Transactivating effect of complete S protein of hepatitis B virus and cloning of genes transactivated by complete S protein using suppression subtractive hybridization technique

Bai, Guiqin; Liu, Yan; Cheng, Jun; Zhang, Shulin; Yue, Yafei; Huang, Yanping; Zhang, Liying

doi:10.3748/wjg.v11.i25.3893

Cited by 4 publications

(2 citation statements)

References 25 publications

(12 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…CSTP1 gene was first identified by Bai GQ in 2005 [15], which was transactived by complete S protein of hepatitis B virus, and we supposed it may be associated with human cancers. We first examined CSTP1 mRNA expression level in several kinds of human cancers, including liver, pancreas, stomach, colon, bladder and renal cancers.…”

Section: Resultsmentioning

confidence: 91%

“…Here, we reported a novel protein phosphatase, termed the complete s transactivated protein 1(CSTP1) [15], whose expression was selectively reduced in non-muscle invasive bladder cancers. To make a further understand of the significance of CSTP1 in bladder carcinogenesis, in this study, we will go deep insight into i. the effects of CSTP1 on bladder cancer cell cycle, apoptosis and tumor formation in vivo and the underlined molecular mechanisms; ii.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

CSTP1, a Novel Protein Phosphatase, Blocks Cell Cycle, Promotes Cell Apoptosis, and Suppresses Tumor Growth of Bladder Cancer by Directly Dephosphorylating Akt at Ser473 Site

et al. 2013

View full text Add to dashboard Cite

Akt/protein kinase B is a pivotal component downstream of phosphatidylinositol 3-kinase (PI3K) pathway, whose activity regulates the balance between cell survival and apoptosis. Phosphorylation of Akt occurs at two key sites either at Thr308 site in the activation loop or at Ser473 site in the hydrophobic motif. The phosphorylated form of Akt (pAkt) is activated to promote cell survival. The mechanisms of pAkt dephosphorylation and how the signal transduction of Akt pathway is terminated are still largely unknown. In this study, we identified a novel protein phosphatase CSTP1(complete s transactivated protein 1), which interacts and dephosphorylates Akt specifically at Ser473 site in vivo and in vitro, blocks cell cycle progression and promotes cell apoptosis. The effects of CSTP1 on cell survival and cell cycle were abrogated by depletion of phosphatase domain of CSTP1 or by expression of a constitutively active form of Akt (S473D), suggesting Ser473 site of Akt as a primary cellular target of CSTP1. Expression profile analysis showed that CSTP1 expression is selectively down-regulated in non-invasive bladder cancer tissues and over-expression of CSTP1 suppressed the size of tumors in nude mice. Kaplan-Meier curves revealed that decreased expression of CSTP1 implicated significantly reduced recurrence-free survival in patients suffered from non-invasive bladder cancers.

show abstract

Section: Resultsmentioning

confidence: 91%

Section: Introductionmentioning

confidence: 99%