TRPM2-mediated Ca2+ influx induces chemokine production in monocytes that aggravates inflammatory neutrophil infiltration
- Shinichiro Yamamoto, S. Shimizu, Y. Mori
- Biology, MedicineNature Network Boston
- 1 July 2008
It is shown that the plasma membrane Ca2+-permeable channel TRPM2 controls ROS-induced chemokine production in monocytes, which aggravates inflammation and is proposed as a new therapeutic strategy for treating inflammatory diseases.
Selective and direct inhibition of TRPC3 channels underlies biological activities of a pyrazole compound
- Shigeki Kiyonaka, Kenta Kato, Y. Mori
- Biology, ChemistryProceedings of the National Academy of Sciences
- 31 March 2009
TheTRPC3-selective inhibitor Pyr3 is a powerful tool to study in vivo function of TRPC3, suggesting a pharmaceutical potential of Pyr3 in treatments of TR PC3-related diseases such as cardiac hypertrophy.
RIM1 confers sustained activity and neurotransmitter vesicle anchoring to presynaptic Ca2+ channels
- Shigeki Kiyonaka, M. Wakamori, Y. Mori
- BiologyNature Neuroscience
- 1 June 2007
RIM1 association with β in the presynaptic active zone supports release via two distinct mechanisms: sustaining Ca2+ influx through inhibition of channel inactivation, and anchoring neurotransmitter-containing vesicles in the vicinity of VDCCs.
Suppression of hippocampal TRPM7 protein prevents delayed neuronal death in brain ischemia
- Hong-Shuo Sun, M. F. Jackson, M. Tymianski
- BiologyNature Neuroscience
- 1 October 2009
Regional suppression of TRPM7 is feasible, well tolerated and inhibits delayed neuronal death in vivo and prevented ischemia-induced deficits in LTP and preserved performance in fear-associated and spatial-navigational memory tasks.
TRPA1 underlies a sensing mechanism for O2.
- N. Takahashi, T. Kuwaki, Y. Mori
- Biology, ChemistryNature Chemical Biology
- 1 October 2011
A systematic evaluation of transient receptor potential (TRP) cation channels using reactive disulfides with different redox potentials reveals the capability of TRPA1 to sense O(2), and suggests a new O( 2)-sensing mechanism mediated by TRpa1.
Molecular characterization of TRPA1 channel activation by cysteine-reactive inflammatory mediators
- N. Takahashi, Y. Mizuno, Y. Mori
- Biology, ChemistryChannels
- 4 July 2008
It is shown that a variety of inflammatory mediators (15-deoxy-Δ12,14-prostaglandin J2 (15d-PGJ2), nitric oxide (NO), hydrogen peroxide (H2O2), and proton (H+) activate human TRPA1 heterologously expressed in HEK cells.
Activation of RasGRP3 by phosphorylation of Thr-133 is required for B cell receptor-mediated Ras activation.
- Y. Aiba, M. Oh‐hora, T. Kurosaki
- BiologyProceedings of the National Academy of Sciences…
- 23 November 2004
It is demonstrated here that RasGRP3 undergoes phosphorylation at Thr-133 upon B cell receptor cross-linking, thereby resulting in its activation, and suggested that PKC, after being activated by diacylglycerol, phosphorylates Ras GRP3, thereby contributing to its full activation.
Three-dimensional Reconstruction Using Transmission Electron Microscopy Reveals a Swollen, Bell-shaped Structure of Transient Receptor Potential Melastatin Type 2 Cation Channel*
- Y. Maruyama, T. Ogura, C. Sato
- BiologyJournal of Biological Chemistry
- 21 December 2007
This purified FLAG-tagged tetrameric TRPM2 channel, analyzed it using negatively stained electron microscopy, and reconstructed the three-dimensional structure at 2.8-nm resolution indicates that the agonist-binding ADPRase domain and the ion gate in the transmembrane region are separately located in the molecule.
Ca2+‐dependent induction of TRPM2 currents in hippocampal neurons
- M. Olah, M. F. Jackson, J. Macdonald
- BiologyJournal of Physiology
- 1 March 2009
Results indicate that hippocampal pyramidal neurons possess functional TRPM2 channels whose activation by ADPR is functionally coupled to VDCCs and NMDARs through a rise in [Ca2+]i.
Cacnb4 directly couples electrical activity to gene expression, a process defective in juvenile epilepsy
- A. Tadmouri, Shigeki Kiyonaka, M. De Waard
- BiologyEMBO Journal
- 12 September 2012
It is demonstrated that an intact VGCC subunit acts as a repressor recruiting platform to control neuronal gene expression in VGCC-positive mice.
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