scholarly journals Detection in Vivo of Very Rapid Red Light-Induced Calcium-Sensitive Protein Phosphorylation in Etiolated Wheat (Triticum aestivum) Leaf Protoplasts

1993 ◽  
Vol 101 (3) ◽  
pp. 1039-1045 ◽  
Author(s):  
K. M. Fallon ◽  
P. S. Shacklock ◽  
A. J. Trewavas
Keyword(s):  
Triticum Aestivum ◽  
Protein Phosphorylation ◽  
Red Light ◽  
Leaf Protoplasts

Liver Nuclear Protein Phosphorylation in Vivo and the Effect of Triiodothyronine*

Endocrinology ◽  
1980 ◽  
Vol 106 (4) ◽  
pp. 1103-1107 ◽  
Author(s):  
ALDO H. COLEONI ◽  
LESLIE J. DEGROOT
Keyword(s):  
Protein Phosphorylation ◽  
Nuclear Protein

Persistent Luminescence Cr3+ Doped Spinels and Use as Biomarker for In Vivo Imaging

2014 ◽  
Vol 90 ◽  
pp. 157-165
Author(s):  
Suchinder K. Sharma ◽  
D. Gourier ◽  
B. Viana ◽  
T. Maldiney ◽  
E. Teston ◽  
...  
Keyword(s):  
Uv Light ◽  
Red Light ◽  
Band Gap Energy ◽  
Transparency Window ◽  
Persistent Luminescence ◽  
High Brightness ◽  
Mouse Imaging ◽  
Classical Quantum ◽  
Living Tissues

ZnGa2O4(ZGO) is a normal spinel. When doped with Cr3+ions, ZGO:Cr becomes a high brightness persistent luminescence material with an emission spectrum perfectly matching the transparency window of living tissues. It allowsin vivomouse imaging with a better signal to background ratio than classical quantum dots. The most interesting characteristic of ZGO:Cr lies in the fact that its LLP can be excited with red light, well below its band gap energy and in the transparency window of living tissues. A mechanism based on the trapping of carriers localized around a special type of Cr3+ions namely CrN2can explain this singularity. The antisite defects of the structure are the main responsible traps in the persistent luminescence mechanism. When located around Cr3+ions, they allow, via Cr3+absorption, the storage of not only UV light but also all visible light from the excitation source.

scholarly journals Analysis of Flagellar Phosphoproteins from Chlamydomonas reinhardtii

2009 ◽  
Vol 8 (7) ◽  
pp. 922-932 ◽  
Author(s):  
Jens Boesger ◽  
Volker Wagner ◽  
Wolfram Weisheit ◽  
Maria Mittag
Keyword(s):  
Chlamydomonas Reinhardtii ◽  
Protein Phosphorylation ◽  
Proteome Analysis ◽  
Physiological Status ◽  
Phosphorylation Sites ◽  
Cell Organelles ◽  
Flagellar Proteins ◽  
Reversible Protein Phosphorylation ◽  
Cilia And Flagella

ABSTRACT Cilia and flagella are cell organelles that are highly conserved throughout evolution. For many years, the green biflagellate alga Chlamydomonas reinhardtii has served as a model for examination of the structure and function of its flagella, which are similar to certain mammalian cilia. Proteome analysis revealed the presence of several kinases and protein phosphatases in these organelles. Reversible protein phosphorylation can control ciliary beating, motility, signaling, length, and assembly. Despite the importance of this posttranslational modification, the identities of many ciliary phosphoproteins and knowledge about their in vivo phosphorylation sites are still missing. Here we used immobilized metal affinity chromatography to enrich phosphopeptides from purified flagella and analyzed them by mass spectrometry. One hundred forty-one phosphorylated peptides were identified, belonging to 32 flagellar proteins. Thereby, 126 in vivo phosphorylation sites were determined. The flagellar phosphoproteome includes different structural and motor proteins, kinases, proteins with protein interaction domains, and many proteins whose functions are still unknown. In several cases, a dynamic phosphorylation pattern and clustering of phosphorylation sites were found, indicating a complex physiological status and specific control by reversible protein phosphorylation in the flagellum.

