Upregulation of Survivin in G2/M Cells and Inhibition of Caspase 9 Activity Enhances Resistance in Staurosporine-Induced Apoptosis

Chandele, Anmol; Prasad, Vandna; Jagtap, Jayashree C.; Shukla, Ravi; Shastry, Padma

doi:10.1016/s1476-5586(04)80051-4

Cited by 95 publications

(74 citation statements)

References 32 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It is reported that Survivin has specific expression during G 2 /M phase of the cell cycle, followed by rapid decline of both mRNA and protein levels at the G 1 phase, and the protein has a half-life about 30 min [12]. Our study revealed that the expression of Survivin in G 2 /M phase was mostly higher among 3 phases, and S phase took the second place, then the G 0 /G 1 phase, which was consistent with the previous study [37][38]. Although LMP1 increase Survivin expression in all the 3 phases, it has more obviously effect on regulating the expression of Survivin in G 0 /G 1 and S phase, which suggested that Survivin may play unusual role in G 1 /S phase.…”

Section: Initiation Of Survivin/ Cdk4 Complex Formation In the Nucleisupporting

confidence: 91%

Regulation of Survivin and CDK4 by Epstein-Barr virus encoded latent membrane protein 1 in nasopharyngeal carcinoma cell lines

Zhao

et al. 2005

Cell Res

View full text Add to dashboard Cite

Latent membrane protein 1 (LMP1), an important protein encoded by Epstein Barr virus (EBV), has been implied to link with the pathogenesis of nasopharyngeal carcinoma (NPC). Its dual effects of increasing cell proliferation and inhibiting cell apoptosis have been confirmed. In this study, we showed that the expression of Survivin and CDK4 protein in CNE-LMP1, a LMP1 positive NPC epithelial cell line, is higher than in LMP1 negative NPC epithelial cell line-CNE1, and the expression is LMP1 dosage-dependent. Although it was reported that Survivin specifically expressed in cell cycle G 2 /M phase, our studies suggested that LMP1 could promote the expression of Survivin in G 0 /G 1 , S and G 2 / M phase. It also showed that Survivin and CDK4 could be accumulated more in the nuclei triggered by LMP1. More interestingly, Survivin and CDK4 could form a protein complex in the nuclei of CNE-LMP1 rather than in that of CNE1, which demonstrated that the interaction between these two proteins could be promoted by LMP1. These results strongly suggested that the role of LMP1 in the regulation of Survivin and CDK4 may also shed some light on the mechanism research of LMP1 in NPC.

show abstract

Section: Initiation Of Survivin/ Cdk4 Complex Formation In the Nucleisupporting

confidence: 91%

Regulation of Survivin and CDK4 by Epstein-Barr virus encoded latent membrane protein 1 in nasopharyngeal carcinoma cell lines

Zhao

et al. 2005

Cell Res

View full text Add to dashboard Cite

show abstract

“…However, our data ruled out this possibility. Survivin, a member of the inhibitor of apoptosis gene family, is expressed in a cell cycle-dependent manner, increasing in the G2/M phase of the cell cycle followed by a rapid decline in the G1 phase [26,27]. Recent studies have revealed that quercetin inhibits cell proliferation by causing cell cycle arrest in G2/M phase [28,29].…”

Section: Discussionmentioning

confidence: 99%

Quercetin augments TRAIL-induced apoptotic death: Involvement of the ERK signal transduction pathway

Kim

Lee

Jeong

et al. 2008

Biochemical Pharmacology

157

115

View full text Add to dashboard Cite

Combined treatment with quercetin and TRAIL induced cytotoxicity and enhanced annexin V staining and poly (ADP-ribose) polymerase (PARP) cleavage in human prostate cancer cell lines DU-145 and PC-3. These indicators of apoptosis resulted from the activation of caspase-8, -9, and -3. Although the expression levels of FLIPs, cIAP1, cIAP2, and the Bcl-2 family were not changed in quercetin-treated cells, significant downregulation of survivin occurred. Knockdown survivin by siRNA significantly increased TRAIL-induced apoptosis. We hypothesized that quercetin-induced activation of MAPK (ERK, p38, JNK) is responsible for downregulation of survivin gene expression. To test this hypothesis, we selectively inhibited MAPK during treatment with quercetin. Our data demonstrated that inhibitor of ERK (PD98059), but not p38 MAPK (SB203580) or JNK (SP600125), significantly maintained the intracellular level of survivin during treatment with quercetin. Interestingly, PD98059 also prevented quercetin-induced deacetylation of histone H3. Data from survivin promoter activity assay suggest that the Sp1 transcription factor binds to the survivin promoter region and quercetin inhibits its binding activity through deacetylation of histone H3. Quercetin-induced activation of the ERK-MSK1 signal transduction pathway may be responsible for deacetylation of histone H3. Taken together, our findings suggest that quercetin enhances TRAIL induced apoptosis by inhibition of survivin expression, through ERK-MSK1-mediated deacetylation of H3.

