Optimizing Cell Synchronization Using Nocodazole or Double Thymidine Block

Surani, Arif A.; Colombo, Sergio; Barlow, George W.; Foulds, Gemma A.; Montiel-Duarte, Cristina

doi:10.1007/978-1-0716-1538-6_9

Cited by 8 publications

(4 citation statements)

References 16 publications

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“…To functionally characterize the cellular heterogeneity of metabolic processes, we further treated the tumor cells with various drugs, which interfere with the metabolic activity of cells. Nocodazole interferes with the metabolic activity of cells by inhibiting the polymerization of microtubules, making cells stay in the G2/M phase of the cell cycle . Cytochalasin D interferes with the metabolic activity of cells by inhibiting actin polymerization, resulting in cell cycle arrest .…”

Section: Resultsmentioning

confidence: 99%

“…Nocodazole interferes with the metabolic activity of cells by inhibiting the polymerization of microtubules, making cells stay in the G2/M phase of the cell cycle. 48 Cytochalasin D interferes with the metabolic activity of cells by inhibiting actin polymerization, resulting in cell cycle arrest. 49 Blebbistatin interferes with the metabolic activity of cells by inhibiting cell division.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

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Metabolic Footprinting-Based DNA-AuNP Encoders for Extracellular Metabolic Response Profiling

Zou

Peng

et al. 2023

Anal. Chem.

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Metabolic footprinting as a convenient and noninvasive cell metabolomics strategy relies on monitoring the whole extracellular metabolic process. It covers nutrient consumption and metabolite secretion of in vitro cell culture, which is hindered by low universality owing to pre-treatment of the cell medium and special equipment. Here, we report the design and a variety of applicability, for quantifying extracellular metabolism, of fluorescently labeled single-stranded DNA (ssDNA)-AuNP encoders, whose multi-modal signal response is triggered by extracellular metabolites. We constructed metabolic response profiling of cells by detecting extracellular metabolites in different tumor cells and drug-induced extracellular metabolites. We further assessed the extracellular metabolism differences using a machine learning algorithm. This metabolic response profiling based on the DNA-AuNP encoder strategy is a powerful complement to metabolic footprinting, which significantly applies potential non-invasive identification of tumor cell heterogeneity.

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Section: Resultsmentioning

confidence: 99%

Section: ■ Results and Discussionmentioning

confidence: 99%

Metabolic Footprinting-Based DNA-AuNP Encoders for Extracellular Metabolic Response Profiling

Zou

Peng

et al. 2023

Anal. Chem.

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“…Thymidine is a DNA synthesis inhibitor that can arrest cell at the G1/S boundary, prior to DNA replication ( Chen and Deng, 2018 ). Thymidine has been widely used to study the mechanisms involved in the regulation of cell cycle progression through cell synchronization ( Su et al, 2021 ; Surani et al, 2021 ). In our study, a total of 15 DEPs common between the thymidine group and PEDV N group were eliminated from the 58 DEPs identified in the PEDV N group using thymidine as the cell cycle arrest control group.…”

Section: Discussionmentioning

confidence: 99%

Up-regulated 60S ribosomal protein L18 in PEDV N protein-induced S-phase arrested host cells promotes viral replication

Zhu

Su²,

Shan³

et al. 2022

Virus Research

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“…Mitotic vs Asynchronous cell synchronization (for ChIP seq): Cells were treated with 100 ng per ml Nocodazole (Sigma M1404) for 24 hours with DMSO (Sigma) as the solvent control (Naumova et al ., 2013; Ma and Poon, 2017; Surani et al ., 2021).…”

Section: Methodsmentioning

confidence: 99%

Compaction of Active Chromatin Domains and Promoters by H3S10 Phosphorylation during Mitosis Preserves Interphase-Specific Chromatin Structure and Function

Meel,

Mishra,

Mann

et al. 2024

Preprint

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Mitotic chromosomes lose interphase-specific genome organization and transcription but gain histone phosphorylation, specifically H3S10p. This phosphorylation event compacts chromosomes in early mitosis by reducing inter-nucleosomal distance before the loading of condensins. However, it is unclear if H3S10p in mitosis preserves the identity of lost chromatin domains and promoters, both physically and functionally. Here, using the pre-mitotic expression of histone H3S10 and its mutants H3S10A and H3S10D, we show that H3S10p hyper-phosphorylates active promoters and spreads into super-domains A in mitosis, causing compaction of these regions. By spreading into active domains in the absence of genome organization, H3S10p retains their identity physically. Functionally, H3S10p ensures optimal closing of promoters by stabilizing the nucleosomes, thereby protecting them from excess loading of transcription machinery post-mitosis. In the H3S10p phospho-mutants, these chromatin regions fail to condense properly during mitosis. As a result, they exhibit enhanced accessibility and transcription of active genes in the next interphase. We propose that the spreading of mitotic H3S10p into active domains preserves their identity during mitosis and, in subsequent interphase, acts as a rheostat to fine-tune transcription and chromatin domain re-formation.

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Optimizing Cell Synchronization Using Nocodazole or Double Thymidine Block

Cited by 8 publications

References 16 publications

Metabolic Footprinting-Based DNA-AuNP Encoders for Extracellular Metabolic Response Profiling

Metabolic Footprinting-Based DNA-AuNP Encoders for Extracellular Metabolic Response Profiling

Up-regulated 60S ribosomal protein L18 in PEDV N protein-induced S-phase arrested host cells promotes viral replication

Compaction of Active Chromatin Domains and Promoters by H3S10 Phosphorylation during Mitosis Preserves Interphase-Specific Chromatin Structure and Function

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