Lighting up alkaline phosphatase in drug-induced liver injury using a new chemiluminescence resonance energy transfer nanoprobe

2018 ◽  
Vol 54 (88) ◽  
pp. 12479-12482 ◽  
Author(s):  
Xueting Liu ◽  
Nannan Fan ◽  
Lijie Wu ◽  
Chuanchen Wu ◽  
Yongqing Zhou ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Energy Transfer ◽  
Liver Injury ◽  
Alkaline Phosphatase Level ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Drug Induced ◽  
Drug Induced Liver Injury

Ultra-sensitive imaging of the alkaline phosphatase levelin vivoin drug-induced liver injury with a new chemiluminescence resonance energy transfer nanoprobe.

scholarly journals Generation of a Transgenic Zebrafish Line for In Vivo Assessment of Hepatic Apoptosis

2021 ◽  
Vol 14 (11) ◽  
pp. 1117
Author(s):  
Aina Higuchi ◽  
Eri Wakai ◽  
Tomoko Tada ◽  
Junko Koiwa ◽  
Yuka Adachi ◽  
...  
Keyword(s):  
Phosphoenolpyruvate Carboxykinase ◽  
Caspase 3 ◽  
Fluorescent Proteins ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Transgenic Zebrafish ◽  
Drug Induced ◽  
Drug Induced Liver Injury ◽  
In Vivo Fluorescence Imaging

Hepatic apoptosis is involved in a variety of pathophysiologic conditions in the liver, including hepatitis, steatosis, and drug-induced liver injury. The development of easy-to-perform and reliable in vivo assays would thus greatly enhance the efforts to understand liver diseases and identify associated genes and potential drugs. In this study, we developed a transgenic zebrafish line that was suitable for the assessment of caspase 3 activity in the liver by using in vivo fluorescence imaging. The larvae of transgenic zebrafish dominantly expressed Casper3GR in the liver under control of the promoter of the phosphoenolpyruvate carboxykinase 1 gene. Casper3GR is composed of two fluorescent proteins, tagGFP and tagRFP, which are connected via a peptide linker that can be cleaved by activated caspase 3. Under tagGFP excitation conditions in zebrafish that were exposed to the well-characterized hepatotoxicant isoniazid, we detected increased and decreased fluorescence associated with tagGFP and tagRFP, respectively. This result suggests that isoniazid activates caspase 3 in the zebrafish liver, which digests the linker between tagGFP and tagRFP, resulting in a reduction in the Förster resonance energy transfer to tagRFP upon tagGFP excitation. We also detected isoniazid-induced inhibition of caspase 3 activity in zebrafish that were treated with the hepatoprotectants ursodeoxycholic acid and obeticholic acid. The transgenic zebrafish that were developed in this study could be a powerful tool for identifying both hepatotoxic and hepatoprotective drugs, as well as for analyzing the effects of the genes of interest to hepatic apoptosis.

Electrochemiluminescence resonance energy transfer immunoassay for alkaline phosphatase using p-nitrophenyl phosphate as substrate

2020 ◽  
Vol 1097 ◽  
pp. 71-77 ◽  
Author(s):  
Wenjing Qi ◽  
Yuling Fu ◽  
Maoyu Zhao ◽  
Hongkun He ◽  
Xue Tian ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Nitrophenyl Phosphate

scholarly journals Measuring ligand-dependent and ligand-independent interactions between nuclear receptors and associated proteins using Bioluminescence Resonance Energy Transfer (BRET2)

2006 ◽  
Vol 4 (1) ◽  
pp. nrs.04021 ◽  
Author(s):  
Kristen L. Koterba ◽  
Brian G. Rowan
Keyword(s):  
Energy Transfer ◽  
Protein Interactions ◽  
Fusion Proteins ◽  
Fluorescent Protein ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Renilla Luciferase ◽  
Receptor Protein ◽  
Protein Protein Interactions

