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Graphene quantum dots prevent α-synucleinopathy in Parkinson’s disease
Kim, Donghoon,Yoo, Je Min,Hwang, Heehong,Lee, Junghee,Lee, Su Hyun,Yun, Seung Pil,Park, Myung Jin,Lee, MinJun,Choi, Seulah,Kwon, Sang Ho,Lee, Saebom,Kwon, Seung-Hwan,Kim, Sangjune,Park, Yong Joo,Kinos Nature Publishing Group 2018 Nature nanotechnology Vol.13 No.9
Kim, Sangjune,Park, Do-Young,Lee, Dohyun,Kim, Wanil,Jeong, Young-Hun,Lee, Juhyun,Chung, Sung-Kee,Ha, Hyunjung,Choi, Bo-Hwa,Kim, Kyong-Tai American Society for Microbiology 2014 Molecular and cellular biology Vol.34 No.4
<P>Misfolding of proteins containing abnormal expansions of polyglutamine (polyQ) repeats is associated with cytotoxicity in several neurodegenerative disorders, including Huntington's disease. Recently, the eukaryotic chaperonin TRiC hetero-oligomeric complex has been shown to play an important role in protecting cells against the accumulation of misfolded polyQ protein aggregates. It is essential to elucidate how TRiC function is regulated to better understand the pathological mechanism of polyQ aggregation. Here, we propose that vaccinia-related kinase 2 (VRK2) is a critical enzyme that negatively regulates TRiC. In mammalian cells, overexpression of wild-type VRK2 decreased endogenous TRiC protein levels by promoting TRiC ubiquitination, but a VRK2 kinase-dead mutant did not. Interestingly, VRK2-mediated downregulation of TRiC increased aggregate formation of a polyQ-expanded huntingtin fragment. This effect was ameliorated by rescue of TRiC protein levels. Notably, small interference RNA-mediated knockdown of VRK2 enhanced TRiC protein stability and decreased polyQ aggregation. The VRK2-mediated reduction of TRiC protein levels was subsequent to the recruitment of COP1 E3 ligase. Among the members of the COP1 E3 ligase complex, VRK2 interacted with RBX1 and increased E3 ligase activity on TRiC <I>in vitro</I>. Taken together, these results demonstrate that VRK2 is crucial to regulate the ubiquitination-proteosomal degradation of TRiC, which controls folding of polyglutamine proteins involved in Huntington's disease.</P>
Macro Histone H2A1.2 (MacroH2A1) Protein Suppresses Mitotic Kinase VRK1 during Interphase
Kim, Wanil,Chakraborty, Goutam,Kim, Sangjune,Shin, Joon,Park, Choon-Ho,Jeong, Min-Woo,Bharatham, Nagakumar,Yoon, Ho Sup,Kim, Kyong-Tai American Society for Biochemistry and Molecular Bi 2012 The Journal of biological chemistry Vol.287 No.8
Kim, Seong-Hoon,Lyu, Ha-Na,Kim, Ye Seul,Jeon, Yong Hyun,Kim, Wanil,Kim, Sangjune,Lim, Jong-Kwan,Lee, Ho Won,Baek, Nam-In,Choi, Kwan-Yong,Lee, Jaetae,Kim, Kyong-Tai American Society for Pharmacology and Experimental 2015 The Journal of Pharmacology and Experimental Thera Vol.352 No.1
<P>To date, many anticancer drugs have been developed by directly or indirectly targeting microtubules, which are involved in cell division. Although this approach has yielded many anticancer drugs, these drugs produce undesirable side effects. An alternative strategy is needed, and targeting mitotic exit may be one alternative approach. Localization of phosphorylated barrier-to-autointegration factor (BAF) to the chromosomal core region is essential for nuclear envelope compartment relocalization. In this study, we isolated brazilin from Caesalpinia sappan Leguminosae and demonstrated that it inhibited BAF phosphorylation in vitro and in vivo. Moreover, we demonstrated direct binding between brazilin and BAF. The inhibition of BAF phosphorylation induced abnormal nuclear envelope reassembly and cell death, indicating that perturbation of nuclear envelope reassembly could be a novel approach to anticancer therapy. We propose that brazilin isolated from C. sappan may be a new anticancer drug candidate that induces cell death by inhibiting vaccinia-related kinase 1-mediated BAF phosphorylation.</P>
Therapeutic Approaches for Inhibition of Protein Aggregation in Huntington's Disease
