scholarly journals Inhibition of Plk1 and Cyclin B1 Expression Results in Panobinostat-Induced G2 Delay and Mitotic Defects

2013 ◽  
Vol 3 (1) ◽  
Author(s):  
Michael Prystowsky ◽  
Katherine Feeney ◽  
Nicole Kawachi ◽  
Cristina Montagna ◽  
Michelle Willmott ◽  
...  
Keyword(s):  
Cyclin B1 ◽  
G2 Delay

scholarly journals Cdc25B cooperates with Cdc25A to induce mitosis but has a unique role in activating cyclin B1–Cdk1 at the centrosome

2005 ◽  
Vol 171 (1) ◽  
pp. 35-45 ◽  
Author(s):  
Arne Lindqvist ◽  
Helena Källström ◽  
Andreas Lundgren ◽  
Emad Barsoum ◽  
Christina Karlsson Rosenthal
Keyword(s):  
Chromatin Condensation ◽  
Three Dimensional ◽  
Time Lapse ◽  
Cyclin B1 ◽  
Hek293 Cells ◽  
Unique Role ◽  
Mitotic Entry ◽  
Mitotic Cyclin ◽  
Interfering Rna ◽  
G2 Delay

Cdc25 phosphatases are essential for the activation of mitotic cyclin–Cdks, but the precise roles of the three mammalian isoforms (A, B, and C) are unclear. Using RNA interference to reduce the expression of each Cdc25 isoform in HeLa and HEK293 cells, we observed that Cdc25A and -B are both needed for mitotic entry, whereas Cdc25C alone cannot induce mitosis. We found that the G2 delay caused by small interfering RNA to Cdc25A or -B was accompanied by reduced activities of both cyclin B1–Cdk1 and cyclin A–Cdk2 complexes and a delayed accumulation of cyclin B1 protein. Further, three-dimensional time-lapse microscopy and quantification of Cdk1 phosphorylation versus cyclin B1 levels in individual cells revealed that Cdc25A and -B exert specific functions in the initiation of mitosis: Cdc25A may play a role in chromatin condensation, whereas Cdc25B specifically activates cyclin B1–Cdk1 on centrosomes.

scholarly journals Decreased cyclin B1 expression contributes to G2 delay in human brain tumor cells after treatment with camptothecin

2001 ◽  
Vol 3 (1) ◽  
pp. 11-21 ◽  
Author(s):  
Anna J. Janss ◽  
Amit Maity ◽  
Cheng-Bi Tang ◽  
Ruth J. Muschel ◽  
W. Gillies McKenna ◽  
...  
Keyword(s):  
Brain Tumor ◽  
Human Brain ◽  
Tumor Cells ◽  
Cyclin B1 ◽  
Human Brain Tumor ◽  
Brain Tumor Cells ◽  
G2 Delay

scholarly journals G2 delay induced by nitrogen mustard in human cells affects cyclin A/cdk2 and cyclin B1/cdc2-kinase complexes differently.

1993 ◽  
Vol 268 (11) ◽  
pp. 8298-8308
Author(s):  
P.M. O'Connor ◽  
D.K. Ferris ◽  
M. Pagano ◽  
G. Draetta ◽  
J. Pines ◽  
...  
Keyword(s):  
Nitrogen Mustard ◽  
Cyclin A ◽  
Cyclin B1 ◽  
Human Cells ◽  
Cdc2 Kinase ◽  
G2 Delay

654: Mitotic Catastrophe Marker Cyclin B1 in Renal Cell Carcinoma Correlates with Stage Metastasis and Survival of Patients

2005 ◽  
Vol 173 (4S) ◽  
pp. 178-178
Author(s):  
Stephen O. Ikuerowo ◽  
Stefan A. Machtens ◽  
Markus A. Kuczyk ◽  
Udo Jonas ◽  
Juergen Serth
Keyword(s):  
Renal Cell Carcinoma ◽  
Cell Carcinoma ◽  
Renal Cell ◽  
Cyclin B1 ◽  
Mitotic Catastrophe

Downregulation of cyclin B1 inhibits proliferation of breast cancer cells

2005 ◽  
Vol 127 (04) ◽  
Author(s):  
J Yuan ◽  
I Androic ◽  
A Kraemer ◽  
M Kaufmann ◽  
K Strebhardt
Keyword(s):  
Breast Cancer ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Cyclin B1

