Comparative effects of overexpression of p27Kip1 and p21Cip1/Waf1 on growth and differentiation in human colon carcinoma cells

Yamamoto, Hideya; Soh, Jae-Won; Shirin, Haim; Wang, Xing; Lim, Jin T. E.; Yao, Yao; Slosberg, Eric D.; Tomita, Naohiro; Schieren, Ira; Weinstein, I. Bernard

doi:10.1038/sj.onc.1202269

Cited by 62 publications

(44 citation statements)

References 66 publications

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“…Most interesting is our observation that activation of PPARg in differentiated colon cells, where RB is almost absent, induces apoptosis. This mimics the in vivo situation, since PPARg is strongly expressed (Lefebvre et al, 1999) and RB is almost absent (Guy et al, 2001;Yamamoto et al, 1999) in differentiated epithelial cells found at the top of the villi in the colon. One of the consequences of the high ratio of PPARg to RB expression in the villi is the stimulation of apoptosis, which contributes to cell turn-over in normal colon.…”

Section: Pparg Rb and Apoptosismentioning

confidence: 99%

PPARγ controls cell proliferation and apoptosis in an RB-dependent manner

et al. 2003

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The nuclear receptor PPARc is implicated in the control of cell proliferation and apoptosis. However, the molecular mechanisms by which it controls these processes remain largely elusive. We show here that PPARc activation in the presence of the retinoblastoma protein (RB) results in the arrest of cells at the G1 phase of the cell cycle, whereas in the absence of RB, cells accumulate in G2/M, endoreduplicate, and undergo apoptosis. Through the use of HDAC inhibitors and coimmunoprecipitations, we furthermore demonstrate that the effects of RB on PPARc-mediated control of the cell cycle and apoptosis depend on the recruitment of histone deacetylase 3 (HDAC3) to PPARc. In combination, these data hence demonstrate that the effects of PPARc on cell proliferation and apoptosis are dependent on the presence of an RB-HDAC3 complex.

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Section: Pparg Rb and Apoptosismentioning

confidence: 99%

PPARγ controls cell proliferation and apoptosis in an RB-dependent manner

et al. 2003

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“…Western blot analysis was performed as described previously (Yamamoto et al, 1999). Briefly, the protein samples (50 mg) were separated using 10% polyacrylamide gel electrophoresis, followed by electroblotting onto a polyvinylidene difluoride membrane.…”

Section: Western Blot Analysismentioning

confidence: 99%

Expression of PPARδ in multistage carcinogenesis of the colorectum: implications of malignant cancer morphology

et al. 2006

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Whether peroxisome proliferator-activated receptor (PPAR) d is a good target for the chemoprevention and/or treatment of colorectal cancer (CRC) remains controversial. Our goal was to examine PPARd expression in multistage carcinogenesis of the colorectum and to assess the relevance of PPARd in CRC. Immunohistochemical analysis indicated that PPARd expression increased from normal mucosa to adenomatous polyps to CRC. In cancer tissues, the PPARd protein was accumulated only in those cancer cells with highly malignant morphology, as represented by a large-sized nucleus, round-shaped nucleus, and presence of clear nucleoli. Interestingly, the cancer tissue often contained both PPARd-positive and -negative areas, each retaining their respective specific morphological features. Moreover, this pattern persisted even when PPARd-positive and -negative cells were aligned next to each other within a single cancer nest or gland and was present in the majority of CRC cases. Immunohistochemistry for Ki-67 proliferation marker showed no significant correlation between Ki-67 and PPARd in CRC samples. Based on Western blot analysis and quantitative RT -PCR, high PPARd protein expression correlated with high PPARd mRNA levels. Peroxisome proliferator-activated receptor d may have a supporting role in tumorigenesis, and the close association between PPARd expression and malignant morphology of CRC cells suggests a pivotal role in cancer tissue.

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“…In the present study, we characterized CacyBP/SIP expression at the mRNA and protein levels in six gastric cancer cell lines and showed that it was expressed at different levels and that the level of expression was positively correlated with the differentiation status of the gastric cancer cells. Many studies have shown that poorly differentiated tumors have an increased growth rate and unfavorable prognosis (19,20), indicating that the level of expression of CacyBP/SIP may be associated with the growth of gastric cancer cells.…”

Section: The Expression Of B-catenin In Transfectantsmentioning

confidence: 99%

Calcyclin-Binding Protein Inhibits Proliferation, Tumorigenicity, and Invasion of Gastric Cancer

Ning¹,

Sun

Li³

et al. 2007

Molecular Cancer Research

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Calcyclin-binding protein/Siah-1 -interacting protein (CacyBP/SIP), a target protein of the S100 family, which includes S100A6, S100A1, S100A12, S100B, and S100P, has been identified as a component of a novel ubiquitinylation complex leading to B-catenin degradation. However, the function of CacyBP/SIP in gastric cancer has not been elucidated. In the present study, we prepared CacyBP/SIP overexpressing and knockdown cell lines of gastric cancer. Forced CacyBP/SIP expression inhibited the proliferation of gastric cancer cells, suppressed tumorigenicity in vitro, and prolonged the survival time of tumor-bearing nude mice. In addition, increased CacyBP/SIP repressed the invasive potential of gastric cancer cells. Conversely, the down-regulation of CacyBP/SIP by RNA interference showed the opposite effects. Further studies showed that depressed CacyBP/SIP increased the expression of total and nuclear B-catenin at the protein level and elevated the transcriptional activity of Tcf/LEF. Taken together, our results suggest that CacyBP/SIP may be a potential inhibitor of cell growth and invasion in the gastric cancer cell, at least in part through the effect on B-catenin protein expression and transcriptional activation of Tcf/LEF.

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Comparative effects of overexpression of p27Kip1 and p21Cip1/Waf1 on growth and differentiation in human colon carcinoma cells

Cited by 62 publications

References 66 publications

PPARγ controls cell proliferation and apoptosis in an RB-dependent manner

PPARγ controls cell proliferation and apoptosis in an RB-dependent manner

Expression of PPARδ in multistage carcinogenesis of the colorectum: implications of malignant cancer morphology

Calcyclin-Binding Protein Inhibits Proliferation, Tumorigenicity, and Invasion of Gastric Cancer

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