Electron-spin double resonance of nitrogen-vacancy centers in diamond under strong driving field

The nitrogen-vacancy (NV) center in diamond has been the focus of research efforts because of its suitability for use in applications such as quantum sensing and quantum simulations. Recently, the electron-spin double resonance (ESDR) of NV centers has been exploited for detecting radio-frequency (RF) fields with continuous-wave optically detected magnetic resonance. However, the characteristic phenomenon of ESDR under a strong RF field remains to be fully elucidated. In this study, we theoretically and experimentally analyzed the ESDR spectra under strong RF fields by adopting the Floquet theory. Our analytical and numerical calculations could reproduce the ESDR spectra obtained by measuring the spin-dependent photoluminescence under the continuous application of microwaves and an RF field for a DC bias magnetic field perpendicular to the NV axis. We found that anticrossing structures that appear under a strong RF field are induced by the generation of RF-dressed states owing to the two-RF-photon resonances. Moreover, we found that $2n$-RF-photon resonances were allowed by an unintentional DC bias magnetic field parallel to the NV axis. These results should help in the realization of precise MHz-range AC magnetometry with a wide dynamic range beyond the rotating wave approximation regime as well as Floquet engineering in open quantum systems.Comment: 11 pages, 4 figure

Characterization of genetically modified mice for phosphoglycerate mutase, a vitally-essential enzyme in glycolysis

Models de ratolí; Glucòlisi; Diabetis mellitusModelos de ratón; Glucólisis; Diabetes mellitusMouse models; Glycolysis; Diabetes mellitusGlycolytic metabolism is closely involved in physiological homeostasis and pathophysiological states. Among glycolytic enzymes, phosphoglycerate mutase (PGAM) has been reported to exert certain physiological role in vitro, whereas its impact on glucose metabolism in vivo remains unclear. Here, we report the characterization of Pgam1 knockout mice. We observed that homozygous knockout mice of Pgam1 were embryonic lethal. Although we previously reported that both PGAM-1 and -2 affect global glycolytic profile of cancers in vitro, in vivo glucose parameters were less affected both in the heterozygous knockout of Pgam1 and in Pgam2 transgenic mice. Thus, the impact of PGAM on in vivo glucose metabolism is rather complex than expected before.This work was supported in part by grants from the Japan Society for the Promotion of Science (Grants No. 26310103 to HK and No. 15K19283 to HK), and by the Japan Agency for Medical Research and Development (AMED), Core Research for Evolutional Science and Technology (CREST JP17gm0610002h0306 to HK). HK; Hiroshi Kondoh

Senescence-inducing stress promotes proteolysis of phosphoglycerate mutase via ubiquitin ligase Mdm2.

細胞老化から癌化への変換のカギとなる解糖系制御機構解明に成功 -代謝を標的とした新しい抗がん剤開発に期待-. 京都大学プレスリリース. 2014-02-24.Despite the well-documented clinical significance of the Warburg effect, it remains unclear how the aggressive glycolytic rates of tumor cells might contribute to other hallmarks of cancer, such as bypass of senescence. Here, we report that, during oncogene- or DNA damage-induced senescence, Pak1-mediated phosphorylation of phosphoglycerate mutase (PGAM) predisposes the glycolytic enzyme to ubiquitin-mediated degradation. We identify Mdm2 as a direct binding partner and ubiquitin ligase for PGAM in cultured cells and in vitro. Mutations in PGAM and Mdm2 that abrogate ubiquitination of PGAM restored the proliferative potential of primary cells under stress conditions and promoted neoplastic transformation. We propose that Mdm2, a downstream effector of p53, attenuates the Warburg effect via ubiquitination and degradation of PGAM

Phosphoglycerate Mutase Cooperates with Chk1 Kinase to Regulate Glycolysis

癌における解糖系代謝の制御機構を発見 --新規抗癌剤治療への応用の可能性--. 京都大学プレスリリース. 2020-07-22.Dysregulated glycolysis, including the cancerous Warburg effect, is closely involved in pathological mechanisms of diseased states. Among glycolytic enzymes, phosphoglycerate mutase (PGAM) has been known to exert certain physiological impact in vitro, whereas its regulatory role on glycolysis remains unclear. Here, we identified that PGAM plays a key role in regulating glycolysis in cancer cells but not in standard cells. Cancer-prone phenotype by PGAM overexpression in vivo was associated with upregulated glycolytic features. PGAM interacts and cooperates with Chk1 to regulate the enhanced glycolysis in cancer cells, especially under oncogenic Ras expressing conditions. Genetic or chemical interference of the PGAM-Chk1 interaction, with intact PGAM activity, abrogated the maintenance of cancerous enhanced glycolysis. Thus, the nonenzymatic function of PGAM is essential for the Warburg effect that accompanies cancerous proliferation

Senescence-inducing stress promotes proteolysis of phosphoglycerate mutase via ubiquitin ligase Mdm2

細胞老化から癌化への変換のカギとなる解糖系制御機構解明に成功 -代謝を標的とした新しい抗がん剤開発に期待-. 京都大学プレスリリース. 2014-02-24.Despite the well-documented clinical significance of the Warburg effect, it remains unclear how the aggressive glycolytic rates of tumor cells might contribute to other hallmarks of cancer, such as bypass of senescence. Here, we report that, during oncogene- or DNA damage-induced senescence, Pak1-mediated phosphorylation of phosphoglycerate mutase (PGAM) predisposes the glycolytic enzyme to ubiquitin-mediated degradation. We identify Mdm2 as a direct binding partner and ubiquitin ligase for PGAM in cultured cells and in vitro. Mutations in PGAM and Mdm2 that abrogate ubiquitination of PGAM restored the proliferative potential of primary cells under stress conditions and promoted neoplastic transformation. We propose that Mdm2, a downstream effector of p53, attenuates the Warburg effect via ubiquitination and degradation of PGAM