https://scholar.dgist.ac.kr/handle/20.500.11750/16865 Thu, 22 Oct 2026 10:31:18 GMT 2026-10-22T10:31:18Z https://scholar.dgist.ac.kr/handle/20.500.11750/60959 Title: Excessive epithelial mechanosensation drives nociceptive innervation and chronic bladder pain via the PIEZO1-SLC7A11-glutamate axis Author(s): Kim, Min Jung; Noh, Joo Hwan; Lee, Ho Young; Lee, Bohm; Park, Alexander Doh; Oh, Hyeonseo; Kim, Geun-Woo D.; Lee, Hye-Sook; Oh, Yeonsoo; Hwang, Hyeonje; Kim, Chungoo; Lee, Hyeonjong; Li, Xue; Oh, Mi Mi; Lim, Donghoon; Abraham, Soman N.; Cho, Yongcheol; Chi, Sung Wook; Choi, Hae Woong Abstract: Epithelial mechanosensation maintains tissue homeostasis by sensing mechanical stimuli. Dysregulated mechanotransduction has been implicated in chronic pain, yet the molecular link between epithelial stress and persistent sensory dysfunction remains unclear. Here, we report that the mechanosensitive ion channel PIEZO1 is markedly upregulated in bladder epithelial cells under recurrent uropathogenic E. coli infection through interleukin-6 (IL-6)-dependent signaling. PIEZO1 overexpression amplifies mechanotransductioninduced reactive oxygen species (ROS) generation, triggering a homeostatic antioxidant response via the cystine-glutamate antiporter system Xc-(SLC7A11). This protective mechanism inadvertently promotes extracellular glutamate accumulation, driving aberrant sprouting and hyperinnervation of peptidergic nociceptive C fibers into the epithelial layer. This neuroepithelial remodeling sensitizes bladder afferents and induces persistent pain-like states resembling chronic visceral pain and organ dysfunction. Our findings reveal a paradoxical role of epithelial antioxidant defense in promoting pain through the PIEZO1-SLC7A11-glutamate axis and highlight the neuroepithelial interface as a key therapeutic target for infection-induced chronic pain syndromes. Fri, 31 Jul 2026 15:00:00 GMT https://scholar.dgist.ac.kr/handle/20.500.11750/60959 2026-07-31T15:00:00Z https://scholar.dgist.ac.kr/handle/20.500.11750/60411 Title: CSDE1 Associates with TOM20 and Mitochondrial Protein-Encoding mRNAs in Sensory Neurons Author(s): Jin, Hoyong; Jang, Eunsu; Park, Eunhye; Lee, Ju Yeon; Song, Ju Hwan; Cho, Yongcheol Abstract: Mitochondrial proteostasis in neurons relies on the coordinated expression, targeting, and import of a predominantly nuclear-encoded proteome to meet high metabolic demands. Here, we identify the RNA-binding protein cold shock domain containing E1 (CSDE1) as a TOM20-associated factor linked to mitochondrial protein-encoding mRNAs in sensory neurons. CSDE1 immunoprecipitation followed by sequencing from na & iuml;ve dorsal root ganglion tissue revealed association with nuclear-encoded mitochondrial mRNAs enriched for inner membrane/matrix and oxidative phosphorylation pathways. A subset of CSDE1 localized to mitochondria and associated with the outer mitochondrial membrane import receptor TOM20 via its N-terminal region in an RNA-independent manner. In cultured sensory neurons, CSDE1 depletion reduced the mitochondrial-fraction abundance of representative nuclear-encoded electron transport chain mRNAs and decreased the abundance of selected mitochondrial proteins in the mitochondrial fraction. CSDE1 depletion reduced TMRM-positive mitochondrial puncta density along sensory neurites, without significantly increasing MitoSOX-detectable mitochondrial superoxide signals under either basal or oxidative challenge conditions. These findings identify CSDE1 as a TOM20-associated RNA-binding protein linked to mitochondrial protein-encoding transcripts in sensory neurons and support a model in which CSDE1 contributes to mitochondria-associated post-transcriptional regulation. Thu, 30 Apr 2026 15:00:00 GMT https://scholar.dgist.ac.kr/handle/20.500.11750/60411 2026-04-30T15:00:00Z https://scholar.dgist.ac.kr/handle/20.500.11750/57301 Title: Dipeptidyl peptidase 4 as an injury-responsive protein in the mouse sciatic nerve Author(s): Oh, Yeonsoo; Cho, Yongcheol Abstract: Dipeptidyl peptidase 4 (DPP4) is a membrane-bound protease known for its roles in immunity and metabolism; however, its function in the nervous system remains largely unexplored. We found that DPP4 is predominantly expressed in the Schwann cells of the sciatic nerve, and its systemic depletion in postnatal mice resulted in a decline in motor function. Importantly, the inhibition of its proteolytic activity did not affect axon regeneration, indicating that DPP4′s protease activity may not be directly involved in axon regeneration. Instead, we observed a reduction in DPP4 protein levels in the sciatic nerve after injury and increased in serum postinjury, suggesting that DPP4 may be shed into circulation, potentially mediating systemic responses following injury. These findings highlight DPP4′s importance in sensory function and its potential role in systemic responses after peripheral nerve injury. © 2024 The Author(s) Sat, 30 Nov 2024 15:00:00 GMT https://scholar.dgist.ac.kr/handle/20.500.11750/57301 2024-11-30T15:00:00Z https://scholar.dgist.ac.kr/handle/20.500.11750/47691 Title: βPix Guanine Nucleotide Exchange Factor Regulates Regeneration of Injured Peripheral Axons Author(s): Jeon, Yewon; Shin, Yoon Kyung; Kim, Hwigyeong; Choi, Yun Young; Kang, Minjae; Kwon, Younghee; Cho, Yongcheol; Chi, Sung Wook; Shin, Jung Eun Abstract: Axon regeneration is essential for successful recovery after peripheral nerve injury. Although growth cone reformation and axonal extension are crucial steps in axonal regeneration, the regulatory mechanisms underlying these dynamic processes are poorly understood. Here, we identify βPix (Arhgef7), the guanine nucleotide exchange factor for Rac1 GTPase, as a regulator of axonal regeneration. After sciatic nerve injury in mice, the expression levels of βPix increase significantly in nerve segments containing regenerating axons. In regrowing axons, βPix is localized in the peripheral domain of the growth cone. Using βPix neuronal isoform knockout (NIKO) mice in which the neuronal isoforms of βPix are specifically removed, we demonstrate that βPix promotes neurite outgrowth in cultured dorsal root ganglion neurons and in vivo axon regeneration after sciatic nerve crush injury. Activation of cJun and STAT3 in the cell bodies is not affected in βPix NIKO mice, supporting the local action of βPix in regenerating axons. Finally, inhibiting Src, a kinase previously identified as an activator of the βPix neuronal isoform, causes axon outgrowth defects in vitro, like those found in the βPix NIKO neurons. Altogether, these data indicate that βPix plays an important role in axonal regrowth during peripheral nerve regeneration. © 2023 by the authors. Thu, 31 Aug 2023 15:00:00 GMT https://scholar.dgist.ac.kr/handle/20.500.11750/47691 2023-08-31T15:00:00Z