Repeated microinjection of CART peptides into the NAc decreased the caffeine-induced enhancement of Ca2+ channels activity, pCaMKIIα levels, the pCaMKIIα-D3R interaction, D3R phosphorylation, cAMP levels, PKA activity and pCREB levels in the NAc. Furthermore, behavioral sensitization was observed in rats that received five-day administration of caffeine following microinjection of saline but not in rats that were treated with caffeine following microinjection of CART peptide. These results suggest that caffeine-induced CREB phosphorylation in the NAc was ameliorated by CART peptide due to its inhibition of D3R phosphorylation. These effects of CART peptides may play a compensatory role by inhibiting locomotor behavior in rats. © 2016 Fu et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.


Gan X.,Jiangxi Provincial Peoples Hospital | Liu Z.,Jiangxi Tumor Hospital | Tong B.,Nanchang University | Zhou J.,Jiangxi Tumor Hospital
Tumor Biology | Year: 2015

Integrin, beta-like 1 (ITGBL1), is a β-integrin-related extracellular matrix protein which contains ten EGF-like repeats domain. Surprisingly, we screen Oncomine Database and found that ITGBL1 is more commonly downregulated in non-small cell lung cancer (NSCLC) tissues, and the result reminds us to explore its significance in NSCLC. Thus, we retrieved DRUGSURV Database and found that downregulated ITGBL1 predicts a poor prognosis of patients. These results provided us the clues that ITGBL1 might be a tumor suppressor in NSCLC. However, the biological functions of ITGBL1 have not been reported to date. In the current study, we surprisingly found that knockdown of ITGBL1 in NSCLC cell lines could promote cancer cell migration and invasion. Furthermore, recombinant ITGBL1 protein-treated cancer cell could inhibit cell migration and invasion. These results suggested that ITGBL1 plays a suppressive role in NSCLC progression. We further found that the downregulation of ITGBL1 might result from highly expressed miR-576-5p in NSCLC tissues, and the activity of Wnt/PCP signaling was enhanced when the level of ITGBL1 was inhibited. In conclusion, our results suggest that ITGBL1 is a novel tumor suppressor in NSCLC progression. © 2015 International Society of Oncology and BioMarkers (ISOBM)


PubMed | Jiangxi Provincial Peoples Hospital, Nanchang University and Jiangxi Tumor Hospital
Type: Journal Article | Journal: Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine | Year: 2016

Integrin, beta-like 1 (ITGBL1), is a -integrin-related extracellular matrix protein which contains ten EGF-like repeats domain. Surprisingly, we screen Oncomine Database and found that ITGBL1 is more commonly downregulated in non-small cell lung cancer (NSCLC) tissues, and the result reminds us to explore its significance in NSCLC. Thus, we retrieved DRUGSURV Database and found that downregulated ITGBL1 predicts a poor prognosis of patients. These results provided us the clues that ITGBL1 might be a tumor suppressor in NSCLC. However, the biological functions of ITGBL1 have not been reported to date. In the current study, we surprisingly found that knockdown of ITGBL1 in NSCLC cell lines could promote cancer cell migration and invasion. Furthermore, recombinant ITGBL1 protein-treated cancer cell could inhibit cell migration and invasion. These results suggested that ITGBL1 plays a suppressive role in NSCLC progression. We further found that the downregulation of ITGBL1 might result from highly expressed miR-576-5p in NSCLC tissues, and the activity of Wnt/PCP signaling was enhanced when the level of ITGBL1 was inhibited. In conclusion, our results suggest that ITGBL1 is a novel tumor suppressor in NSCLC progression.


PubMed | Nanchang University, Chungbuk National University and Jiangxi Tumor Hospital
Type: Journal Article | Journal: PloS one | Year: 2016

