Antitumor effect of F-PBFβ-TrCP-induced targeted PTTG1 degradation in HeLa cells

Mo, Zhuohua; Zu, Xuyu; Xie, Zhizhong; Li, Wenpeng; Ning, Hang; Jiang, Yuyang; Xu, Wei

doi:10.1016/j.jbiotec.2008.09.004

Cited by 9 publications

(5 citation statements)

References 31 publications

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“…Interestingly, similar effect of regulation of PTTG1IP expression by phosphorylation has been observed in breast cancer cells [ 20 ]. Moreover, decreased cell growth has been demonstrated in HeLa cells when securin expression has been suppressed by a PTTG1IP combined with the F-box motive of β-TrCP [ 21 ].…”

Section: Discussionmentioning

confidence: 99%

PTTG1-interacting protein (PTTG1IP/PBF) predicts breast cancer survival

et al. 2017

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BackgroundPTTG1-interacting protein (PTTG1IP) is an oncogenic protein, which participates in metaphase-anaphase transition of the cell cycle through activation of securin (PTTG1). PTTG1IP promotes the shift of securin from the cell cytoplasm to the nucleus, allowing the interaction between separase and securin. PTTG1IP overexpression has been previously observed in malignant disease, e.g. in breast carcinoma. However, the prognostic value of PTTG1IP in breast carcinoma patients has not previously been revealed.MethodsA total of 497 breast carcinoma patients with up to 22-year follow-up were analysed for PTTG1IP and securin immunoexpression. The results were evaluated for correlations with the clinical prognosticators and patient survival.ResultsIn our material, negative PTTG1IP immunoexpression predicted a 1.5-fold risk of breast cancer death (p = 0.02). However, adding securin immunoexpression to the analysis indicated an even stronger and independent prognostic power in the patient material (HR = 2.5, p < 0.0001). The subcellular location of securin was found with potential prognostic value also among the triple-negative breast carcinomas (n = 96, p = 0.052).ConclusionsPTTG1IP-negativity alone and in combination with high securin immunoexpression indicates a high risk of breast cancer death, resulting in up to 14-year survival difference in our material.

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Section: Discussionmentioning

confidence: 99%

PTTG1-interacting protein (PTTG1IP/PBF) predicts breast cancer survival

et al. 2017

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“…The ubiquitin-proteasome dependent proteolysis is the important system in the control of protein degradation in cells [29]. The ubiquitination system is consisted of ubiquitin-activating enzymes (E1), ubiquitin-conjugating enzymes (E2), and ubiquitin-protein ligases (E3) [30,31], among which E3 is the specific enzyme for each degraded protein.…”

Section: Discussionmentioning

confidence: 99%

Berberine Suppresses Cyclin D1 Expression through Proteasomal Degradation in Human Hepatoma Cells

Wang

Tan

et al. 2016

IJMS

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The aim of this study is to explore the underlying mechanism on berberine-induced Cyclin D1 degradation in human hepatic carcinoma. We observed that berberine could suppress both in vitro and in vivo expression of Cyclin D1 in hepatoma cells. Berberine exhibits dose- and time-dependent inhibition on Cyclin D1 expression in human hepatoma cell HepG2. Berberine increases the phosphorylation of Cyclin D1 at Thr286 site and potentiates Cyclin D1 nuclear export to cytoplasm for proteasomal degradation. In addition, berberine recruits the Skp, Cullin, F-box containing complex-β-Transducin Repeat Containing Protein (SCFβ-TrCP) complex to facilitate Cyclin D1 ubiquitin-proteasome dependent proteolysis. Knockdown of β-TrCP blocks Cyclin D1 turnover induced by berberine; blocking the protein degradation induced by berberine in HepG2 cells increases tumor cell resistance to berberine. Our results shed light on berberine′s potential as an anti-tumor agent for clinical cancer therapy.

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“…This was accompanied by reduced FGF-2 expression, cell growth and ability to form colonies in soft agar (Ref. 139).…”

Section: Pttg and Pbf As Therapeutic Targetsmentioning

confidence: 99%

Pituitary tumor-transforming gene and its binding factor in endocrine cancer

Smith

Franklyn

McCabe

2010

Expert Rev. Mol. Med.

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The pituitary tumor-transforming gene (PTTG1) encodes a multifunctional protein (PTTG) that is overexpressed in numerous tumours, including pituitary, thyroid, breast and ovarian carcinomas. PTTG induces cellular transformation in vitro and tumourigenesis in vivo, and several mechanisms by which PTTG contributes to tumourigenesis have been investigated. Also known as the human securin, PTTG is involved in cell cycle regulation, controlling the segregation of sister chromatids during mitosis. This review outlines current information regarding PTTG structure, expression, regulation and function in the pathogenesis of neoplasia. Recent progress concerning the use of PTTG as a prognostic marker or therapeutic target will be considered. In addition, the PTTG binding factor (PBF), identified through its interaction with PTTG, has also been established as a proto-oncogene that is upregulated in several cancers. Current knowledge regarding PBF is outlined and its role both independently and alongside PTTG in endocrine and related cancers is discussed.

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Antitumor effect of F-PBFβ-TrCP-induced targeted PTTG1 degradation in HeLa cells

Cited by 9 publications

References 31 publications

PTTG1-interacting protein (PTTG1IP/PBF) predicts breast cancer survival

PTTG1-interacting protein (PTTG1IP/PBF) predicts breast cancer survival

Berberine Suppresses Cyclin D1 Expression through Proteasomal Degradation in Human Hepatoma Cells

Pituitary tumor-transforming gene and its binding factor in endocrine cancer

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