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Choi, Soo Young,Park, Jinseu,Kang, Young Hee,Lee, Yoon,Lee, Hangyu,Rhim, Hyangshuk The Korea Science and Technology Center 2000 BMB Reports Vol.33 No.4
The human immunodeficiency virus type 1 (HIV-1), transactivator of transcription (Tat), is one of the viral gene products that is essential for HIV-1 replication. The HIV-1 Tat protein regulates transcription from an HIV-1 long terminal repeat (LTR) and affects the gene expression of cellular proteins during infection. In order to develop an expression system to overexpress and simply purify HIV-1 Tat proteins, the HIV-1 Tat coding sequences that contain one or two exons were amplified using PCR and cloned into a pET vector, which contains a consecutive stretch of six histidine residues at the amino-terminus. The reconstituted vectors were overexpressed in the E. coli strain and the soluble recombinant proteins were purified to be homogeneity in a single step by Ni??-nitrilotriacetic acid Sepharose chromatography under nondenaturing conditions. Recombinant HIV-1 LTR promoter in a dose-dependent manner when introduced into mammalian cells. In addition, treatment of human endothelial cells with purified Tat proteins resulted in a significant increase in the level of vascular cell adhesion molecule-1 (VCAM-1) expression. These results indicate that the recombinant HIV-1 Tat proteins are active in transactivating viral and cellular described in this study will facilitate in characterizing the biological functions of the Tat proteins.
Choi, Soo Young,Bahn, Jae Hoon,Park, Jinseu,Jin, Li Hua,Lee, Byung Ryong,Kim, Chung Kwon,Cho, Sung-Woo,Jeon, Seong Gyu,Cho, Yong Joon,Jang, Joong Sik,Kwon, Oh-Shin The Korea Science and Technology Center 2000 BMB Reports Vol.33 No.4
The succinic semialdehyde dehydrogenase from bovine brain was inactivated by treatment with phenylglyoxal, a reagent that specifically modifies arginine residues. The inhibition at various phenylglyoxal ocncentrations shows pseudo-first-order kinetics with an apparent second-order rate constant of 30 M-¹min-¹ for inactivation. Partial pretection against inactivation was provided by the coenzyme NAD+, but not by the substrate succinic semialdehyde. Spectrophotoetric studies indicated that complete inactivation of the enzyme resulted from the binding of 2 mol phenylglyoxal per mol of enzyme. These results suggest that essential arginine residues, located at or near the coenzyme-bindig site, are connected with the catalytic activity of brain succinic semialdehyde dehydrogenase.
Kim, Hyun Ah,Won Kim, Dae,Park, Jinseu,Choi, Soo Young BioMed Central 2006 ARTHRITIS RESEARCH AND THERAPY Vol.8 No.4
<P>This study was performed to investigate the transduction of a full-length superoxide dismutase (SOD) protein fused to transactivator of transcription (Tat) into human chondrocytes, and to determine the regulatory function of transduced Tat-SOD in the inflammatory cytokine induced catabolic pathway. The pTat-SOD expression vector was constructed to express the basic domain of HIV-1 Tat as a fusion protein with Cu, Zn-SOD. We also purified histidine-tagged SOD without an HIV-1 Tat and Tat-GFP as control proteins. Cartilage samples were obtained from patients with osteoarthritis (OA) and chondrocytes were cultured in both a monolayer and an explant. For the transduction of fusion proteins, cells/explants were treated with a variety of concentrations of fusion proteins. The transduced protein was detected by fluorescein labeling, western blotting and SOD activity assay. Effects of transduced Tat-SOD on the regulation of IL-1 induced nitric oxide (NO) production and inducible nitric oxide synthase (iNOS) mRNA expression was assessed by the Griess reaction and reverse transcriptase PCR, respectively. Tat-SOD was successfully delivered into both the monolayer and explant cultured chondrocytes, whereas the control SOD was not. The intracellular transduction of Tat-SOD into cultured chondrocytes was detected after 1 hours, and the amount of transduced