scholarly journals A Microscopic View of the Store-Operated Calcium Entry-Pathway

2013 ◽  
Vol 2013 ◽  
pp. 1-13 ◽  
Author(s):  
Jonathan Pacheco ◽  
Luis Vaca
Keyword(s):  
Plasma Membrane ◽  
Protein Complexes ◽  
Imaging Techniques ◽  
Calcium Entry ◽  
Point Of View ◽  
Alternative Methods ◽  
Entry Pathway ◽  
Imaging Point ◽  
Store Operated Calcium Entry ◽  
Microscopy Techniques

Orai and STIM are the basic components of a highly complex and regulated mechanism for Ca2+ entry into the cell, known as store-operated calcium entry (SOCE). The activation of plasma membrane G-protein-coupled receptors associated with the phospholipase C cascade results in the rapid and massive production of inositol 1,4,5-triphosphate (IP3). This second messenger triggers the massive efflux of Ca2+ from the endoplasmic reticulum and into the cytosol, resulting in the oligomerization of the stromal interacting molecule (STIM1), a sensor of ER Ca2+. STIM1 oligomers (the so-called puncta) activate Orai channels at the plasma membrane, triggering the influx of Ca2+ into the cytosol. Several microscopy techniques have been implemented to study SOCE, resulting in stunning images of protein complexes assembling in real time. However, little attention has been paid to the findings about this complex mechanism from the imaging point of view, some of which appear to produce contradictory results. In the present review we gathered all the information about SOCE obtained with imaging techniques and contrast these findings with those obtained with alternative methods.

scholarly journals Redox modulation of intracellular free calcium concentration in thyroid FRTL-5 cells: evidence for an enhanced extrusion of calcium

1999 ◽  
Vol 339 (3) ◽  
pp. 621-628 ◽  
Author(s):  
Kid TÖRNQUIST ◽  
Petri VAINIO ◽  
Alexey TITIEVSKY ◽  
Benoit DUGUÉ ◽  
Raimo TUOMINEN
Keyword(s):  
Plasma Membrane ◽  
Calcium Concentration ◽  
Calcium Entry ◽  
Free Calcium ◽  
Redox Modulation ◽  
Kinase C ◽  
Store Operated Calcium Entry ◽  
Intracellular Free Calcium Concentration ◽  
Free Calcium Concentration ◽  
In Cells

Redox modulation is involved in the regulation of the intracellular free calcium concentration ([Ca2+]i) in several cell types. In thyroid cells, including thyroid FRTL-5 cells, changes in [Ca2+]i regulate important functions. In the present study we investigated the effects of the oxidizing compounds thimerosal and t-butyl hydroperoxide on [Ca2+]i in thyroid FRTL-5 cells. Thimerosal mobilized sequestered calcium, and evoked modest store-dependent calcium entry. Both compounds potently attenuated the increase in [Ca2+]i when store-operated calcium entry was evoked with thapsigargin. The entry of barium was not attenuated. Experiments performed with high extracellular pH, in sodium-free buffer and in the presence of vanadate suggested that thimerosal decreased [Ca2+]i by activating a calcium extrusion mechanism, probably a plasma membrane Ca2+-ATPase. All the observed effects were abrogated by the reducing agent β-mercaptoethanol. The mechanism of action was apparently mediated via activation of protein kinase C, as thimerosal potently stimulated binding of [3H]phorbol 12,13-dibutyrate, and was without effect on store-operated calcium entry in cells treated with staurosporine or in cells with down-regulated protein kinase C. Thimerosal did not depolarize the membrane potential, as evaluated using patch-clamp in the whole-cell mode. In immunoprecipitates obtained with an antibody against plasma membrane Ca2+-ATPase, we observed several phosphorylated bands in cells stimulated with thimerosal. In conclusion, we have shown that thimerosal attenuates an increase in [Ca2+]i, probably by activating a plasma membrane Ca2+-ATPase.

scholarly journals S1P triggers cerebral vessel constriction through the store‐operated calcium entry pathway