Bioluminescent resonance energy transfer (BRET2) is a recently developed technology for the measurement of protein-protein interactions in a live, cell-based system. BRET2 is characterized by the efficient transfer of excited energy between a bioluminescent donor molecule (Renilla luciferase) and a fluorescent acceptor molecule (a mutant of Green Fluorescent Protein (GFP2)). The BRET2 assay offers advantages over fluorescence resonance energy transfer (FRET) because it does not require an external light source thereby eliminating problems of photobleaching and autoflourescence. The absence of contamination by light results in low background that permits detection of very small changes in the BRET2 signal. BRET2 is dependent on the orientation and distance between two fusion proteins and therefore requires extensive preliminary standardization experiments to conclude a positive BRET2 signal independent of variations in protein titrations and arrangement in tertiary structures. Estrogen receptor (ER) signaling is modulated by steroid receptor coactivator 1 (SRC-1). To establish BRET2 in a ligand inducible system we used SRC-1 as the donor moiety and ER as the acceptor moiety. Expression and functionality of the fusion proteins were assessed by transient transfection in HEK-293 cells followed by Western blot analysis and measurement of ER-dependent reporter gene activity. These preliminary determinations are required prior to measuring nuclear receptor protein-protein interactions by BRET2. This article describes in detail the BRET2 methodology for measuring interaction between full-length ER and coregulator proteins in real-time, in an in vivo environment.

Drug-induced liver injury classification model based on in vitro human transcriptomics and in vivo rat clinical chemistry data

2014 ◽  
Vol 2 (4) ◽  
pp. 63-70 ◽  
Author(s):  
Danyel Jennen ◽  
Jan Polman ◽  
Mark Bessem ◽  
Maarten Coonen ◽  
Joost van Delft ◽  
...  
Keyword(s):  
Liver Injury ◽  
Clinical Chemistry ◽  
Classification Model ◽  
Drug Induced ◽  
Drug Induced Liver Injury ◽  
Chemistry Data ◽  
Model Based ◽  
Injury Classification

scholarly journals A genetically encoded Förster resonance energy transfer sensor for monitoring in vivo trehalose-6-phosphate dynamics

2015 ◽  
Vol 474 ◽  
pp. 1-7 ◽  
Author(s):  
Estevão A. Peroza ◽  
Jennifer C. Ewald ◽  
Geetha Parakkal ◽  
Jan M. Skotheim ◽  
Nicola Zamboni
Keyword(s):  
Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Forster Resonance Energy Transfer ◽  
Förster Resonance Energy Transfer ◽  
Förster Resonance

scholarly journals Affinity series of genetically encoded high sensitivity Förster Resonance Energy Transfer sensors for sucrose

2020 ◽  
Author(s):  
Mayuri Sadoine ◽  
Mira Reger ◽  
Ka Man Wong ◽  
Wolf B. Frommer
Keyword(s):  
Energy Transfer ◽  
Steady State ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Forster Resonance Energy Transfer ◽  
Förster Resonance Energy Transfer ◽  
Detection Range ◽  
Steady State Levels ◽  
Förster Resonance

ABSTRACTGenetically encoded fluorescent sugar sensors are valuable tools for the discovery of transporters and for quantitative monitoring of sugar steady-state levels in intact tissues. Genetically encoded Förster Resonance Energy Transfer sensors for glucose have been designed and optimized extensively, and a full series of affinity mutants is available for in vivo studies. However, to date, only a single improved sensor FLIPsuc-90µΔ1 with a Km for sucrose of ∼90 µM is available for sucrose monitoring. This sucrose sensor was engineered on the basis of an Agrobacterium tumefaciens sugar binding protein. Here, we took a two-step approach to first systematically improve the dynamic range of the FLIPsuc nanosensor and then expand the detection range from micromolar to millimolar sucrose concentrations by mutating a key residue in the binding site. The resulting series of sucrose sensors may allow systematic investigation of sucrose transporter candidates and comprehensive in vivo analyses of sucrose concentration in plants. Since FLIPsuc-90µ also detects trehalose in animal cells, the new series of sensors can be used to investigate trehalose transporter candidates and monitor trehalose steady-state levels in vivo as well.

