In Vivo Imaging of Nuclear Receptor Transcriptional Activity

2016 ◽  
pp. 203-217 ◽  
Author(s):  
D. Alwyn Dart ◽  
Charlotte L. Bevan
Keyword(s):  
Nuclear Receptor ◽  
In Vivo Imaging ◽  
Transcriptional Activity

scholarly journals Orphan nuclear receptor TR3/Nur77 regulates VEGF-A–induced angiogenesis through its transcriptional activity

2006 ◽  
Vol 203 (3) ◽  
pp. 719-729 ◽  
Author(s):  
Huiyan Zeng ◽  
Liuliang Qin ◽  
Dezheng Zhao ◽  
Xiaolian Tan ◽  
Eleanor J. Manseau ◽  
...  
Keyword(s):  
Nuclear Receptor ◽  
Transcriptional Activity ◽  
Umbilical Vein ◽  
Early Response ◽  
Tube Formation ◽  
Orphan Nuclear Receptor ◽  
Dna Binding Domains ◽  
Binding Domains ◽  
Umbilical Vein Endothelial Cells

Vascular endothelial growth factor (VEGF)-A has essential roles in vasculogenesis and angiogenesis, but the downstream steps and mechanisms by which human VEGF-A acts are incompletely understood. We report here that human VEGF-A exerts much of its angiogenic activity by up-regulating the expression of TR3 (mouse homologue Nur77), an immediate-early response gene and orphan nuclear receptor transcription factor previously implicated in tumor cell, lymphocyte, and neuronal growth and apoptosis. Overexpression of TR3 in human umbilical vein endothelial cells (HUVECs) resulted in VEGF-A–independent proliferation, survival, and induction of several cell cycle genes, whereas expression of antisense TR3 abrogated the response to VEGF-A in these assays and also inhibited tube formation. Nur77 was highly expressed in several types of VEGF-A–dependent pathological angiogenesis in vivo. Also, using a novel endothelial cell-selective retroviral targeting system, overexpression of Nur77 DNA potently induced angiogenesis in the absence of exogenous VEGF-A, whereas Nur77 antisense strongly inhibited VEGF-A–induced angiogenesis. B16F1 melanoma growth and angiogenesis were greatly inhibited in Nur77−/− mice. Mechanistic studies with TR3/Nur77 mutants revealed that TR3/Nur77 exerted most of its effects on cultured HUVECs and its pro-angiogenic effects in vivo, through its transactivation and DNA binding domains (i.e., through transcriptional activity).

Fluorescent proteins for in vivo imaging, where's the biliverdin?

2020 ◽  
Vol 48 (6) ◽  
pp. 2657-2667
Author(s):  
Felipe Montecinos-Franjola ◽  
John Y. Lin ◽  
Erik A. Rodriguez
Keyword(s):  
Hydrogen Peroxide ◽  
In Vivo Imaging ◽  
Near Infrared ◽  
Fluorescent Protein ◽  
Fluorescent Proteins ◽  
Fluorescent Imaging ◽  
Infrared Light ◽  
Red Fluorescent Protein ◽  
Color Palette

Noninvasive fluorescent imaging requires far-red and near-infrared fluorescent proteins for deeper imaging. Near-infrared light penetrates biological tissue with blood vessels due to low absorbance, scattering, and reflection of light and has a greater signal-to-noise due to less autofluorescence. Far-red and near-infrared fluorescent proteins absorb light >600 nm to expand the color palette for imaging multiple biosensors and noninvasive in vivo imaging. The ideal fluorescent proteins are bright, photobleach minimally, express well in the desired cells, do not oligomerize, and generate or incorporate exogenous fluorophores efficiently. Coral-derived red fluorescent proteins require oxygen for fluorophore formation and release two hydrogen peroxide molecules. New fluorescent proteins based on phytochrome and phycobiliproteins use biliverdin IXα as fluorophores, do not require oxygen for maturation to image anaerobic organisms and tumor core, and do not generate hydrogen peroxide. The small Ultra-Red Fluorescent Protein (smURFP) was evolved from a cyanobacterial phycobiliprotein to covalently attach biliverdin as an exogenous fluorophore. The small Ultra-Red Fluorescent Protein is biophysically as bright as the enhanced green fluorescent protein, is exceptionally photostable, used for biosensor development, and visible in living mice. Novel applications of smURFP include in vitro protein diagnostics with attomolar (10−18 M) sensitivity, encapsulation in viral particles, and fluorescent protein nanoparticles. However, the availability of biliverdin limits the fluorescence of biliverdin-attaching fluorescent proteins; hence, extra biliverdin is needed to enhance brightness. New methods for improved biliverdin bioavailability are necessary to develop improved bright far-red and near-infrared fluorescent proteins for noninvasive imaging in vivo.

In vivo imaging of beta-amyloid load in transgenic rodents with [F-18]FDDNP microPET

2005 ◽  
Vol 25 (1_suppl) ◽  
pp. S588-S588
Author(s):  
Vladimir Kepe ◽  
Gregory M Cole ◽  
Jie Liu ◽  
Dorothy G Flood ◽  
Stephen P Trusko ◽  
...  
Keyword(s):  
In Vivo Imaging ◽  
Beta Amyloid ◽  
Amyloid Load

In vivo imaging of liver injury and regeneration by functional two-photon microscopy

2016 ◽  
Vol 54 (12) ◽  
pp. 1343-1404
Author(s):  
A Ghallab ◽  
R Reif ◽  
R Hassan ◽  
AS Seddek ◽  
JG Hengstler
Keyword(s):  
Liver Injury ◽  
In Vivo Imaging ◽  
Two Photon Microscopy ◽  
Two Photon

In vivo imaging of human monocyte localization in the early and late inflammatory phase of mouse myocardial infarction

2020 ◽  
Author(s):  
J Iking ◽  
S Hermann ◽  
L Honold ◽  
M Kuhlmann ◽  
M Schäfers ◽  
...  
Keyword(s):  
Myocardial Infarction ◽  
In Vivo Imaging ◽  
Human Monocyte ◽  
Inflammatory Phase

In vivo imaging reveals prostate pathology in the PTEN knockout murine model of prostate cancer

2016 ◽  
Author(s):  
Alysha Bhatti ◽  
Almeida Gilberto Serrano de ◽  
Serena Tommasini Ghelfi ◽  
Alwyn Dart ◽  
Anabel Varela-Carver ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Murine Model ◽  
In Vivo Imaging
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