Kim, Sangjune,Kim, Kyong-Tai The Korean Society for Brain and Neural Science 2014 Experimental Neurobiology Vol.23 No.1
<P>Huntington's disease (HD) is a late-onset and progressive neurodegenerative disorder that is caused by aggregation of mutant huntingtin protein which contains expanded-polyglutamine. The molecular chaperones modulate the aggregation in early stage and known for the most potent protector of neurodegeneration in animal models of HD. Over the past decades, a number of studies have demonstrated molecular chaperones alleviate the pathogenic symptoms by polyQ-mediated toxicity. Moreover, chaperone-inducible drugs and anti-aggregation drugs have beneficial effects on symptoms of disease. Here, we focus on the function of molecular chaperone in animal models of HD, and review the recent therapeutic approaches to modulate expression and turn-over of molecular chaperone and to develop anti-aggregation drugs.</P>
Kim, Sangjune,Lee, Dohyun,Lee, Juhyun,Song, Haengjin,Kim, Hyo-Jin,Kim, Kyong-Tai American Society for Microbiology 2015 Molecular and cellular biology Vol.35 No.10
<P>Molecular chaperones monitor the proper folding of misfolded proteins and function as the first line of defense against mutant protein aggregation in neurodegenerative diseases. The eukaryotic chaperonin TRiC is a potent suppressor of mutant protein aggregation and toxicity in early stages of disease progression. Elucidation of TRiC functional regulation will enable us to better understand the pathological mechanisms of neurodegeneration. We have previously shown that vaccinia-related kinase 2 (VRK2) downregulates TRiC protein levels through the ubiquitin-proteasome system by recruiting the E3 ligase COP1. However, although VRK2 activity was necessary in TRiC downregulation, the phosphorylated substrate was not determined. Here, we report that USP25 is a novel TRiC interacting protein that is also phosphorylated by VRK2. USP25 catalyzed deubiquitination of the TRiC protein and stabilized the chaperonin, thereby reducing accumulation of misfolded polyglutamine protein aggregates. Notably, USP25 deubiquitinating activity was suppressed when VRK2 phosphorylated the Thr<SUP>680</SUP>, Thr<SUP>727</SUP>, and Ser<SUP>745</SUP> residues. Impaired USP25 deubiquitinating activity after VRK2-mediated phosphorylation may be a critical pathway in TRiC protein destabilization.</P>
Clinical Characteristics of Patients Diagnosed With Odontogenic Rhinosinusitis After Dental Implants
Kim Sangjun,Lee Eun Soo,Bae Woo Yong,Kim Chul-Hoon,Yun Ji-Eon 대한비과학회 2022 Journal of rhinology Vol.29 No.1
Background and Objectives: With the ongoing development of intraoral surgical treatment and invasive dental treatments such as implants, odontogenic rhinosinusitis (ORS) is on the rise. ORS related to dental implants accounts for 8% to 37% of cases. The purpose of this study is to define the characteristics of patients with ORS related to dental implants.Methods: From 2015 to 2019, the medical records of 15 patients who developed maxillary sinus disease after receiving dental implants were retrospectively analyzed among patients who visited the ear nose and throat and dentistry departments. We reviewed the chief complaint, assessment, diagnosis, treatment and prognosis of these patients.Results: Of the 15 patients, all were diagnosed with ORS. One patient with a post-operative cheek cyst, 1 with fungal sinusitis, 1 with an inverted papilloma, 1 with chronic rhinosinusitis, and 1 with a radicular cyst were diagnosed after surgery. Endoscopic sinus surgery was performed in 14 patients and 2 patients underwent a combined operation. One patient improved after medical treatment. The follow-up period was about 8.6 months. No recurrence was found in any of the patients.Conclusion: If an implant problem is suspected based on history-taking and physical examination, active consultation with dentistry is needed to diagnose ORS.