1-Nitropyrene disrupts testosterone biogenesis via AKAP1 degradation promoted mitochondrial fission in mouse Leydig cell

Zhang, Weiwei; Li, Xiu-liang; Liu, Yulin; Liu, Jiayu; Zhu, Xin‐Xin; Li, Jian; Zhao, Lingli; Zhang, Cheng; Wang, Hua; D, Xu; Gao, Lan

doi:10.1016/j.envpol.2022.119484

Cited by 11 publications

(1 citation statement)

References 45 publications

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“…Mitochondrial damage will activate the mitochondrial apoptosis program, which greatly limits the normal physiological function including protein synthesis. We herein used commercially available time-dependent mitochondrial damage agent 1-Nitropyrene (1-NP) and Carbonyl cyanide 3-chlorophenylhydrazone (CCCP) to induce mitochondrial apoptosis, atempting to explore the effect of mitochondria dysfuntion on protein expression. , To test whether mitochondrial dysfunction leads to decreased protein expression, we treated HEK293 cells with CCCP and 1-NP (1 μM) for 8, 24, and 48 h, respectively, before expressed SOD1(A4 V)-Halo and costaining with commercial mitochondrial labeling reagent (MitoTracker Green, 2 μM) and A9-Halo (2 μM). After treatment with MG132 (1 μM) for 24 h, a decreased fluorescent signal from A9-Halo was observed comparing to cells without treatment, suggesting there was a reduced level of protein expression (Figure a).…”

Section: Resultsmentioning

confidence: 99%

NRhFluors: Quantitative Revealing the Interaction between Protein Homeostasis and Mitochondria Dysfunction via Fluorescence Lifetime Imaging

Huang,

Chang,

Gao

et al. 2024

ACS Cent. Sci.

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Degenerative diseases are closely related to the changes of protein conformation beyond the steady state. The development of feasible tools for quantitative detection of changes in the cellular environment is crucial for investigating the process of protein conformational variations. Here, we have developed a near-infrared AIE probe based on the rhodamine fluorophore, which exhibits dual responses of fluorescence intensity and lifetime to local viscosity changes. Notably, computational analysis reveals that NRhFluors fluorescence activation is due to inhibition of the RACI mechanism in viscous environment. In the chemical regulation of rhodamine fluorophores, we found that variations of electron density distribution can effectively regulate CI states and achieve fluorescence sensitivity of NRhFluors. In addition, combined with the AggTag method, the lifetime of probe A9-Halo exhibits a positive correlation with viscosity changes. This analytical capacity allows us to quantitatively monitor protein conformational changes using fluorescence lifetime imaging (FLIM) and demonstrate that mitochondrial dysfunction leads to reduced protein expression in HEK293 cells. In summary, this work developed a set of nearinfrared AIE probes activated by the RACI mechanism, which can quantitatively detect cell viscosity and protein aggregation formation, providing a versatile tool for exploring disease-related biological processes and therapeutic approaches.

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Section: Resultsmentioning

confidence: 99%