TARGETING CYCLIN B1 WITH ANTISENSE OLIGONUCLETOTIDES- COATED SUPERPARAMAGNETIC IRON OXIDE NANOPARTICLES

2018 ◽  
Vol 6 (10) ◽  
Author(s):  
Hosam Zaghloul ◽  
Doaa A. Shahin ◽  
Ibrahim El- Dosoky ◽  
Mahmoud E. El-awady ◽  
Fardous F. El-Senduny ◽  
...  
Keyword(s):  
Iron Oxide ◽  
Iron Oxide Nanoparticles ◽  
Cellular Uptake ◽  
Superparamagnetic Iron Oxide ◽  
Cyclin B1 ◽  
Superparamagnetic Iron Oxide Nanoparticles ◽  
Oxide Nanoparticles ◽  
Mcf7 Cells ◽  
M Phase ◽  
The Impact

Antisense oligonucleotides (ASO) represent an attractive trend as specific targeting molecules but sustain poor cellular uptake meanwhile superparamagnetic iron oxide nanoparticles (SPIONs) offer stability of ASO and improved cellular uptake. In the present work we aimed to functionalize SPIONs with ASO targeting the mRNA of Cyclin B1 which represents a potential cancer target and to explore its anticancer activity. For that purpose, four different SPIONs-ASO conjugates, S-M (1–4), were designated depending on the sequence of ASO and constructed by crosslinking carboxylated SPIONs to amino labeled ASO. The impact of S-M (1–4) on the level of Cyclin B1, cell cycle, ROS and viability of the cells were assessed by flowcytometry. The results showed that S-M3 and S-M4 reduced the level of Cyclin B1 by 35 and 36%, respectively. As a consequence to downregulation of Cyclin B1, MCF7 cells were shown to be arrested at G2/M phase (60.7%). S-M (1–4) led to the induction of ROS formation in comparison to the untreated control cells. Furthermore, S-M (1–4) resulted in an increase in dead cells compared to the untreated cells and SPIONs-treated cells. In conclusion, targeting Cyclin B1 with ASO-coated SPIONs may represent a specific biocompatible anticancer strategy.

Expression of histone H3, p53, cyclin D1, and cyclin B1 in oral mucosal lesions

2009 ◽  
Vol 13 (4) ◽  
pp. 119-126
Author(s):  
Yoshimitsu Bamba ◽  
Tetsunari Nishikawa ◽  
Akio Tanaka
Keyword(s):  
Cyclin D1 ◽  
Histone H3 ◽  
Cyclin B1 ◽  
Oral Mucosal Lesions ◽  
Mucosal Lesions

Activation of bovine oocytes by protein synthesis inhibitors: new findings on the role of MPF/MAPKs†

2021 ◽  
Author(s):  
Cecilia Valencia ◽  
Felipe Alonso Pérez ◽  
Carola Matus ◽  
Ricardo Felmer ◽  
María Elena Arias
Keyword(s):  
Protein Synthesis ◽  
Kinase Activity ◽  
Cyclin B1 ◽  
Protein Synthesis Inhibitors ◽  
Vitro Fertilization ◽  
New Findings ◽  
Bovine Oocytes ◽  
Dependent Pathway

Abstract The present study evaluated the mechanism by which protein synthesis inhibitors activate bovine oocytes. The aim was to analyze the dynamics of MPF and MAPKs. MII oocytes were activated with ionomycin (Io), ionomycin+anisomycin (ANY) and ionomycin+cycloheximide (CHX) and by in vitro fertilization (IVF). The expression of cyclin B1, p-CDK1, p-ERK1/2, p-JNK, and p-P38 were evaluated by immunodetection and the kinase activity of ERK1/2 was measured by enzyme assay. Evaluations at 1, 4, and 15 hours postactivation (hpa) showed that the expression of cyclin B1 was not modified by the treatments. ANY inactivated MPF by p-CDK1Thr14-Tyr15 at 4 hpa (P < 0.05), CHX increased pre-MPF (p-CDK1Thr161 and p-CDK1Thr14-Tyr15) at 1 hpa and IVF increased p-CDK1Thr14-Tyr15 at 17 hours postfertilization (hpf) (P < 0.05). ANY and CHX reduced the levels of p-ERK1/2 at 4 hpa (P < 0.05) and its activity at 4 and 1 hpa, respectively (P < 0.05). Meanwhile, IVF increased p-ERK1/2 at 6 hpf (P < 0.05); however, its kinase activity decreased at 6 hpf (P < 0.05). p-JNK in ANY, CHX, and IVF oocytes decreased at 4 hpa (P < 0.05). p-P38 was only observed at 1 hpa, with no differences between treatments. In conclusion, activation of bovine oocytes by ANY, CHX, and IVF inactivates MPF by CDK1-dependent specific phosphorylation without cyclin B1 degradation. ANY or CHX promoted this inactivation, which seemed to be more delayed in the physiological activation (IVF). Both inhibitors modulated MPF activity via an ERK1/2-independent pathway, whereas IVF activated the bovine oocytes via an ERK1/2-dependent pathway. Finally, ANY does not activate the JNK and P38 kinase pathways.

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