scholarly journals Optogenetic activation of spinal microglia triggers chronic pain in mice

PLoS Biology ◽  
2021 ◽  
Vol 19 (3) ◽  
pp. e3001154
Author(s):  
Min-Hee Yi ◽  
Yong U. Liu ◽  
Anthony D. Umpierre ◽  
Tingjun Chen ◽  
Yanlu Ying ◽  
...  
Keyword(s):  
Chronic Pain ◽  
Microglial Activation ◽  
Red Light ◽  
Inflammasome Activation ◽  
Pain Hypersensitivity ◽  
Microglial Phenotype ◽  
C Fiber ◽  
Inward Currents ◽  
Calcium Elevation

Spinal microglia are highly responsive to peripheral nerve injury and are known to be a key player in pain. However, there has not been any direct evidence showing that selective microglial activation in vivo is sufficient to induce chronic pain. Here, we used optogenetic approaches in microglia to address this question employing CX3CR1creER/+: R26LSL-ReaChR/+ transgenic mice, in which red-activated channelrhodopsin (ReaChR) is inducibly and specifically expressed in microglia. We found that activation of ReaChR by red light in spinal microglia evoked reliable inward currents and membrane depolarization. In vivo optogenetic activation of microglial ReaChR in the spinal cord triggered chronic pain hypersensitivity in both male and female mice. In addition, activation of microglial ReaChR up-regulated neuronal c-Fos expression and enhanced C-fiber responses. Mechanistically, ReaChR activation led to a reactive microglial phenotype with increased interleukin (IL)-1β production, which is likely mediated by inflammasome activation and calcium elevation. IL-1 receptor antagonist (IL-1ra) was able to reverse the pain hypersensitivity and neuronal hyperactivity induced by microglial ReaChR activation. Therefore, our work demonstrates that optogenetic activation of spinal microglia is sufficient to trigger chronic pain phenotypes by increasing neuronal activity via IL-1 signaling.

High-accuracy identification and bioinformatic analysis of in vivo protein phosphorylation sites in yeast

PROTEOMICS ◽  
2009 ◽  
Vol 9 (20) ◽  
pp. 4642-4652 ◽  
Author(s):  
Florian Gnad ◽  
Lyris M. F. de Godoy ◽  
Jürgen Cox ◽  
Nadin Neuhauser ◽  
Shubin Ren ◽  
...  
Keyword(s):  
Protein Phosphorylation ◽  
Bioinformatic Analysis ◽  
High Accuracy ◽  
Phosphorylation Sites

Is the in vivo Photosystem I Function Resistant to Photoinhibition? An Answer from Photoacoustic and Far-Red Absorbance Measurements in Intact Leaves

1991 ◽  
Vol 46 (11-12) ◽  
pp. 1038-1044 ◽  
Author(s):  
Michel Havaux ◽  
Murielle Eyletters
Keyword(s):  
Light Stress ◽  
Red Light ◽  
Light Treatment ◽  
High Light ◽  
Saturation Curve ◽  
Strong Light ◽  
Ps Ii ◽  
Fluorescence Measurements ◽  
Ps I

