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1.
Journal of China Medical University ; (12): 711-714, 2016.
Article in Chinese | WPRIM | ID: wpr-492779

ABSTRACT

Objective To detect the presence of DEK protein in the tissue and voided urine of patients with bladder urothelial carcinoma ,and an?alyze the relationship between DEK protein and clinical pathological classification of bladder cancer. Methods The expression of DEK protein was examined by immunohistochemistry in 48 bladder cancer tissues and 18 adjacent normal tissues(control group). The presence of DEK protein in voided urine was analyzed by western blot in 28 bladder cancer patients and 6 healthy individuals(control group). Results The positive ex?pression of DEK protein in bladder tumor tissues(73%)is higher than in adjacent normal tissues(33%,P<0.05). The expression of DEK in su?perficial bladder cancer(86%)was found higher than invasive bladder cancer(55%)with significant differences(P<0.05). The expression of DEK in urine samples of bladder cancer patients(0.834)was found higher than control group(0.242,P<0.05);Compared with the DEK expres?sion of control group,the sensitivity of diagnosis of bladder cancer with voided urine could be 82.1%. Conclusion DEK protein positive ex?pressed in tissues and voided urine of patients with bladder urothelial carcinoma. The expression was correlated with pathological classification of bladder cancer. The positive rate of DEK expression in early stage of tumor tissues is higher than late stage. The presence of DEK protein in tissues and voided urine can be considered as a suitable biomarker for bladder cancer potentially.

2.
China Biotechnology ; (12)2006.
Article in Chinese | WPRIM | ID: wpr-686322

ABSTRACT

DEK protein's carboxy-terminal DNA-binding region(CBD)is a newly found DNA-binding domain of DEK,which contains several phosphorylation sites and has a close correlation with DEK protein's function in vivo and in vitro.Using prokaryotic expression system,the peptide of DEK protein's carboxy-terminal DNA-binding region(CDB)was expressed and purified.In detail,the CDB DNA fragment was constructed into pET-30a(+)vector,and E.coli BL21(DE3)competent cells were used as host cells.The fusion protein His-CBD was expressed by induction of IPTG and purified by Ni-NTA agarose.The result of SDS-PAGE showed that the molecular weight of the purified protein was about 10.7kDa.Electrophoretic mobility shift assay(EMSA)indicated that DEK-CDB prefered to bind to supercoiled form of DNA in vitro,it had similar character to the binding of whole length DEK protein with DNA.This suggested that the carboxy-terminal DNA-binding region of DEK protein might function on the binding of DEK protein to DNA partly.

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