Recombinant Human Cell Division Cycle 25A CDC25A
- Known as:
- Recombinant Human Cell Division Cycle 25A CDC25A
- Catalog number:
- enz-091
- Product Quantity:
- 1
- Category:
- -
- Supplier:
- Prospecbio
- Gene target:
- Recombinant Human Cell Division Cycle 25A CDC25A
Related genes to: Recombinant Human Cell Division Cycle 25A CDC25A
- Gene:
- CDC25A NIH gene
- Name:
- cell division cycle 25A
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 3p21.31
- Locus Type:
- gene with protein product
- Date approved:
- 1992-07-31
- Date modifiied:
- 2017-12-06
Related products to: Recombinant Human Cell Division Cycle 25A CDC25A
Related articles to: Recombinant Human Cell Division Cycle 25A CDC25A
- The review covers research on dual-target antitumor agents over the past five years. One of the targets is histone deacetylases (HDACs), while the second potential target is a protein group located both on the membrane surface (phosphatidylinositol 3-kinase (PI3K), anaplastic lymphoma kinase (ALK), receptor tyrosine kinase (AXL), tyrosine protein kinase (HER2), FMS-like tyrosine kinase (FLT3), and vascular endothelial growth factor receptor (VEGFR2)) and in the nucleus (serine/threonine protein kinase Wee1, DNA methyltransferase (DNMT), dual-specificity phosphatase (CDC25A), an enzyme from the cyclin-dependent kinase family (CDK9), dual-specificity tyrosine-serine/threonine kinase (DYRK2), and BET family proteins (BRD4, BD1, and BD2)). This review presents the results of studies on the inhibitory activity of various HDAC isoforms and other enzymes, as well as in vitro cytotoxicity studies on both neoplastic and healthy cells. It also includes selectivity studies, in vivo experiments (changes in tumor volume in mice) and oral bioavailability assessments. The review also describes the chemical structures of several dual-target agents and identifies the molecular fragments responsible for inhibiting different targets. Based on the studies reviewed in this paper, it can be concluded that some dual inhibitors have superior in vitro cytotoxicity and exhibit selectivity towards some tumor cells compared to monofunctional reference compounds. These findings may be useful for molecular design in the field of polypharmacology, with the aim of developing new dual-target molecules that exhibit improved antitumor activity and selectivity towards neoplastic cells. - Source: PubMed
Publication date: 2026/07/24
Yudaev PavelAleksandrova YuliaNeganova Margarita - Hepatocellular carcinoma (HCC) is a leading cause of cancer death, yet immune checkpoint inhibitors (ICIs) benefit only a minority of patients-a limitation attributed to low tumor mutational burden (TMB) and an immunologically cold microenvironment. SMG1, a serine/threonine kinase of the phosphatidylinositol 3-kinase-related kinase (PIKK) superfamily, sits at the intersection of RNA surveillance, the DNA damage response, and oncogenic signaling. As the master kinase of nonsense-mediated mRNA decay (NMD), SMG1 phosphorylates UPF1 to degrade transcripts bearing premature termination codons; independently, it restrains tumor growth by phosphorylating p53 (Ser15) and promoting Cdc25A turnover. SMG1 was originally identified as a tumor-suppressive modulator of sorafenib resistance in HCC (Nam, S.W. et al., 2014), and subsequent work shows SMG1 is reduced in HCC, predicts adverse outcome, and is recurrently silenced by reversible promoter hypermethylation. Paradoxically, the same kinase conceals mutation-derived neoantigens, and its selective inhibition (e.g., KVS0001) raises HLA class I neoantigen presentation toward high-TMB levels and improves checkpoint-inhibitor efficacy in preclinical and liver-specific models. This critical review integrates SMG1 structural biology, clinicopathology, signaling, sorafenib resistance, and NMD-directed immunotherapy, grading established versus inferential mechanisms, and nominates SMG1 and NMD as dual, context-dependent targets for HCC precision oncology. - Source: PubMed
Publication date: 2026/07/31
Nam Soon Woo - Protein phosphatase PP2A-the most abundant Ser/Thr phosphatase in cells-is a heterotrimeric holoenzyme comprising a catalytic subunit, a scaffold subunit, and a regulatory subunit. The B55 regulatory subunit is primarily localized in the cytoplasm, where it provides a surface for recruiting substrates and regulatory proteins to the PP2A:B55 holoenzyme. SERTAD family proteins-SERTAD1, SERTAD2, SERTAD3, SERTAD4, and CDCA4-share a SERTA domain that binds to the B55 subunit. In this study, we aimed to demonstrate that SERTAD proteins function as substrate adapters and induce dephosphorylation at Ser178 of CDC25A, which is crucial for activating cyclin-dependent kinases. The conserved properties of SERTAD proteins-namely, nuclear localization and B55-binding-are necessary for the dephosphorylation of nuclear CDC25A and the subsequent dissociation of the inhibitory protein 14-3-3. Structural modeling and mutational analysis further revealed that the SERTA/B55-binding domain interacts directly with CDC25A, positioning its Ser178 close to the active site of PP2A:B55. Collectively, these results suggested that the SERTA/B55-binding domain provides a new surface for substrate binding. - Source: PubMed