Abstract Preillumination of intact pea leaves with a strong blue-green light of 400 W m-2 markedly inhibited both photoacoustically monitored O2-evolution activity and PS II photochemistry as estimated from chlorophyll fluorescence measurements. The aim of the present work was to examine, with the help of the photoacoustic technique, whether this high-light treatment deteriorated the in vivo PS I function too. High-frequency photoacoustic measurements indicated that photochemical conversion of far-red light energy in PS I was preserved (and even transiently stimulated) whereas photochemical energy storage monitored in light exciting both PS I and PS II was markedly diminished. Low-frequency photoacoustic measurements of the Emerson enhancement showed a spectacular change in the PS II/PS I activity balance in favor of PS I. It was also observed that the linear portion of the saturation curve of the far-red light effect in the Emerson enhancement was not changed by the light treatment. Those results lead to the conclusion that, in contrast to PS II, the in vivo PS I photofunctioning was resistant to strong light stress, thus confirming previous suggestions derived from in vitro studies. Estimation of the redox state of the PS I reaction center by leaf absorbance measurements at ca. 820 nm suggested that, under steady illumination, a considerably larger fraction of PS I centers were in the closed state in high-light pretreated leaves as compared to control leaves, presumably allowing passive adjustment of the macroscopic quantum yield of PS I photochemis­ try to the strongly reduced photochemical efficiency of photoinhibited PS II.

Microtubule-entrained kinase activities associated with the cortical cytoskeleton during cytokinesis

1997 ◽  
Vol 110 (12) ◽  
pp. 1373-1386 ◽  
Author(s):  
G.R. Walker ◽  
C.B. Shuster ◽  
D.R. Burgess
Keyword(s):  
Cell Cycle ◽  
Protein Kinase ◽  
Protein Phosphorylation ◽  
Immunoblot Analysis ◽  
Negative Regulator ◽  
Mitogen Activated Protein Kinase ◽  
Mitotic Apparatus ◽  
Cortical Cytoskeleton

Research over the past few years has demonstrated the central role of protein phosphorylation in regulating mitosis and the cell cycle. However, little is known about how the mechanisms regulating the entry into mitosis contribute to the positional and temporal regulation of the actomyosin-based contractile ring formed during cytokinesis. Recent studies implicate p34cdc2 as a negative regulator of myosin II activity, suggesting a link between the mitotic cycle and cytokinesis. In an effort to study the relationship between protein phosphorylation and cytokinesis, we examined the in vivo and in vitro phosphorylation of actin-associated cortical cytoskeletal (CSK) proteins in an isolated model of the sea urchin egg cortex. Examination of cortices derived from eggs or zygotes labeled with 32P-orthophosphate reveals a number of cortex-associated phosphorylated proteins, including polypeptides of 20, 43 and 66 kDa. These three major phosphoproteins are also detected when isolated cortices are incubated with [32P]ATP in vitro, suggesting that the kinases that phosphorylate these substrates are also specifically associated with the cortex. The kinase activities in vivo and in vitro are stimulated by fertilization and display cell cycle-dependent activities. Gel autophosphorylation assays, kinase assays and immunoblot analysis reveal the presence of p34cdc2 as well as members of the mitogen-activated protein kinase family, whose activities in the CSK peak at cell division. Nocodazole, which inhibits microtubule formation and thus blocks cytokinesis, significantly delays the time of peak cortical protein phosphorylation as well as the peak in whole-cell histone H1 kinase activity. These results suggest that a key element regulating cortical contraction during cytokinesis is the timing of protein kinase activities associated with the cortical cytoskeleton that is in turn regulated by the mitotic apparatus.

Visible red light enhances physiological anagen entry in vivo and has direct and indirect stimulative effects in vitro

2014 ◽  
Vol 47 (1) ◽  
pp. 50-59 ◽  
Author(s):  
Yi-Shuan Sheen ◽  
Sabrina Mai-Yi Fan ◽  
Chih-Chieh Chan ◽  
Yueh-Feng Wu ◽  
Shiou-Hwa Jee ◽  
...  
Keyword(s):  
Red Light

Development of a Red-Light-Controllable Nitric Oxide Releaser to Control Smooth Muscle Relaxation in Vivo

2020 ◽  
Vol 15 (11) ◽  
pp. 2958-2965
Author(s):  
Naoya Ieda ◽  
Yuji Hotta ◽  
Ayaka Yamauchi ◽  
Atsushi Nishikawa ◽  
Takahiro Sasamori ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Smooth Muscle ◽  
Muscle Relaxation ◽  
Red Light ◽  
Smooth Muscle Relaxation
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