Xiaoqing Feng
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Xiaoqing Feng has a total of 11 co-authors. Here are the top co-authors by number of shared publications:
- Changzhu Li
State Key Laboratory of Utilization of Woody Oil Resource, Hunan Academy of Forestry, Changsha 410004, China
1 shared publication - Jingzhen Chen
State Key Laboratory of Utilization of Woody Oil Resource, Hunan Academy of Forestry, Changsha 410004, China
1 shared publication - Lijuan Jiang
College of Life Science and Technology, Central South University of Forestry and Technology, 498 South Shaoshan Road, Changsha 410004, China
1 shared publication - Peiwang Li
State Key Laboratory of Utilization of Woody Oil Resource, Hunan Academy of Forestry, Changsha 410004, China
1 shared publication - Qiang Liu
College of Life Science and Technology, Central South University of Forestry and Technology, 498 South Shaoshan Road, Changsha 410004, China
1 shared publication - Shushan Jia
Qingdao Research Academy of Environmental Sciences, Qingdao 266000, China
1 shared publication
Latest Publications
- Open Access
- 30 June 2026
- Published by MDPI AG in Antioxidants
- Vol. 15 (7) , 824
Camelliasaponin B1, a Saponin from Camellia oleifera Seed, Protects Against Oxidative Stress and Is Associated with Reduced BNIP3/NIX-LC3B Expression in PC12 Cells
Camelliasaponins, bioactive constituents abundant in the by-products of Camellia oleifera oil production, exhibit diverse biological activities. However, their potential in regulating neuroprotective mitophagy remains largely unexplored. This study identifies camelliasaponin B1 (CSB1) as an abundant component in C. oleifera seeds and investigates its cytoprotective mechanisms against oxidative stress. Using an in vitro model of H2O2-induced oxidative damage in PC12 cells, we found that CSB1 pretreatment significantly alleviated oxidative stress, as evidenced by reduced reactive oxygen species (ROS) accumulation and enhanced antioxidant enzyme activities (SOD, CAT, GSH-Px). CSB1 also preserved mitochondrial function, restoring membrane potential (ΔΨm), ultrastructure, and respiratory capacity. Mechanistically, CSB1 reduces the expression of BNIP3/NIX-LC3B pathway-related proteins, suggesting a modulatory effect on mitophagy, as supported by transcriptomic analysis, Western blotting, and immunofluorescence. Molecular docking computationally predicted potential interactions between CSB1 and BNIP3/NIX proteins, which require experimental validation. Collectively, these findings suggest that CSB1 acts as a cytoprotective agent that enhances antioxidant defenses, safeguards mitochondrial integrity, and is associated with reduced BNIP3/NIX-LC3B expression and co-localization, offering a potential molecular basis for its development as a neuroprotective agent targeting oxidative stress-related mitochondrial dysfunction.
- 30 June 2026
- Published by MDPI AG in Antioxidants
- Vol. 15 (7) , 824
Open AccessCamelliasaponin B1, a Saponin from Camellia oleifera Seed, Protects Against Oxidative Stress and Is Associated with Reduced BNIP3/NIX-LC3B Expression in PC12 Cells
Camelliasaponins, bioactive constituents abundant in the by-products of Camellia oleifera oil production, exhibit diverse biological activities. However, their potential in regulating neuroprotective mitophagy remains largely unexplored. This study identifies camelliasaponin B1 (CSB1) as an abundant component in C. oleifera seeds and investigates its cytoprotective mechanisms against oxidative stress. Using an in vitro model of H2O2-induced oxidative damage in PC12 cells, we found that CSB1 pretreatment significantly alleviated oxidative stress, as evidenced by reduced reactive oxygen species (ROS) accumulation and enhanced antioxidant enzyme activities (SOD, CAT, GSH-Px). CSB1 also preserved mitochondrial function, restoring membrane potential (ΔΨm), ultrastructure, and respiratory capacity. Mechanistically, CSB1 reduces the expression of BNIP3/NIX-LC3B pathway-related proteins, suggesting a modulatory effect on mitophagy, as supported by transcriptomic analysis, Western blotting, and immunofluorescence. Molecular docking computationally predicted potential interactions between CSB1 and BNIP3/NIX proteins, which require experimental validation. Collectively, these findings suggest that CSB1 acts as a cytoprotective agent that enhances antioxidant defenses, safeguards mitochondrial integrity, and is associated with reduced BNIP3/NIX-LC3B expression and co-localization, offering a potential molecular basis for its development as a neuroprotective agent targeting oxidative stress-related mitochondrial dysfunction.