Cyclin B1 Expression in HeLa S3 Cells Studied by Flow Cytometry

Sherwood, Sylvia; Rush, Daphne F.; Kung, Andrew L.; Schimke, Robert T.

doi:10.1006/excr.1994.1087

Cited by 61 publications

(43 citation statements)

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“…The level of cyclin B1 expression was different between the two methods as well as that of cyclin A. A striking increase in p53 and p21 proteins was found in chemically-synchronized cells (13), and the level of cyclins A and B1 was higher in HeLa cells synchronized by drugs than in normally growing controls (1,14,15). Therefore caution should be exercised when interpreting data from experiments using cells synchronized by chemical agents.…”

Section: Discussionmentioning

confidence: 85%

“…To illustrate the quantitative alterations in gene products within cells, one-by-one measurement has been made for each cell sample harvested at hourly intervals after synchronization, and thus it has to be repeated to obtain a set of data. In addition, the intracellular localization and kinetic pattern of gene products are valuable information for estimating their function, because topographical alterations in some of products are closely associated with cellular events such as cell cycle progression (1)(2)(3). In this context, an efficient and practical method is necessary for measurement of the gene expression and for elucidation of the function of gene products at the cellular level.…”

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confidence: 99%

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An analysis of changes in the expression of cyclins A and B1 by the cell array system during the cell cycle: Comparison between cell synchronization methods

et al. 2003

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Background: A novel high-throughput analysis, cell array system, was developed for an extensive study of the expression of genes and/or the degradation of gene products at the cellular level. To exemplify the usefulness of this system, we showed the changes in the expression level of cyclin A and B1 during the cell cycle in a single experiment. Methods: We used the cell array system to chase the changes in cyclin A and B1 expression during the cell cycle in HeLa cells. Cells were synchronized by mitotic selection and thymidine-hydroxyurea methods. Cells were harvested at intervals of 1 h from 0 through 23 h. These 48 cell samples were spotted on a circle of the cell array glass slide. Cyclin A and B1 were immunologically stained with Alexa Fluor 488, and nuclear DNA was stained with propidium iodide. The amount of cyclins and nuclear DNA

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Section: Discussionmentioning

confidence: 85%

mentioning

confidence: 99%

An analysis of changes in the expression of cyclins A and B1 by the cell array system during the cell cycle: Comparison between cell synchronization methods

et al. 2003

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“…In cycling cells, the level of cyclinB1 protein increases abruptly during late S-early G 2 , peaks during the metaphase/anaphase transition, and declines precipitously upon completion of mitosis (Pines and Hunter, 1991;Sherwood et al, 1994;Widrow et al, 1997). Degradation of cyclinB1 is necessary for mitotic exit (Sherwood et al, 1994;Widrow et al, 1997).…”

Section: Discussionmentioning

confidence: 99%

Diallyl trisulfide-induced G2–M phase cell cycle arrest in human prostate cancer cells is caused by reactive oxygen species-dependent destruction and hyperphosphorylation of Cdc25C

Xiao

Herman-Antosiewicz²,

Antosiewicz³

et al. 2005

Oncogene

179

195

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Molecular mechanism of cell cycle arrest caused by diallyl trisulfide (DATS), a garlic-derived cancer chemopreventive agent, has been investigated using PC-3 and DU145 human prostate cancer cells as a model. Treatment of PC-3 and DU145 cells, but not a normal prostate epithelial cell line (PrEC), with growth suppressive concentrations of DATS caused enrichment of the G 2 -M fraction. The DATS-induced cell cycle arrest in PC-3 cells was associated with increased Tyr 15 phosphorylation of cyclin-dependent kinase 1 (Cdk1) and inhibition of Cdk1/cyclinB1 kinase activity. The DATStreated PC-3 and DU145 cells also exhibited a decrease in the protein level of Cdc25C and an increase in its Ser 216 phosphorylation. The DATS-mediated decrease in protein level and Ser 216 phosphorylation of Cdc25C as well as G 2 -M phase cell cycle arrest were significantly attenuated in the presence of N-acetylcysteine implicating reactive oxygen species (ROS) in cell cycle arrest caused by DATS. ROS generation was observed in DATS-treated PC-3 and DU145 cells. DATS treatment also caused an increase in the protein level of Cdk inhibitor p21, but DATS-induced G 2 -M phase arrest was not affected by antisense-mediated suppression of p21 protein level. In conclusion, the results of the present study indicate that DATS-induced G 2 -M phase cell cycle arrest in human prostate cancer cells is caused by ROS-mediated destruction and hyperphosphorylation of Cdc25C.

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“…The frequency of BrdU and ␥-H2AX double-positive cells was similar in MLH1 ϩ and MLH1 Ϫ/Ϫ cells. We next examined the presence of DSB in G 2 cells using cyclin B1 expression as a marker (24,46). At 12 h after exposure to 20 M Cr(VI), approximately 80% of ␥-H2AX focus-containing MLH1 ϩ cells were positive for cyclin B1 staining, indicating a predominant production of DSB in G 2 phase (Fig.…”

Section: And E) Mmr Deficiency In Mlh1mentioning

confidence: 99%

Mismatch Repair Proteins Are Activators of Toxic Responses to Chromium-DNA Damage

Peterson-Roth

Reynolds

Quievryn

et al. 2005

Molecular and Cellular Biology

117

116

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Cyclin B1 Expression in HeLa S3 Cells Studied by Flow Cytometry

Cited by 61 publications

References 0 publications

An analysis of changes in the expression of cyclins A and B1 by the cell array system during the cell cycle: Comparison between cell synchronization methods

An analysis of changes in the expression of cyclins A and B1 by the cell array system during the cell cycle: Comparison between cell synchronization methods

Diallyl trisulfide-induced G2–M phase cell cycle arrest in human prostate cancer cells is caused by reactive oxygen species-dependent destruction and hyperphosphorylation of Cdc25C

Mismatch Repair Proteins Are Activators of Toxic Responses to Chromium-DNA Damage

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