show abstract

“…In particular, downregulation of the mitochondrial IAP antagonist Smac/DIABLO is associated with renal cell carcinomas, and overexpression of survivin, another IAP, has been observed in most transformed cell lines and cancers tested to date, as compared with its absence in most normal adult tissues. 12,13 Although there is evidence suggesting an indirect caspase-9 processing interference by survivin, 14 malfunctions of mitotic spindle checkpoint and aberrant progression of transformed cells may be due to non-apoptotic functions of this particular IAP. 15 Association between X-linked inhibitor of apoptosis protein (XIAP) overexpression and poor clinical outcome has been reported for both renal cell carcinomas and acute myelogenous leukemia (AML).…”

Section: Apoptosis As a Defense Strategy Against Tumorogenesismentioning

confidence: 99%

Caspases and cancer

2011

View full text Add to dashboard Cite

Evasion of apoptosis is considered to be one of the hallmarks of human cancers. This cell death modality is executed by caspases and several upstream regulatory factors, which direct their proteolytic activity, have been defined as either tumor suppressors or oncogenes. Often these regulatory factors, in addition to being potent apoptosis inducers, function in cell survival or repair signaling pathways in response to cellular stress. Thus, loss of function in a distinct regulatory mechanism does not necessarily mean that tumor formation is due to apoptosis malfunction resulting from insufficient caspase activation. Although each caspase has been assigned a distinct role in apoptosis, some redundancy with respect to their regulatory functions and substrate recognition is evident. Jointly, these proteases could be considered to possess solid tumor suppressor function, but what is the evidence that deregulation of specific caspases per se induces inappropriate cell survival, leading to enhanced tumorigenic potential? This question will be addressed in this review, which covers basic molecular mechanisms derived from in vitro analyses and emphasizes new insights that have emerged from in vivo and clinical studies. In organisms, excess cells during development, as well as potentially harmful cells resulting from pathophysiological conditions, are eliminated by various cell death modalities. Among them, apoptosis is the most investigated, and almost 40 years ago, it was described as a major defense strategy that prevents cells from acquiring tumorigenic potential. 1 This suicide mechanism is controlled by multiple and interrelated pathways ensuring that caspases, the proteolytic initiators and executioners of apoptosis, are triggered only in cells requiring termination. There is overwhelming experimental evidence supporting the idea that disturbances in the regulation of caspase activation are central for the avoidance of cancer cell death, both in vitro and in vivo. However, what evidences suggest that caspases per se act as tumor suppressors? It was reported that cells do not necessarily undergo caspaseindependent cell death in the absence of active caspases, but may instead survive insult and even promote clonogenic tumor growth. 2 Yet, it was unclear which individual caspases could fulfill this function. Recently, certain initiator caspases have been suggested as putative tumor suppressor genes. 3,4 This review is focusing on caspases and their role in tumor suppression, and emphasizing new evidences that have emerged from in vivo observations and clinical material, taking into consideration supporting in vitro data that has enlightened basic molecular mechanisms. CaspasesClassification of human caspases is based either on their function, the size of their pro-domain or cleavage specificity.Considering the first criteria, caspase-1, -4 and -5 belong to the group I (inflammatory) caspases that are involved in cytokine maturation. These proteases are primarily associated with the innate immunity against pathogens an...

show abstract

Upregulation of Survivin in G2/M Cells and Inhibition of Caspase 9 Activity Enhances Resistance in Staurosporine-Induced Apoptosis

Cited by 95 publications

References 32 publications

Regulation of Survivin and CDK4 by Epstein-Barr virus encoded latent membrane protein 1 in nasopharyngeal carcinoma cell lines

Regulation of Survivin and CDK4 by Epstein-Barr virus encoded latent membrane protein 1 in nasopharyngeal carcinoma cell lines

Quercetin augments TRAIL-induced apoptotic death: Involvement of the ERK signal transduction pathway

Caspases and cancer

Contact Info

Product

Resources

About