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Ishiyama, M.

Publications and source records attributed to Ishiyama, M..

5 recordsLinked to original sources

Fragile X syndrome-linked mutations impair FMRP accumulation in neuronal transport granules

RNA granules are biomolecular condensates that are reversibly formed through multivalent interactions among mRNAs and RNA-binding proteins (RBPs). RNA granules include stress granules and neuronal transport granules, which share common components and functions in translational regulation. Fragile X messenger ribonucleoprotein (FMRP) is an RBP encoded by FMR1, whose loss of function causes fragile X syndrome (FXS), a neurodevelopmental disorder. FMRP is a component of both stress granules and neuronal transport granules. Although several FXS-associated missense mutations in FMRP have been identified, it remains unclear whether these mutations affect the assembly of FMRP into RNA granules. Here, we found that the KH1 domain mutation G266E markedly reduced the accumulation of FMRP in stress granules in HEK293T cells, whereas the KH2 domain mutation I304N had little effect. In addition, both G266E and I304N reduced the accumulation of FMRP within neuronal transport granules in FMRP-deficient mouse cortical neurons. Because G266E and I304N have been reported to impair the RNA-binding and/or RNA-associated functions of FMRP, our findings suggest that the KH1 and KH2 domains are important for the assembly of FMRP into RNA granules. These findings further raise the possibility that impaired RNA granule assembly may contribute to the pathogenesis of FXS and other neurodevelopmental disorders.

neuroscience↗

A small-molecule fluorescent probe for live-cell imaging of endocytosis

Endocytosis involves plasma membrane-derived vesicles for the recycling of intra- and extracellular components. Increasing evidence suggests that endocytosis is related to maintaining intracellular homeostasis and defense against disease. Consequently, investigation of the endocytic pathway attracts considerable scientific interest. This study reports live-cell imaging of endocytosis using the newly-developed fluorescent probe ECGreen. We demonstrate that ECGreen is not membrane permeable and its fluorescence signal increases in acidic conditions. Because of these characteristics, ECGreen remains on the plasma membrane, and then shows increased fluorescence when it is internalized into the acidic vesicles formed in the endocytic process. ECGreen allows direct observation of the internalized vesicle; it is a valuable new probe for endocytic imaging.

biochemistry↗

A Simple Fluorescence Assay for Cystine Uptake via the xCT in Cells using Selenocystine and a Fluorescent Probe

The cystine/glutamate antiporter (xCT) is a crucial transporter that maintains cellular redox balance by regulating intracellular glutathione synthesis via cystine uptake. However, no robust and simple method to determine the cystine uptake activity of xCT is currently available. We have developed a method to measure the xCT activity via the reaction of selenocysteine and fluorescein O,O'-diacrylate (FOdA). Selenocystine, a cystine analog, is transported into cells through xCT on the cell membrane. The amount of the transported selenocystine was then determined by a reaction using tris(2-carboxyethyl)phosphine (TCEP) and FOdA in a weak acidic buffer at pH 6. Using this method, the cystine uptake activity of xCT in various cells, and the inhibitory efficiency of xCT inhibitors, were evaluated.

cell biology↗

Amphipathic Fluorescent Dyes for Sensitive and Long-Term Monitoring of Plasma Membranes

The plasma membrane (PM) plays a critical role in many cellular processes, and PM dysfunction is a key biomarker related to the cell status and several diseases. Imaging techniques using small fluorescent probes have become increasingly important tools for visualizing living cells, particularly their PMs. Among the commercially available PM-specific probes, PKH dyes are widely used; however, the utility of these dyes is limited by their short membrane retention times and high cytotoxicity. Herein, PlasMem Bright Green and Red are implemented as new PM-specific fluorescent probes, which employ a polycyclic aromatic fluorophore to improve their retention ability and a strong acid moiety to reduce their transmembrane diffusion and cytotoxicity. We demonstrate that the long retention and low cytotoxicity of the PlasMem Bright dyes enable them to be applied for observing neuronal PMs and monitoring PM dynamics involving the endocytic pathway. Furthermore, we successfully detected mitochondria in nerve axons over long periods using PlasMem Bright dyes. Finally, the combined use of exosome staining probes and PlasMem Bright dyes allowed clear visualization of the endocytic pathway. TOC graphic O_FIG_DISPLAY_L [Figure 1] M_FIG_DISPLAY C_FIG_DISPLAY

biochemistry↗

New Lipophilic Fluorescent Dyes for Exosome Labeling: Monitoring of Cellular Uptake of Exosomes

We have developed three types of exosomal membrane binding fluorescent probes, Mem Dye-Green, Mem Dye-Red and Mem Dye-Deep Red, to monitor exosome uptake into cells. The dyes contain a cyanine group as a fluorescent scaffold, which allows for highly sensitive fluorescence imaging of the exosome. These dyes can also be used to observe the dynamics of exosomes in live cells. The use of PKH dyes (Figure 1), which are currently the most widely-used fluorescent probes for exosome labeling, has some limitations. For example, PKH dyes tend to aggregate to form exosome-like nanoparticles, and these nanoparticles are uptaken by cells. Moreover, Mehdi suggested that the use of PKH dyes triggers an enlargement of the exosome size owing to membrane fusion or intercalation. To overcome the limitations of PKH dyes, we introduce amphiphilic moieties to the cyanine. To investigate the characteristics of the Mem Dyes as exosome labeling probes, we perform nanoparticle tracking analysis (NTA), zeta potential measurement and confocal microscopy. The Mem Dyes show excellent performance for exosome labeling (no aggregation and less size shift). O_FIG O_LINKSMALLFIG WIDTH=91 HEIGHT=200 SRC="FIGDIR/small/931295v1_fig1.gif" ALT="Figure 1"> View larger version (8K): org.highwire.dtl.DTLVardef@e978aeorg.highwire.dtl.DTLVardef@1f208cdorg.highwire.dtl.DTLVardef@11fdb1dorg.highwire.dtl.DTLVardef@6a7373_HPS_FORMAT_FIGEXP M_FIG O_FLOATNOFigure 1.C_FLOATNO Chemical structure of PKH26. C_FIG

biochemistry↗