The purpose of this study was to characterize the inhibitory modulation of cocaine- and amphetamine-regulated transcript (CART) peptides, particularly with respect to the function of the D3 dopamine receptor (D3R), which is activated by its interaction with phosphorylated CaMKII (pCaMKII) in the nucleus accumbens (NAc). After repeated oral administration of caffeine (30 mg/kg) for five days, microinjection of CART peptide (0.08 M/0.5 l/hemisphere) into the NAc affected locomotor behavior. The pCaMKII-D3R interaction, D3R phosphorylation and cAMP/PKA/phosphorylated CREB (pCREB) signaling pathway activity were measured in NAc tissues, and Ca2+ influx and pCaMKII levels were measured in cultured NAc neurons. We found that CART attenuated the caffeine-mediated enhancement of depolarization-induced Ca2+ influx and CaMKII phosphorylation in cultured NAc neurons. Repeated microinjection of CART peptides into the NAc decreased the caffeine-induced enhancement of Ca2+ channels activity, pCaMKII levels, the pCaMKII-D3R interaction, D3R phosphorylation, cAMP levels, PKA activity and pCREB levels in the NAc. Furthermore, behavioral sensitization was observed in rats that received five-day administration of caffeine following microinjection of saline but not in rats that were treated with caffeine following microinjection of CART peptide. These results suggest that caffeine-induced CREB phosphorylation in the NAc was ameliorated by CART peptide due to its inhibition of D3R phosphorylation. These effects of CART peptides may play a compensatory role by inhibiting locomotor behavior in rats.


Gao Z.,University of Chinese Academy of Sciences | Gao Z.,Wuhan University | Zhang H.,University of Chinese Academy of Sciences | Hu F.,Wuhan Brain Hospital | And 6 more authors.
Cellular Signalling | Year: 2016

Whether the two N-linked glycans are important in prion, PrP, biology is unresolved. In Chinese hamster ovary (CHO) cells, the two glycans are clearly not important in the cell surface expression of transfected human PrP. Compared to fully-glycosylated PrP, glycan-deficient PrP preferentially partitions to lipid raft. In CHO cells glycan-deficient PrP also interacts with glycosaminoglycan (GAG) and vascular endothelial growth factor receptor 2 (VEGFR2), resulting in VEGFR2 activation and enhanced Akt phosphorylation. Accordingly, CHO cells expressing glycan-deficient PrP lacking the GAG binding motif or cells treated with heparinase to remove GAG show diminished Akt signaling. Being in lipid raft is critical, chimeric glycan-deficient PrP with CD4 transmembrane and cytoplasmic domains is absent in lipid raft and does not activate Akt signaling. CHO cells bearing glycan-deficient PrP also exhibit enhanced cellular adhesion and migration. Based on these findings, we propose a model in which glycan-deficient PrP, GAG, and VEGFR2 interact, activating VEGFR2 and resulting in changes in cellular behavior. © 2016 Elsevier Inc..


PubMed | Jiangxi Tumor Hospital, CAS Wuhan Institute of Virology, Wuhan Brain Hospital, University of Chinese Academy of Sciences and 2 more.
Type: Journal Article | Journal: Cellular signalling | Year: 2016

Whether the two N-linked glycans are important in prion, PrP, biology is unresolved. In Chinese hamster ovary (CHO) cells, the two glycans are clearly not important in the cell surface expression of transfected human PrP. Compared to fully-glycosylated PrP, glycan-deficient PrP preferentially partitions to lipid raft. In CHO cells glycan-deficient PrP also interacts with glycosaminoglycan (GAG) and vascular endothelial growth factor receptor 2 (VEGFR2), resulting in VEGFR2 activation and enhanced Akt phosphorylation. Accordingly, CHO cells expressing glycan-deficient PrP lacking the GAG binding motif or cells treated with heparinase to remove GAG show diminished Akt signaling. Being in lipid raft is critical, chimeric glycan-deficient PrP with CD4 transmembrane and cytoplasmic domains is absent in lipid raft and does not activate Akt signaling. CHO cells bearing glycan-deficient PrP also exhibit enhanced cellular adhesion and migration. Based on these findings, we propose a model in which glycan-deficient PrP, GAG, and VEGFR2 interact, activating VEGFR2 and resulting in changes in cellular behavior.


Zhang R.,Jiangxi University of Traditional Chinese Medicine | Liu J.-Q.,Jiangxi University of Traditional Chinese Medicine | Liu L.-Y.,Jiangxi Tumor Hospital | Xue P.,Jiangxi University of Traditional Chinese Medicine
Chinese Traditional and Herbal Drugs | Year: 2010

Objective: To establish a separation method of tricin reference substance from Bambusa textilis. Methods: After extracted with ethyl acetate, the extract of B. textilis was isolated and purified by silica gel column chromatography and preparative HPLC. Tricins were identified by melting point, UV, and IR spectroscopy. Results: The content of tricin was over 98% by normalization method of HPLC. Conclusion: The developed method is simple with lower cost, by which tricin can be used as reference substances for the qualitative and quantitative analyses of Chinese herbal medicine.

Loading Jiangxi Tumor Hospital collaborators
Loading Jiangxi Tumor Hospital collaborators