protein did not change significantly after further incubation. SOD enzyme activity increased in a dose-dependent manner. NO production and iNOS mRNA expression, in response to IL-1 stimulation, was significantly down-regulated by pretreatment with Tat-SOD fusion proteins. This study shows that protein delivery employing the Tat-protein transduction domain is feasible as a therapeutic modality to regulate catabolic processes in cartilage. Construction of additional Tat-fusion proteins that can regulate cartilage metabolism favorably and application of this technology in <I>in vivo </I>models of arthritis are the subjects of future studies.</P>
Tat-indoleamine 2,3-dioxygenase 1 elicits neuroprotective effects on ischemic injury
박정환,Dae Won Kim,Min Jea Shin,Jinseu Park,한규형,이근욱,Jong Kook Park,Yeon Joo Choi,여현지,여은지,Eun Jeong Sohn,Hyoung-Chun Kim,Eun-Joo Shin,Eun-Joo Shin,김덕수,조용준,Won Sik Eum,최수영 생화학분자생물학회 2020 BMB Reports Vol.53 No.11
It is well known that oxidative stress participates in neuronal cell death caused production of reactive oxygen species (ROS). The increased ROS is a major contributor to the development of ischemic injury. Indoleamine 2,3-dioxygenase 1 (IDO-1) is involved in the kynurenine pathway in tryptophan metabolism and plays a role as an anti-oxidant. However, whether IDO-1 would inhibit hippocampal cell death is poorly known. Therefore, we explored the effects of cell permeable Tat-IDO-1 protein against oxidative stress-induced HT-22 cells and in a cerebral ischemia/reperfusion injury model. Transduced Tat-IDO-1 reduced cell death, ROS production, and DNA fragmentation and inhibited mitogen-activated protein kinases (MAPKs) activation in H2O2 exposed HT-22 cells. In the cerebral ischemia/ reperfusion injury model, Tat-IDO-1 transduced into the brain and passing by means of the blood-brain barrier (BBB) significantly prevented hippocampal neuronal cell death. These results suggest that Tat-IDO-1 may present an alternative strategy to improve from the ischemic injury.
( Su Jin Lee ),( Hyung Kyung Kang ),( Yeon Joo Choi ),( Won Sik Eum ),( Jinseu Park ),( Soo Young Choi ),( Hyeok Yil Kwon ) 생화학분자생물학회(구 한국생화학분자생물학회) 2018 BMB Reports Vol.51 No.10
Pancreatic beta cell destruction and dysfunction induced by cytokines is a major cause of type 1 diabetes. Paraoxonase 1 (PON1), an arylesterase with antioxidant activity, has been shown to play an important role in preventing the development of diabetes in transgenic mice. However, no studies have examined the anti-diabetic effect of PON1 delivered to beta cells using protein transduction. In this study, we expressed the cell-permeable PON1 fused with PEP-1 protein transduction domain (PEP-1-PON1) to investigate whether transduced PEP-1-PON1 protects beta cells against cytokine-induced cytotoxicity. PEP-1-PON1 was effectively delivered to INS-1 cells and prevented cytokine-induced cell destruction in a dose-dependent manner. Transduced PEP-1-PON1 significantly reduced the levels of reactive oxygen species (ROS) and nitric oxide (NO), DNA fragmentation, and expression of inflammatory mediators, endoplasmic reticulum (ER) stress proteins, and apoptosis-related proteins in cytokine-treated cells. Moreover, transduced PEP-1-PON1 restored the decrease in basal and glucose-stimulated insulin secretion induced by cytokines. These data indicate that PEP-1-PON1 protects beta cells from cytokine-induced cytotoxicity by alleviating oxidative/nitrosative stress, ER stress, and inflammation. Thus, PEP-1-mediated PON1 transduction might be an effective method to reduce the extent of destruction and dysfunction of pancreatic beta cells in autoimmune diabetes. [BMB Reports 2018; 51(10): 538-543]
A Transparent artificial dura mater made of silk fibroin inhibits inflammation in craniotomized rats
Dae Won Kim,Won Sik Eum,Sang Ho Jang,Jinseu Park,Dong-Hwa Heo,Sung-Min Cho,Seung-Hoon Sheen,Hae-Ran Lee,Hae Young Kweon,Seok-Woo Kang,Kwang-Gill Lee,Se Youn Cho,Hyoung-Joon Jin,Yong-Jun Cho,Soo Young 한국실험동물학회 2010 한국실험동물학회 학술발표대회 논문집 Vol.2010 No.8