2010 ◽  
Vol 24 (S1) ◽  
Author(s):  
Kristen Park Hopson ◽  
Jessica Truelove ◽  
Yumei Wang ◽  
Christian Waeber
Keyword(s):  
Calcium Entry ◽  
Cerebral Vessel ◽  
Entry Pathway ◽  
Store Operated Calcium Entry

Mass Spectrometry for Proteomics and Recent Developments in ESI, MALDI and other Ionization Methodologies

2019 ◽  
Vol 16 (4) ◽  
pp. 267-276
Author(s):  
Qurat ul Ain Farooq ◽  
Noor ul Haq ◽  
Abdul Aziz ◽  
Sara Aimen ◽  
Muhammad Inam ul Haq
Keyword(s):  
Mass Spectrometry ◽  
Electrospray Ionization ◽  
New Technologies ◽  
Protein Complexes ◽  
Imaging Techniques ◽  
Desorption Electrospray Ionization ◽  
High Throughput Analysis ◽  
Enhanced Sensitivity ◽  
Recent Developments ◽  
The Way

Background: Mass spectrometry is a tool used in analytical chemistry to identify components in a chemical compound and it is of tremendous importance in the field of biology for high throughput analysis of biomolecules, among which protein is of great interest. Objective: Advancement in proteomics based on mass spectrometry has led the way to quantify multiple protein complexes, and proteins interactions with DNA/RNA or other chemical compounds which is a breakthrough in the field of bioinformatics. Methods: Many new technologies have been introduced in electrospray ionization (ESI) and Matrixassisted Laser Desorption/Ionization (MALDI) techniques which have enhanced sensitivity, resolution and many other key features for the characterization of proteins. Results: The advent of ambient mass spectrometry and its different versions like Desorption Electrospray Ionization (DESI), DART and ELDI has brought a huge revolution in proteomics research. Different imaging techniques are also introduced in MS to map proteins and other significant biomolecules. These drastic developments have paved the way to analyze large proteins of >200kDa easily. Conclusion: Here, we discuss the recent advancement in mass spectrometry, which is of great importance and it could lead us to further deep analysis of the molecules from different perspectives and further advancement in these techniques will enable us to find better ways for prediction of molecules and their behavioral properties.

Design process for serious activities inspired by play and games: a problem solving with a board game from disengamement and gamification processes (Preprint)

2020 ◽  
Author(s):  
Stéphane Goria ◽  
Louise Dupet ◽  
Maëva Négroni ◽  
Gabriel Sega ◽  
Philippe Arnoux ◽  
...  
Keyword(s):  
Cancer Detection ◽  
Serious Games ◽  
Diagnostic Method ◽  
Scientific Literature ◽  
Imaging Techniques ◽  
Point Of View ◽  
Board Game ◽  
Advantages And Disadvantages ◽  
Design Result

BACKGROUND most serious games and other game-based tools are designed as digital games or escape games. They are designed for learning or sometimes in the field of medicine as an aid to care. However, they can also be seen as an aid to research, in our case, to evaluate the advantages and disadvantages of imaging techniques for cancer detection. OBJECTIVE we present a case study of action research on the design of a serious board game intended to consider the advantages and weaknesses of a diagnostic method in a different ways. The goal was to better understand the principles of designing a tool using game or play. METHODS we explicitly implemented another process than gamification to develop a structure reminiscent of the game to highlight the strengths and weaknesses of different imaging techniques from the point of view of the respondents (in this case specialists not directly involved in the project). Based on this feedback and the scientific literature on this subject, we detail the main categories of games and games developed for serious use in order to understand their differences. Concerning the cancer research part to which game contributes, our method is based on questions asked to experts and practitioners of this specialty. RESULTS an expert point of view translation tool in the form of a game has been realized to apprehend a research in a different way. CONCLUSIONS we show with the help of a diagram, some possible design paths leading to this type of design result including two hidden dimensions to consider (the awareness of the game or play by the "player" and his role as a contributor or recipient).

Sign in / Sign up

Export Citation Format

Share Document