Expression of a murine homologue of the inhibitor of apoptosis protein is related to cell proliferation

Kobayashi, Koichi S.; Hatano, Masahiko; Otaki, Masayuki; Ogasawara, Takeshi; Tokuhisa, Takeshi

doi:10.1073/pnas.96.4.1457

Cited by 237 publications

(195 citation statements)

References 31 publications

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“…It is expressed during human foetal development, but not detectable in normal adult tissues, except in thymus and placenta. Its expression has been showed in several neoplasms, including pancreatic, gastric, colonic, lung, breast, prostatic and bladder cancers, neuroblastomas, and lymphomas (Adida et al, 1998a;Ambrosini et al, 1998;Kawasaki et al, 1998;Lu et al, 1998;Swana et al, 1999;Kobayashi et al, 1999).…”

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confidence: 99%

Nuclear and cytoplasmic expression of survivin in 67 surgically resected pancreatic cancer patients

et al. 2005

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Pancreatic cancer is one of the most aggressive gastrointestinal cancer with less than 10% long-term survivors. The apoptotic pathway deregulation is a postulated mechanism of carcinogenesis of this tumour. The present study investigated the prognostic role of apoptosis and apoptosis-involved proteins in a series of surgically resected pancreatic cancer patients. All patients affected by pancreatic adenocarcinoma and treated with surgical resection from 1988 to 2003 were considered for the study. Patients' clinical data and pathological tumour features were recorded. Survivin and Cox-2 expression were evaluated by immunohistochemical staining. Apoptotic cells were identified using the TUNEL method. Tumour specimen of 67 resected patients was included in the study. By univariate analysis, survival was influenced by Survivin overexpression. The nuclear Survivin overexpression was associated with better prognosis (P ¼ 0.0009), while its cytoplasmic overexpression resulted a negative prognostic factor (P ¼ 0.0127). Also, the apoptotic index was a statistically significant prognostic factor in a univariate model (P ¼ 0.0142). By a multivariate Cox regression analysis, both the nuclear (P ¼ 0.002) and cytoplasmic (P ¼ 0.040) Survivin overexpression maintained the prognostic statistical value. This is the first study reporting a statistical significant prognostic relevance of nuclear and cytoplasmic Survivin overexpression in pancreatic cancer. In particular, patients with high nuclear Survivin staining showed a longer survival, whereas patients with high cytoplasmic Survivin staining had a shorter overall survival.

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confidence: 99%

Nuclear and cytoplasmic expression of survivin in 67 surgically resected pancreatic cancer patients

et al. 2005

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“…7 Similar to oncofetal antigens, Survivin is strongly expressed in embryonic and fetal organs but is undetectable in most terminally differentiated normal tissues. 7,8,14,23,24 Moreover, genome-wide searches revealed Survivin to be the fourth top 'transcriptome' in various cancers, while remaining low or undetectable in the matched normal tissues. 25 A unique property of Survivin is a sharp cell-cycle-dependent expression at mitosis.…”

Section: Discussionmentioning

confidence: 99%

Survivin expression is associated with bladder cancer presence, stage, progression, and mortality

Shariat

Ashfaq

Karakiewicz

et al. 2007

Cancer

136

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BACKGROUNDThe purpose was to compare the differential expression of Survivin in normal bladder tissue, bladder transitional cell carcinoma (TCC) of different stages, and to determine whether expression of Survivin is associated with TCC clinical outcomes.METHODSImmunohistochemical staining for Survivin was carried out on archival bladder specimens from 9 normal controls and 222 consecutive patients who underwent radical cystectomy and bilateral lymphadenectomy. Lymph node tissue involved with TCC from 50 of the 222 cystectomy patients was also evaluated.RESULTSSurvivin was expressed in none of the normal bladder specimens, 64% of the cystectomy specimens, and 94% of the malignant lymph nodes. Multivariable analyses performed in the cystectomy patients revealed that Survivin expression was associated with disease recurrence (P = .040), disease‐specific mortality (P = .037), and all‐cause mortality (P = .044).CONCLUSIONSThe findings of the study provide a rationale for further evaluation of Survivin and its downstream signaling pathways in bladder cancer and raise the potential for Survivin‐targeted therapy for bladder cancer. Cancer 2007. © 2007 American Cancer Society.

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“…Further analysis indicated that survivin can partially block activation of caspases and cell death induced by a variety of stimuli, such as Bax, Fas engagement, and etoposide [25]. This appears to be due to its ability to bind to activated caspases [25], [26]. Survivin expression is also closely connected with cell cycle.…”

Section: Iaps and Cell Cycle Controlmentioning

confidence: 99%

“…This is presumably due to failed cytokinesis, the process of separating a cell into two after it has duplicated its genetic material. It has also been shown that the murine homolog of survivin is highly expressed in thymocytes and induced in peripheral T cells upon activation [26], indicating that survivin is also associated with cell cycle progression in untransformed cells. In addition, C. elegans embryos that lack the survivin homologue bir-1 were unable to complete cytokinesis and became multinucleated [30].…”

Section: Iaps and Cell Cycle Controlmentioning

confidence: 99%

The IAP family: endogenous caspase inhibitors with multiple biological activities

2000

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IAPs (inhibitors of apoptosis) are a family of proteins containing one or more characteristic BIR domains. These proteins have multiple biological activities that include binding and inhibiting caspases, regulating cell cycle progression, and modulating receptor-mediated signal transduction. Our recent studies found the IAP family members XIAP and c-IAP1 are ubiquitinated and degraded in proteasomes in response to apoptotic stimuli in T cells, and their degradation appears to be important for T cells to commit to death. In addition to three BIR domains, each of these IAPs also contains a RING finger domain. We found this region confers ubiquitin protease ligase (E3) activity to IAPs, and is responsible for the auto-ubiquitination and degradation of IAPs after an apoptotic stimulus. Given the fact that IAPs can bind a variety of proteins, such as caspases and TRAFs, it will be of interest to characterize potential substrates of the E3 activity of IAPs and the effects of ubiquitination by IAPs on signal transduction, cell cycle, and apoptosis.

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Expression of a murine homologue of the inhibitor of apoptosis protein is related to cell proliferation

Cited by 237 publications

References 31 publications

Nuclear and cytoplasmic expression of survivin in 67 surgically resected pancreatic cancer patients

Nuclear and cytoplasmic expression of survivin in 67 surgically resected pancreatic cancer patients

Survivin expression is associated with bladder cancer presence, stage, progression, and mortality

The IAP family: endogenous caspase inhibitors with multiple biological activities

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