Dae Joong Kim
Kangwon National University
Network
Latest external collaboration on country level. Dive into details by clicking on the dots.
Publication
Featured researches published by Dae Joong Kim.
Experimental and Molecular Medicine | 2006
Kyoung-Jin Lee; Yoo Mih Kim; Daeyoung Kim; Dooil Jeoung; Kyuhyung Han; Seung-Taek Lee; Yun-Sil Lee; Kyeong Han Park; Jeong Hyun Park; Dae Joong Kim; Jang-Hee Hahn
Heat shock protein 70 (Hsp70) release and its effects on pro-inflammatory cytokine production have been controversial. In this study, we investigated whether Hsp70 could be released from monocytes and activates matrix metalloproteinase-9 (MMP-9) gene expression. Hsp70 overexpression in human monocytic cell line U937 was found to increase PMA- induced MMP-9 expression and enhance cell motility. Hsp70 cDNA transfectants released Hsp70 protein into culture supernatants, and a part of released Hsp70 subsequently was bound to the surface of U937 cells. Addition of culture medium containing the extracelluar Hsp70 led to an increase not only in proMMP-9 secretion, but also the invasiveness of U937 cells through Matrigel or human umbilical vascular endothelial cells (HUVEC) in vitro. Immunodepletion of Hsp70 abolished its effect on MMP-9 expression. The released Hsp70 activated nuclear factor κ B (NF-κ B) and activating protein-1 (AP-1), which led to the activation of MMP-9 transcription. Taken together, these results suggest that extracellular Hsp70 induces the expression of MMP-9 gene through activation of NF-κ B and AP-1.
Experimental and Molecular Medicine | 2004
Kyoung-Jin Lee; Hyuna Kim; Pyeung-Hyeun Kim; Hansoo Lee; Kyung-Ran Ma; Jeong Hyun Park; Dae Joong Kim; Jang-Hee Hahn
During chronic inflammatory response, mono- cytes/macrophages produce 92-kDa matrix metalloproteinase-9 (MMP-9), which may contribute to their extravasation, migration and tissue remodeling. Activation of peroxisome proliferator- activated factor receptor-γ (PPAR-γ) has been shown to inhibit MMP-9 activity. To evaluate whether ox-LDL, a PPAR-γ activator, inhibits PMA-induced MMP-9 expression and activity, and if so, whether CD36 and PPAR-γ are involved in this process, we investigated the effect of ox-LDL on MMP-9 expression and activity in PMA-activated human monocytic cell line U937. PMA-induced MMP-9 expression and activity were suppressed by the treatment with ox-LDL (50 µg/ml) or PPAR-γ activators such as troglitazone (5 µM), ciglitazone (5 µM), and 15d- PGJ2 (1 µM) for 24 h. This ox-LDL or PPAR-γ activator-mediated inhibition of µM P-9 activity was diminished by the pre-treatment of cells with a blocking antibody to CD36, or PGF2a (0.3 µM), which is a PPAR-γ inhibitor, as well as overexpression of a dominant-negative form of CD36. Taken together, these results suggest that ox-LDL suppresses PMA-induced MMP-9 expression and activity through CD36-mediated activation of PPAR-γ.
Experimental and Molecular Medicine | 2008
Kyoung-Jin Lee; Eun-Soo Ha; Minkyoung Kim; Sang-Hoon Lee; Jae Sung Suh; Sun-Hee Lee; Kyeong Han Park; Jeong Hyun Park; Dae Joong Kim; Kang D; Byung-Chul Kim; Dooil Jeoung; Young-Kyoun Kim; Ho-dirk Kim; Jang-Hee Hahn
Oxidized LDL (OxLDL), a causal factor in atherosclerosis, induces the expression of heat shock proteins (Hsp) in a variety of cells. In this study, we investigated the role of CD36, an OxLDL receptor, and peroxisome proliferator-activated receptor γ (PPARγ) in OxLDL-induced Hsp70 expression. Overexpression of dominant-negative forms of CD36 or knockdown of CD36 by siRNA transfection increased OxLDL-induced Hsp70 protein expression in human monocytic U937 cells, suggesting that CD36 signaling inhibits Hsp70 expression. Similar results were obtained by the inhibition of PPARγ activity or knockdown of PPARγ expression. In contrast, overexpression of CD36, which is induced by treatment of MCF-7 cells with troglitazone, decreased Hsp70 protein expression induced by OxLDL. Interestingly, activation of PPARγ through a synthetic ligand, ciglitazone or troglitazone, decreased the expression levels of Hsp70 protein in OxLDL-treated U937 cells. However, major changes in Hsp70 mRNA levels were not observed. Cycloheximide studies demonstrate that troglitazone attenuates Hsp70 translation but not Hsp70 protein stability. PPARγ siRNA transfection reversed the inhibitory effects of troglitazone on Hsp70 translation. These results suggest that CD36 signaling may inhibit stress-induced gene expression by suppressing translation via activation of PPARγ in monocytes. These findings reveal a new molecular basis for the anti-inflammatory effects of PPARγ.
Journal of Korean Medical Science | 2000
Joong Seok Seo; Sang Yong Lee; Kyung Joon Won; Dae Joong Kim; Dong Seup Sohn; Ki Min Yang; Sang Ho Cho; Jung Duck Park; Kyung-Hoon Lee; Ho Dirk Kim
Korean Journal of Physical Anthropology | 2009
Chan Woong Kim; Jee Hee Kim; Kyeong Han Park; Dae Joong Kim; Jang Hee Hahn; Young Il Lee; Young Cheol Choi; Jeong Hyun Park
Korean Journal of Physical Anthropology | 2009
Seung Oh Kim; Min-kyung Kim; Seung Su Lee; Byung Ryul Cho; Dae Joong Kim
Korean Circulation Journal | 2001
Dae Joong Kim; Sang Yong Lee; Jeong Hyun Park; Jang Hee Hahn; Sung Man Park; Jin Sook Jeong; Ho Dirk Kim
Korean Journal of Physical Anthropology | 2007
Seung Oh Kim; Min Kyoung Kim; Dong Hyun Suh; Chan Woong Kim; Seung Muk Cho; Jang Hee Hahn; Jeong Hyun Park; Kyoung Han Park; Dae Joong Kim
Korean Journal of Physical Anthropology | 2007
Sun Mi Kim; Jae Myoung Kim; Joon Seong Jeon; Zoon Seog Ahn; Dae Young Kim; Jae Sung Suh; Kyoung Han Park; Jung Hyun Park; Dae Joong Kim; Jang Hee Hahn
Korean Journal of Medical Education | 2007
Jee Hee Kim; Tae Young Moon; Young Mee Lee; Kyoung-Han Park; Dae Joong Kim; Jang Hee Hahn; Chan Woong Kim; Jeong Hyun Park