Involvement of Histone H1.2 in Apoptosis Induced by DNA Double-Strand Breaks

Konishi, Akimitsu; Shimizu, Shigeomi; Hirota, Junko; Takao, Toshifumi; Fan, Yuhong; Matsuoka, Yosuke; Zhang, Lilin; Yoneda, Yoshihiro; Fujii, Yoshitaka; Skoultchi, Arthur I.; Tsujimoto, Yoshihide

doi:10.1016/s0092-8674(03)00719-0

Cited by 308 publications

(315 citation statements)

References 59 publications

Supporting

Mentioning

294

Contrasting

Unclassified

Order By: Relevance

“…RNAs were converted to cDNAs using MMLV reverse transcriptase (Life Technologies) and oligo(dT) [12][13][14][15][16][17][18] (Amersham Biosciences). The cDNA was then amplified by polymerase chain reaction (PCR) using AmpliTaq Gold DNA polymerase (Applied Biosystems).…”

Section: Semiquantitative Rt-pcr Analysismentioning

confidence: 99%

See 1 more Smart Citation

Sodium orthovanadate suppresses DNA damage-induced caspase activation and apoptosis by inactivating p53

et al. 2005

View full text Add to dashboard Cite

We previously reported that p42/SETb is a substrate for caspase-7 in irradiated MOLT-4 cells, and that treating the cells with sodium orthovanadate (vanadate) inhibits p42/SETb's caspase-mediated cleavage. Here, we initially found that the inhibitory effect of vanadate was due to the suppression of caspase activation but not of caspase activity. Further investigations revealed that vanadate suppressed upstream of apoptotic events, such as the loss of mitochondrial membrane potential, the conformational change of Bax, and p53 transactivation, although the accumulation, total phosphorylation, and phosphorylation of six individual sites of p53 were not affected. Importantly, vanadate suppressed p53-dependent apoptosis, but not p53-independent apoptosis. Finally, gel-shift and chromatin immunoprecipitation assays conclusively demonstrated that vanadate inhibits the DNA-binding activity of p53. Vanadate is conventionally used as an inhibitor of protein tyrosine phosphatases (PTPs); however, we recommend that the influence of vanadate not only on PTPs but also on p53 be considered before using it.

show abstract

Section: Semiquantitative Rt-pcr Analysismentioning

confidence: 99%

“…1 Recent studies have revealed two potential mediators of p53-dependent apoptosis, p53 upregulated modulator of apoptosis (PUMA) 11 and Histone H1 (especially Histone H1.2). 12 Once transactivated by p53, they cause the release of mitochondrial proapoptotic molecules into the cytosol and initiate the caspase cascade.…”

Section: Introductionmentioning

confidence: 99%

Sodium orthovanadate suppresses DNA damage-induced caspase activation and apoptosis by inactivating p53

et al. 2005

View full text Add to dashboard Cite

show abstract

“…Thus, GFP-labeled H1.1, H1.2, and H1.3 were mainly found in euchromatin, whereas H1.4 and H1.5 were more common in heterochromatin (12). Some of the H1 subtypes have been assigned specific roles such as H1.2, which participates in apoptosis signaling after induction of DNA double strand breaks (15).…”

mentioning

confidence: 99%

Translocation of histone H1 subtypes between chromatin and cytoplasm during mitosis in normal human fibroblasts

et al. 2010

View full text Add to dashboard Cite

Histone H1 is an important constituent of chromatin, which undergoes major structural rearrangements during mitosis. However, the role of H1, multiple H1 subtypes, and H1 phosphorylation is still unclear. In normal human fibroblasts, phosphorylated H1 was found located in nuclei during prophase and in both cytoplasm and condensed chromosomes during metaphase, anaphase, and telophase as detected by immunocytochemistry. Moreover, we detected remarkable differences in the distribution of the histone H1 subtypes H1.2, H1.3, and H1.5 during mitosis. H1.2 was found in chromatin during prophase and almost solely in the cytoplasm of metaphase and early anaphase cells. In late anaphase, it appeared in both chromatin and cytoplasm and again in chromatin during telophase. H1.5 distribution pattern resembled that of H1.2, but H1.5 was partitioned between chromatin and cytoplasm during metaphase and early anaphase. H1.3 was detected in chromatin in all cell cycle phases. We propose therefore, that H1 subtype translocation during mitosis is controlled by phosphorylation, in combination with H1 subtype inherent affinity. We conclude that H1 subtypes, or their phosphorylated forms, may leave chromatin in a regulated way to give access for chromatin condensing factors or transcriptional regulators during mitosis. ' 2010International Society for Advancement of Cytometry Key terms histone H1; chromatin; cell cycle; mitosis IN the cell cycle, DNA and protein content are duplicated, and the cell divides in two in a strict sequential order of events. During prophase, the replicated chromosomes condense, and the nuclear membrane breaks down in prometaphase. At metaphase, the chromosomes are aligned at the equator of the mitotic spindle, and the sister chromatids are segregated to the two poles of the spindle during anaphase. Finally, the separation is completed during telophase by cytoplasmic division. Impaired cell cycle control or cell cycle progression may result in cell death or malignant transformation.

show abstract

“…This subtype of histone H1 is the one which binds most weakly to DNA [23] and is also released from nuclei of apoptotic cells upon genotoxic damage [24]. Nuclei of HeLa cells expressing PA-GFP-H1.2 were either irradiated at 1050 nm to induce DNA-SBs in a rectangular volume, or left unirradiated.…”

Section: Resultsmentioning

confidence: 99%

Imaging of the DNA damage‐induced dynamics of nuclear proteins via nonlinear photoperturbation

Tomas

Blumhardt

Deutzmann

et al. 2012

Journal of Biophotonics

View full text Add to dashboard Cite

Understanding the cellular response to DNA strand breaks is crucial to decipher the mechanisms maintaining the integrity of our genome. We present a novel method to visualize how the mobility of nuclear proteins changes in response to localized DNA damage. DNA strand breaks are induced via nonlinear excitation with femtosecond laser pulses at λ = 1050 nm in a 3D‐confined subnuclear volume. After a time delay of choice, protein mobility within this volume is analysed by two‐photon photoactivation of PA‐GFP fusion proteins at λ = 775 nm. By changing the position of the photoactivation spot with respect to the zone of lesion the influence of chromatin structure and of the distance from damage are investigated. As first applications we demonstrate a locally confined, time‐dependent mobility increase of histone H1.2, and a progressive retardation of the DNA repair factor XRCC1 at damaged sites. This assay can be used to map the response of nuclear proteins to DNA damage in time and space. (© 2013 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim)

show abstract

Involvement of Histone H1.2 in Apoptosis Induced by DNA Double-Strand Breaks

Cited by 308 publications

References 59 publications

Sodium orthovanadate suppresses DNA damage-induced caspase activation and apoptosis by inactivating p53

Sodium orthovanadate suppresses DNA damage-induced caspase activation and apoptosis by inactivating p53

Translocation of histone H1 subtypes between chromatin and cytoplasm during mitosis in normal human fibroblasts

Imaging of the DNA damage‐induced dynamics of nuclear proteins via nonlinear photoperturbation

Contact Info

Product

Resources

About