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이철중 대한마취통증의학회 2010 Anesthesia and pain medicine Vol.5 No.4
The prevalence of lumbar spinal pain rose significantly over 10 years. With respect to clinical management of lumbar spinal pain, the most important things are to understand the definition of terms related to lumbar spinal pain. Despite the efforts of the International Association for the Study of Pain, misuse and confusion still continue among clinicians about the definition of terms related to lumbar spinal pain; back pain, referred pain, radicular pain, radiculopathy, and sciatica. Failure to distinguish one type of lumbar spinal pain from the others may lead to unnecessary tests, misdiagnosis, and mismanagement such as an unnecessary surgery. This confusion also exists in developing animal models of lumbar spinal pain by basic scientists. Thus, the exact understandings of definition and physiology of terms related to lumbar spinal pain are essential to manage patients and research the lumbar spinal pain properly.
설인신경통 환자의 박동성 고주파술을 이용한 치료 경험 -증례보고-
이철중,문지연,조주연,김양현,이은형,이상철,김종성 대한마취통증의학회 2006 Korean Journal of Anesthesiology Vol.50 No.1
Glossopharyngeal neuralgia (GPN) is a pain syndrome characterized by unilateral sharp pain in the sensory distribution of the ninth cranial nerve. The first line of treatment for GPN is medical. However, it usually provides only partial relief. Pulsed radiofrequency has been proposed as safe, nondestructive treatment method. We present two cases of secondary GPN that was managed with pulsed radiofrequency by extraoral approach. The results were satisfactory. (Korean J Anesthesiol 2006; 50: 115~8)
Stat2 stability regulation: an intersection between immunity and carcinogenesis
이철중,안현정,Cho Eun Suh,강한창,이주영,이혜숙,조용연 생화학분자생물학회 2020 Experimental and molecular medicine Vol.52 No.-
Signal transducer and activator of transcription (STAT2) is a member of the STAT family that plays an essential role in immune responses to extracellular and intracellular stimuli, including inflammatory reactions, invasion of foreign materials, and cancer initiation. Although the majority of STAT2 studies in the last few decades have focused on interferon (IFN)-α/β (IFNα/β) signaling pathway-mediated host defense against viral infections, recent studies have revealed that STAT2 also plays an important role in human cancer development. Notably, strategic research on STAT2 function has provided evidence that transient regulatory activity by homo- or heterodimerization induces its nuclear localization where it to forms a ternary IFN-stimulated gene factor 3 (ISGF3) complex, which is composed of STAT1 and/or STAT2 and IFN regulatory factor 9 (IEF9). The molecular mechanisms of ISGF3-mediated ISG gene expression provide the basic foundation for the regulation of STAT2 protein activity but not protein quality control. Recently, previously unknown molecular mechanisms of STAT2-mediated cell proliferation via STAT2 protein quality control were elucidated. In this review, we briefly summarize the role of STAT2 in immune responses and carcinogenesis with respect to the molecular mechanisms of STAT2 stability regulation via the proteasomal degradation pathway.
이철중,이미현,조용연 대한암예방학회 2014 Journal of cancer prevention Vol.19 No.3
Background: Extracellular stimulation of cells with growth factors such as epidermal growth factor (EGF) induces cell proliferation and cell transformation. Although fibroblast growth factor (FGF) is a well-known family member of growth factors and acts as a ligand of FGF receptor (FGFR), a receptor tyrosine kinase, in cytoplasmic membrane, the tumor promoter potential of FGF has not been clearly understood. Methods: The role of FGF as a tumor promoter was determined measuring its effects of cell proliferation and transformation by the 3-(4,5-dimethylthiazol-2-yl)-5-(3-carboxymethoxyphenyl)-2-(4-sulfophenyl)-2H-tetrazolium and anchorage-independent cell transformation assays, respectively. The antibody specificity of phospho-RSK2 Tyr529 was determined by Western blotting using a purified FGFR kinase domain in vitro and the membrane fraction of JB6 Cl41 cells ex vivo. The signaling pathways mediated by FGF or EGF were determined by the comparisons of phosphorylation inhibitory efficacy using signaling inhibitors including kaempferol. Results: FGF acted as a tumor promoter. FGF induced cell proliferation by stimulation of G1/S cell cycle transition, and anchorageindependent cell transformation in JB6 Cl41 cells. FGF-induced FGFR phosphorylation was suppressed by kaempferol treatment in a dose dependent manner. Interestingly, FGF stimulation utilized a non-canonical signaling pathway to activate RSK2 and activating transcription factor (ATF)-1, which was not transduced by EGF stimulation. Importantly, kaempferol inhibited tyrosine phosphorylation of FGFR by FGF stimulation and nuclear accumulation of phospho-ATF-1 at Ser63. Moreover, although kaempferol, 4'-N-benzoyl staurosporine(PKC412), 2-(2'-amino-3'-methoxyphenyl)oxanaphthalen-4-one (PD98059) and 1,4-diamino-2,3-dicyano-1,4-bis(2-aminophenylthio)butadiene (U0126) inhibited EGF-induced anchorage-independent cell transformation in JB6 Cl41 cells, FGF-induced cell transformation in soft agar was only inhibited by PKC412 and kaempferol, but not by PD98059 and U0126. Conclusions: FGF acts as a tumor promoter and dual inhibition of kaempferol on the kinase activities of FGFR3 and RSK2 suppresses the FGF-induced neoplastic cell transformation through a non-canonical signaling pathway which is not utilized by EGF stimulation.
F-box Protein βTrCP1 Is a Substrate of Extracellular Signal-regulated Kinase 2
이철중,이가은,안현정,Eun Suh Cho,Weidong Chen,이주영,강한창,이혜숙,조용연 대한암예방학회 2021 Journal of cancer prevention Vol.26 No.3
F-box proteins, consisting of 69 members which are organized into the three subclasses FBXW, FBXL, and FBXO, are the substrate specific recognition subunits of the SKP1-Cullin 1-F-box protein E3 ligase complex. Although βTrCP 1 and 2, members of the FBXW subfamily, are known to regulate some protein stability, molecular mechanisms by which these proteins can recognize proper substrates are unknown. In this study, it was found that βTrCP1 showed strong interaction with members of mitogen-activated protein kinases. Although extracellular signal-regulated kinase (ERK) 3, p38β, and p38δ showed weak interactions, ERK2 specifically interacted with βTrCP1 as assessed by immunoprecipitation. In interaction domain determination experiments, we found that ERK2 interacted with two independent ERK docking sites located in the F-box domain and linker domain, but not the WD40 domain, of βTrCP1. Notably, mutations of βTrCP1 at the ERK docking sites abolished the interaction with ERK2. βTrCP1 underwent phosphorylation by EGF stimulation, while the presence of the mitogen-activated protein kinase kinases inhibitor U0126, genetic silencing by sh-ERK2, and mutation of the ERK docking site of βTrCP1 inhibited phosphorylation. This inhibition of βTrCP1 phosphorylation resulted in a shortened half-life and low protein levels. These results suggest that ERK2-mediated βTrCP1 phosphorylation may induce the destabilization of βTrCP1