scholarly journals Efficient Synthesis and In Vivo Incorporation of Acridon-2-ylalanine, a Fluorescent Amino Acid for Lifetime and Förster Resonance Energy Transfer/Luminescence Resonance Energy Transfer Studies

2013 ◽  
Vol 135 (50) ◽  
pp. 18806-18814 ◽  
Author(s):  
Lee C. Speight ◽  
Anand K. Muthusamy ◽  
Jacob M. Goldberg ◽  
John B. Warner ◽  
Rebecca F. Wissner ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Amino Acid ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Forster Resonance Energy Transfer ◽  
Förster Resonance Energy Transfer ◽  
Efficient Synthesis ◽  
Fluorescent Amino Acid ◽  
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.

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

scholarly journals Förster resonance energy transfer imaging in vivo with approximated radiative transfer equation

2011 ◽  
Vol 50 (36) ◽  
pp. 6583 ◽  
Author(s):  
Vadim Y. Soloviev ◽  
James McGinty ◽  
Daniel W. Stuckey ◽  
Romain Laine ◽  
Marzena Wylezinska-Arridge ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Radiative Transfer ◽  
Transfer Equation ◽  
Radiative Transfer Equation ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Forster Resonance Energy Transfer ◽  
Förster Resonance Energy Transfer ◽  
Förster Resonance

scholarly journals Calcineurin Aβ–Specific Anchoring Confers Isoform-Specific Compartmentation and Function in Pathological Cardiac Myocyte Hypertrophy

Circulation ◽  
2020 ◽  
Vol 142 (10) ◽  
pp. 948-962 ◽  
Author(s):  
Xiaofeng Li ◽  
Jinliang Li ◽  
Eliana C. Martinez ◽  
Alexander Froese ◽  
Catherine L. Passariello ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Cardiac Myocyte ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Forster Resonance Energy Transfer ◽  
Förster Resonance Energy Transfer ◽  
Myocyte Hypertrophy ◽  
Calcineurin Activity ◽  
Förster Resonance

Background: The Ca 2+ /calmodulin-dependent phosphatase calcineurin is a key regulator of cardiac myocyte hypertrophy in disease. An unexplained paradox is how the β isoform of the calcineurin catalytic A-subunit (CaNAβ) is required for induction of pathological myocyte hypertrophy, despite calcineurin Aα expression in the same cells. It is unclear how the pleiotropic second messenger Ca 2+ drives excitation–contraction coupling while not stimulating hypertrophy by calcineurin in the normal heart. Elucidation of the mechanisms conferring this selectivity in calcineurin signaling should reveal new strategies for targeting the phosphatase in disease. Methods: Primary adult rat ventricular myocytes were studied for morphology and intracellular signaling. New Förster resonance energy transfer reporters were used to assay Ca 2+ and calcineurin activity in living cells. Conditional gene deletion and adeno-associated virus–mediated gene delivery in the mouse were used to study calcineurin signaling after transverse aortic constriction in vivo. Results: CIP4 (Cdc42-interacting protein 4)/TRIP10 (thyroid hormone receptor interactor 10) was identified as a new polyproline domain-dependent scaffold for CaNAβ2 by yeast 2-hybrid screen. Cardiac myocyte–specific CIP4 gene deletion in mice attenuated pressure overload–induced pathological cardiac remodeling and heart failure. Blockade of CaNAβ polyproline-dependent anchoring using a competing peptide inhibited concentric hypertrophy in cultured myocytes; disruption of anchoring in vivo using an adeno-associated virus gene therapy vector inhibited cardiac hypertrophy and improved systolic function after pressure overload. Live cell Förster resonance energy transfer biosensor imaging of cultured myocytes revealed that Ca 2+ levels and calcineurin activity associated with the CIP4 compartment were increased by neurohormonal stimulation, but minimally by pacing. Conversely, Ca 2+ levels and calcineurin activity detected by nonlocalized Förster resonance energy transfer sensors were induced by pacing and minimally by neurohormonal stimulation, providing functional evidence for differential intracellular compartmentation of Ca 2+ and calcineurin signal transduction. Conclusions: These results support a structural model for Ca 2+ and CaNAβ compartmentation in cells based on an isoform-specific mechanism for calcineurin protein–protein interaction and localization. This mechanism provides an explanation for the specific role of CaNAβ in hypertrophy and its selective activation under conditions of pathologic stress. Disruption of CaNAβ polyproline-dependent anchoring constitutes a rational strategy for therapeutic targeting of CaNAβ-specific signaling responsible for pathological cardiac remodeling in cardiovascular disease deserving of further preclinical investigation.

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