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Zhong, Dong,Ran, Jian-Hua,Tang, Wen-Yuan,Zhang, Xiao-Dong,Tan, Yun,Chen, Gui-Jie,Li, Xiao-Song,Yan, Yi Asian Pacific Journal of Cancer Prevention 2012 Asian Pacific journal of cancer prevention Vol.13 No.6
Invasion is usually recognized as the main reason for the high recurrence and death rates of glioma and restricts the efficacy of surgery and other therapies. Therefore, we aimed to investigate the mechanism involved in promotion effects of mda-9/syntenin on human glioma cell migration. The wound healing method was used to test the migration ability of human glioma cells CHG-5 and CHG-hS, stably overexpressing mda-9/syntenin. Western blotting was performed to determine the expression and phosphorylation of focal adhesion kinase (FAK) and JNK in CHG-5 and CHG-hS cells. The migration ability of CHG-hS cells was significantly higher than that of CHG-5 cells in fibronectin (FN)-coated culture plates. Phosphorylation of FAK on tyrosine 397, 576, and 925 sites was increased with time elapsed in CHG-hS cells. However, phosphorylated FAK on the tyrosine 861 site was not changed. Phosphorylated Src, JNK and Akt levels in CHG-hS cells were also significantly upregulated. Phosphorylation of JNK and Akt were abolished by the specific inhibitors SP600125 and LY294002, respectively, and the migration ability of CHG-hS cells was decreased, indicating that the JNK and PI3K/Akt pathways play important roles in regulating mda-9/syntenin-induced human brain glioma migration. Our results indicate Mda-9/syntenin overexpression could activate FAK-JNK and FAK-Akt signaling and then enhance the migration capacity of human brain glioma cells.
( Jing Wu ),( Xin Yu Tan ),( Xiao Zhong Peng ),( Jian Gang Yuan ),( Bo Qin Qiang ) 생화학분자생물학회 2003 BMB Reports Vol.36 No.4
For better understanding of functions of the Calcyclin Binding Protein (CacyBP) and exploring its possible roles in neuronal differentiation, the subcellular localization of human CacyBP was examined in retinoic acid(RA)-induced and uninduced neuroblastoma SH-SY5Y cells. Immunostaining indicated that CacyBP was present in the cytoplasm of uninduced SH-SY5Y cells, in which the resting Ca^(2+) concentration was relatively lower than that of RA-induced cells. After the RA induction, immunostaining was seen in both the nucleus and cytoplasm. In the RA-induced differentiated SH-SYSY cells, CacyBP was phosphorylated on serine residue(s), while it existed in a dephosphorylated form in normal (uninduced) cells. Thus, the phosphorylation of CacyBP occurs when it is translocated to the nuclear region. The translocation of CacyBP during the RA-induced differentiation of SH-SY5Y cells suggested that this protein might play a role in neuronal differentiation.
The role of protein arginine-methyltransferase 1 in gliomagenesis
( Shan Wang ),( Xiao Chao Tan ),( Bin Yang ),( Bin Yin ),( Jian Gang Yuan ),( Bo Qin Qiang ),( Xiao Zhong Peng ) 생화학분자생물학회 2012 BMB Reports Vol.45 No.8
Protein arginine methyltransferase 1 (PRMT1), a type-I arginine methyltransferase, has been implicated in diverse cellular events. We have focused on the role of PRMT1 in gliomagenesis. In this study, we showed that PRMT1 expression was up-regulated in glioma tissues and cell lines compared with normal brain tissues. The knock-down of PRMT1 resulted in an arrest in the G1-S phase of the cell cycle, proliferation inhibition and apoptosis induction in four glioma cell lines (T98G, U87MG, U251, and A172). Moreover, an in vivo study confirmed that the tumor growth in nude mouse xenografts was significantly decreased in the RNAi-PRMT1 group. Additionally, we found that the level of the asymmetric dimethylated modification of H4R3, a substrate of PRMT1, was higher in glioma cells than in normal brain tissues and decreased after PRMT1 knock-down. Our data suggest a potential role for PRMT1 as a novel biomarker of and therapeutic target in gliomas. [BMB Reports 2012; 45(8): 470-475]
Zhi-PingWu,Yan-Yan Liu,Guo-Qiang Chen,Ting-LiangWang,Jian-Zhong Tan 한국응용곤충학회 2014 Journal of Asia-Pacific Entomology Vol.17 No.1
The silkworm fat body is the site of many intermediary metabolic processes, and a source of sustenance forgrowth throughout the life cycle. Fat body proteins are responsible for storing nutrients, providing energy, andregulating hormones, and they have been identified using proteomic approaches. However, detailed differentialexpression of sex-related fat body proteins has not previously been evaluated. In the present study, we characterizedthe differential expression of sex-related fat body proteins, by using 2-dimensional gel electrophoresis(2-DE) followed bymass spectrometry identification and bioinformaticsmethods.We extracted the fat body proteinsfrom 5-day-old fifth instar larvae (L5), 10-day-old fifth instar larvae (corresponding to the end of spinning[LE]), and 0-day-old pupae (P0) of the multivoltine silkworm variety “Da Zao”. We confirmed the presence of 11important sex-specific expression proteins and 14 stage-specific expression proteins.We accurately identified 13of these specific expression proteins, including actin, calponin-like protein, 75 kDa subunit NADH, receptor foractivated protein kinase C from Bombyx mori (BmRACK), IMP (inosine monophosphate) cyclohydrolase, tropomyosin1, β-tubulin, hypothetical protein, antichymotrypsin precursor, and 30 K protein precursor.We showedthat BmRACK was differentially expressed betweenmale and female silkworms.Wediscuss the biological roles ofthe specific expression proteins during the larval–pupal developmental stages.
TC1 (C8orf4) is involved in ERK1/2 pathway-regulated G1-to S-phase transition
( Yi Dong Wang ),( Guo Hui Bian ),( Xiao Yan Lv ),( Rong Zheng ),( Huan Sun ),( Zheng Zhang ),( Ye Chen ),( Qin Wei Li ),( Yan Xiao ),( Qiu Tan Yang ),( Jian Zhong Ai ),( Yu Quan Wei ),( Qin Zhou ) 생화학분자생물학회 2008 BMB Reports Vol.41 No.10