Organic nanoparticle tracking during pharmacokinetic studies

Nanomedicine ◽  
2021 ◽  
Author(s):  
Samuel Bonnet ◽  
Rana Elfatairi ◽  
Florence Franconi ◽  
Emilie Roger ◽  
Samuel Legeay
Keyword(s):  
Energy Transfer ◽  
Structural Integrity ◽  
Biological Fluids ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Förster Resonance Energy Transfer ◽  
Pharmacokinetic Studies ◽  
Biological Barriers ◽  
Over Time

To understand how nanoparticles (NPs) interact with biological barriers and to ensure they maintain their integrity over time, it is crucial to study their in vivo pharmacokinetic (PK) profiles. Many methods of tracking have been used to describe the in vivo fate of NPs and to evaluate their PKs and structural integrity. However, they do not deliver the same level of information and this may cause misinterpretations. Here, the authors review and discuss the different methods for in vivo tracking of organic NPs. Among them, Förster resonance energy transfer (FRET) presents great potential to track NPs' integrity. However, FRET still requires validated methods to extract and quantify NPs in biological fluids and tissues.

scholarly journals Förster Resonance Energy Transfer-Based Stability Assessment of PLGA Nanoparticles in Vitro and in Vivo

2019 ◽  
Vol 2 (3) ◽  
pp. 1131-1140 ◽  
Author(s):  
Edyta Swider ◽  
Sanish Maharjan ◽  
Karlijne Houkes ◽  
Nicolaas Koen van Riessen ◽  
Carl Figdor ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Plga Nanoparticles ◽  
Forster Resonance Energy Transfer ◽  
Förster Resonance Energy Transfer ◽  
Stability Assessment ◽  
Förster Resonance

Ginsenoside Rb1, A Major Saponin from Panax ginseng, Exerts Protective Effects Against Acetaminophen-Induced Hepatotoxicity in Mice

2019 ◽  
Vol 47 (08) ◽  
pp. 1815-1831 ◽  
Author(s):  
Shen Ren ◽  
Jing Leng ◽  
Xing-Yue Xu ◽  
Shuang Jiang ◽  
Ying-Ping Wang ◽  
...  
Keyword(s):  
Liver Injury ◽  
Panax Ginseng ◽  
Inflammatory Responses ◽  
Interleukin 1 ◽  
Protective Effects ◽  
Ginsenoside Rb1 ◽  
Drug Induced ◽  
Drug Induced Liver Injury ◽  
Oxide Synthase

Acute liver injury (ALI) induced by acetaminophen (APAP) is the main cause of drug-induced liver injury. Previous reports indicated liver failure could be alleviated by saponins (ginsenosides) from Panax ginseng against APAP-induced inflammatory responses in vivo. However, validation towards ginsenoside Rb1 as a major and marker saponin may protect liver from APAP-induced ALI and its mechanisms are poorly elucidated. In this study, the protective effects and the latent mechanisms of Rb1 action against APAP-induced hepatotoxicity were investigated. Rb1 was administered orally with 10[Formula: see text]mg/kg and 20[Formula: see text]mg/kg daily for 1 week before a single injection of APAP (250[Formula: see text]mg/kg, i.p.) 1[Formula: see text]h after the last treatment of Rb1. Serum alanine/aspartate aminotransferases (ALT/AST), liver glutathione (GSH) depletion, as well as the inflammatory cytokines, such as tumor necrosis factor-[Formula: see text] (TNF-[Formula: see text]), interleukin-1[Formula: see text] (IL-1[Formula: see text]), inducible nitric oxide synthase (iNOS), and cyclooxygenase-2 (COX-2), were analyzed to indicate the underlying protective effects of Rb1 against APAP-induced hepatotoxicity with significant inflammatory responses. Histological examination further proved Rb1’s protective effects. Importantly, Rb1 mitigated the changes in the phosphorylation of MAPK and PI3K/Akt, as well as its downstream factor NF-[Formula: see text]B. In conclusion, experimental data clearly demonstrated that Rb1 exhibited a remarkable liver protective effect against APAP-induced ALI, partly through regulating MAPK and PI3K/Akt signaling pathways-mediated inflammatory responses.

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