Biology subjects

Liu, S.-M.

Publications and source records attributed to Liu, S.-M..

5 recordsLinked to original sources

bioRxiv2025

Debutylation and Dephenylation of Organotin Compounds Through Fungal Laccase-Mediator Systems

In this study, the biodegradation of tetrabutyltin (TeBT) and tetraphenyltin (TePhT) through various laccase-mediator systems were investigated. The fungal laccases used were from the extracellular fluid of solid fermentation culture of white-rot fungi Perenniporia tephropora TFRI 707, Agrocybe aegerita, and Pleurotus geesteranus, with 2,2-azino-bis (3-ethylbenzthiazoline-6-sulfonic acid), violuric acid, 4-hydroxyacetophenone, and syringaldehyde being used as mediators. After 7 days of incubation, 300 g/L of TeBT or 1000 g/L of TePhT were added, the laccase obtained from P. tephropora TFRI 707 removed 83.9%-87.4% of TeBT and 78.0%-91.9% of TePhT; the laccase obtained from A. aegerita removed 73.7%-88.9% of TeBT and 75.5%-92.0% of TePhT; and the laccase obtained from Pl. geesteranus removed 70.4%-85.3% of TeBT and 72.9%-90.2% of TePhT (percentages include incubation with and without mediators). Tributyltin (TBT), dibutyltin (DBT), and monobutyltin (MBT) were detected during the degradation of TeBT. Triphenyltin (TPhT), diphenyltin (DPhT), and monophenyltin (MPhT) were detected during the degradation of TePhT. Therefore, laccases can effectively and rapidly remove butyl or phenyl side chains from the organotin compounds. Because dealkylated alkyl organotin compounds and the elemental tin exhibit considerably low toxicity, laccases can potentially be used in environmental cleanup.

microbiology↗

bioRxiv2025

Myocyte Enhancer Factor 2A Orchestrates Vascular Redox Homeostasis via Direct Transcriptional Activation of SIRT1

Myocyte enhancer factor 2A (MEF2A), a transcription factor implicated in coronary artery disease, remains unexplored in vascular redox regulation. To address this gap and overcome limitations of current antioxidant therapies, we investigated MEF2As role in oxidative defense using human umbilical vein endothelial cells (HUVECs) and murine models. Adenoviral vectors encoding MEF2A-specific shRNA or mRNA were employed to silence or overexpress MEF2A in HUVECs. For in vivo validation, endothelial-targeted MEF2A knockdown was achieved via AAV1-shRNA delivery in mice fed a high-fat diet. Systemic redox status was assessed by measuring reactive oxygen species (ROS), glutathione homeostasis (GSH/GSSG ratio), NADH/NAD+ balance, mitochondrial membrane potential ({Delta}{Psi}m), and 8-hydroxy-2'-deoxyguanosine (8-OHdG). Mechanistic insights were derived from immunofluorescence, qPCR, western blotting, and dual-luciferase reporter assays. MEF2A silencing induced redox imbalance, characterized by elevated ROS, reduced GSH/GSSG ratio, and {Delta}{Psi}m collapse. Conversely, MEF2A overexpression synergized with SIRT1 to restore glutathione pools, maintain NAD+ homeostasis, and suppress ROS under oxidative stress. Chromatin immunoprecipitation confirmed direct MEF2A binding to two cis-elements in the SIRT1 promoter, driving transcriptional activation. In vivo, MEF2A-deficient mice exhibited amplified vascular oxidative damage, including elevated DNA damage marker (8-OHdG) and ROS levels. Downregulation of SIRT1/PGC-1 in MEF2A silenced cells was verified in vivo. Our findings establish MEF2A as a master regulator of endothelial redox defense via the SIRT1-PGC-1 axis, offering a mechanistic foundation for targeting oxidative cardiovascular disorders. This work suggests pharmacological MEF2A activation as a novel strategy for precision antioxidant therapy in vascular medicine.

