Shinji MATSUDA (松田 信爾)

Abstract

Persistent organic room‐temperature phosphorescence (RTP) enables high‐resolution afterglow bioimaging, independent of autofluorescence. However, the yield of organic RTP in the long‐wavelength region is generally low, which limits the high‐resolution information that can be obtained from the long‐wavelength region. Moreover, this makes it impossible to obtain multicolor and high‐resolution afterglow images. This report describes a molecule containing no atoms from the fourth or higher period that exhibits efficient red RTP in high yield. A molecule with red phosphorescent chromophores substituted with multiple phenylthio groups reached an RTP yield of 46.3% and an RTP lifetime of 0.43 s in an appropriate crystalline host medium. The selective lower‐occupied through‐bond or through‐space interactions among molecules significantly enhance the phosphorescence in the long‐wavelength region. The highly efficient and bright red persistent RTP induces a red afterglow from individual nanoparticles. Tuning the selective lower‐occupied through‐bond or through‐space interactions allows for the design of high‐performance RTP dyes and offers a novel approach to explore high‐resolution full‐color afterglow imaging.

Long-term depression (LTD) is a form of synaptic plasticity thought to be the cellular basis of experience-dependent learning and memory. LTD is caused by an activity-dependent decrease in cell surface α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA)-type glutamate receptors (AMPA receptors) at the postsynaptic sites. However, the mechanism through which AMPA receptors are removed from the cell surface via neuronal activity is not fully understood. In this study, we showed that small interfering RNA (siRNA)-mediated knockdown of sterile alpha and toll/interleukin receptor motif containing 1 (SARM1) in cultured hippocampal neurons prevented the N-methyl-d-aspartate (NMDA)-induced reduction in cell surface AMPA receptors. However, the control RNA did not affect NMDA-mediated AMPA receptor trafficking. Overexpression of the siRNA-resistant form of SARM1 in SARM1-knocked-down neurons restored AMPA receptor trafficking. However, overexpression of SARM1, which lacks the mitochondrial transport signal, in the SARM1-knocked-down neurons did not restore NMDA-dependent AMPA receptor endocytosis. Moreover, the inhibition of the NADase activity of SARM1 blocked the NMDA-induced reduction of cell surface AMPA receptors. These results suggest that both the mitochondrial localization and NADase activity of SARM1 are essential for NMDA receptor-dependent AMPA receptor internalization in the hippocampal neurons.