Publication date: 2026/07/22
Yano KoyoSugiyama HarukaNakada TaiseiYoshii YutoSakurai Hiroshi - Colorectal cancer (CRC) is one of the global health issues. Current treatments still present major challenges such as off-target cytotoxicity and the emergence of drug resistance, the development of potent and innovative therapeutics is urgently needed. Here, we synthesized copper‑aluminum (CuAl) layered double hydroxides (LDH) using a hydrothermal method and loaded them with the 5-fluorouracil (5-FU) (CuAl-5FU) to improve their anticancer efficacy. The LDHs were 2D-sheeted and rosette-like in shape. The hydrodynamic diameter of CuAl and CuAl-5FU was 568 and 661 nm, respectively. Zeta potential values of CuAl-5FU ranged from +31.39 to +34.93 mV across pH 3 to 9, indicating good colloidal stability. The drug loading and encapsulation efficiency were 18.19% and 36.37%, respectively. Dose-dependent cytotoxicity was seen in HCT-116 and HT-29 CRC cells. Comparatively, CuAl-5FU LDH exhibited greater anticancer activity compared to LDH alone and free 5-FU drug in both monolayer and tumor spheroid models. Mechanistic studies revealed that CuAl-5FU significantly induced reactive oxygen species (ROS) production, mitochondrial membrane depolarization, and promoted apoptosis by upregulating the pro-apoptotic Bax protein and PARP cleavage in both CRC cells. Transcriptomic analysis and qPCR validation revealed the downregulation of oncogenic MAPK signaling and modulation of key genes related to proliferation (JUN, DUSP1, FOSB, EGR1, and FOS), apoptosis (TP53I3, ZMAT3, GADD45A, BBC3, MDM2, TNFRSF10B, E2F1, and ORC1), and cell cycle arrest (CDKN1A and CDC25A). Notably, we identified altered expression of several chemoresistance-related genes (AVPI1, HROB, DDIAS, PTGES, and LAMA3), suggesting the early emergence of adaptive responses in CRC cells. To validate this observation, CuAl-5FU-resistant HCT-116 G3 and HT-29 G2 cell lines were established and their chemoresistant phenotypes were characterized. Indeed, the chemoresistance-associated genes were upregulated, together with significantly higher IC values and clonogenic survival fractions than their respective parental cells. Collectively, these findings suggest that CuAl-5FU improves anticancer activity in CRC cells by modulating multiple genes involved in ROS production, mitochondrial membrane depolarization, apoptosis, and cell cycle regulation. Nevertheless, chemoresistance developed rapidly following repeated treatment, highlighting a potential limitation of this therapeutic approach. Overall, this study provides a new potential strategy for CRC treatment while emphasizing the importance of elucidating the molecular mechanisms underlying acquired chemoresistance. Future studies should also optimize the physicochemical properties of the CuAl-5FU LDH, particularly the large particle size (∼661 nm) by optimizing the hydrothermal synthesis conditions and incorporating surface modifications to further improve the tumor penetration and drug delivery. - Source: PubMed
Publication date: 2026/07/10
Yin YingShi JiayanLu DingyiWang YueranXiang XuemianLiu RuohanHu ZhantuBahadur AliArtoadi Muhammad IdrusZheng ChenxiaoShameli KamyarZhang XiaodongTeow Sin-Yeang - Molecular and functional networks driving coordination between cell cycle and mRNA translation remain to be explored. Here, we use mass spectrometry-based proteomics to comprehensively investigate the interactome and phosphoproteome of the cell cycle regulator CDC25A. We identify actors of mRNA regulation, such as RNA-binding proteins and translation factors, as interacting partners of CDC25A. CDC25A overexpression increases global translation, whereas catalytic inactivation or pharmacological inhibition decreases protein synthesis. A Cyclin-Dependent Kinase (CDK) interaction-deficient mutant of CDC25A also enhances translation, indicating a CDK-independent role. Our results further reveal an interplay between CDC25A and CDC25B whereby downregulation of CDC25A leads to compensatory overexpression of CDC25B. The roles of CDC25A and CDC25B in mRNA translation are independent of their roles in the cell cycle, with CDC25A possibly regulating translation elongation and CDC25B rather involved in initiation. In acute myeloid leukemia cells, CDC25A depletion also inhibits translation, suggesting its potential relevance as a therapeutic target. We propose that CDC25 phosphatases might be signaling platforms coordinating cell cycle progression with protein synthesis. - Source: PubMed
Publication date: 2026/07/14
Shin SauyeunCargnello MariePinchedé LisaMedale Giamarchi ClaireVillette CléaGay AlexandreSalnot VirginieGautier Emilie-FleurDassi ErikMillevoi StefaniaCammas AnneManenti Stéphane