molecular biology↗

bioRxiv2020

Methylation of Dual Specificity Phosphatase 4 Controls Cell Differentiation

A collection of signaling and epigenetic events needs to be orchestrated for normal development of hematopoietic lineages. While mitogen-activated protein (MAP) kinases (MAPKs) and multiple epigenetic modulators have been implicated in the megakaryocytic (Mk) cell differentiation, the underlying molecular mechanisms of signaling-epigenetic crosstalk remain unclear. MAPKs are in general inactivated by dual specificity phosphatases (DUSPs), whose activities are tightly regulated by various posttranslational modifications. Using knockdown screening and single-cell transcriptional analysis, we determined that DUSP4 is the phosphatase that inactivates p38 MAPK in hematopoietic cells and serves as a key regulator to promote Mk differentiation. With the nextgeneration Bioorthogonal Profiling of Protein Methylation technology for live cells, we identified DUSP4 as a PRMT1 substrate. Mechanistically, PRMT1-mediated Arg351 methylation of DUSP4 triggers its ubiquitinylation by HUWE1 (an E3 ligase) and then degradation, which results in p38 MAPK activation and inhibition of Mk differentiation in vitro and in vivo. Interestingly, the mechanistic axis of the DUSP4 degradation and p38 activation is also associated with a transcriptional signature of immune activation and thus argues immunological roles of Mk cells. Collectively, these results demonstrate a critical role of PRMT1-mediated posttranslational modification of DUSP4 in regulation of Mk differentiation and maturation. In the context of thrombocytopenia observed in myelodysplastic syndromes (MDS), we demonstrated that high levels of p38 MAPK and PRMT1 are associated with low platelet counts and adverse prognosis, while pharmacological inhibition of p38 MAPK or PRMT1 stimulates megakaryopoiesis in MDS samples. These findings provide novel mechanistic insights into the role of the PRMT1-DUSP4-p38 axis on Mk differentiation and present a targeting strategy for treatment of thrombocytopenia associated with myeloid malignancies such as MDS.

cell biology↗

bioRxiv2020

Structural visualization of septum formation in Staphylococcus warneri using atomic force microscopy

Cell division of Staphylococcus adopts a "popping" mechanism that mediates extremely rapid separation of the septum. Elucidating the structure of the septum is crucial for understanding this exceptional bacterial cell division mechanism. Here, the septum structure of Staphylococcus warneri is extensively characterized using high-speed time-lapse confocal microscopy, atomic force microscopy, and electron microscopy. The cells of S. warneri divide in a fast "popping" manner on a millisecond timescale. Our results show that the septum is composed of two separable layers, providing a structural basis for the ultrafast daughter cell separation. The septum is formed progressively toward the center with non-uniform thickness of the septal disk in radial directions. The peptidoglycan on the inner surface of double-layered septa is organized into concentric rings, which are generated along with septum formation. Moreover, this study signifies the importance of new septum formation in initiating new cell cycles. This work unravels the structural basis underlying the "popping" mechanism that drives Staphylococcus cell division and reveals a generic structure of the bacterial cell. IMPORTRANCEThis work shows that the septum of Staphylococcus warneri is composed of two layers and the peptidoglycan on the inner surface of the double-layered septum is organized into concentric rings. Moreover, new cell cycles of Staphylococcus could be initiated before the previous cell cycle is complete. This work advances our knowledge about a basic structure of bacterial cell and provides the double layered structural information of septum for the bacterium that divide with the "popping" mechanism.

biophysics↗

bioRxiv2017

mTORC1 in AGRP neurons integrates exteroceptive and interoceptive food-related cues in the modulation of adaptive energy expenditure in mice

Energy dissipation through interscapular brown adipose tissue (iBAT) thermogenesis is an important contributor to adaptive energy expenditure. However, it remains unresolved how acute and chronic changes in energy availability are detected by the brain to adjust iBAT activity and maintain energy homeostasis. Here we provide evidence that AGRP inhibitory tone to iBAT represents an energy-sparing circuit that integrates environmental food cues and internal signals of energy availability. We establish a role for the nutrient-sensing mTORC1 signaling pathway within AGRP neurons in the detection of environmental food cues and internal signals of energy availability, and in the bi-directional control of iBAT thermogenesis during nutrient deficiency and excess. Collectively, our findings provide insights into how mTORC1 signaling within AGRP neurons surveys energy availability to engage iBAT thermogenesis, and identify AGRP neurons as a neuronal substrate for the coordination of energy intake and adaptive expenditure under varying physiological and environmental contexts.

neuroscience↗