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A Possible Role of Kainate Receptors in C2C12 Skeletal Myogenic Cells
Jae-YongPark, JaeheeHan, Seong-GeunHong 대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 5 Pages
대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 2003, Vol.7 No.6 13 375-379 (5 pages)
Ca2 influx appears to be important for triggering myoblast fusion. It remains, however, unclear how Ca2 influx rises prior to myoblast fusion. Recently, several studies suggested that NMDA receptors may be involved in Ca2 mobilization of muscle, and that Ca2 influx is mediated by NMDA receptors in C2C12 myoblasts. Here, we report that other types of ionotropic glutamate receptors, non-NMDA receptors (AMPA and KA receptors), are also involved in Ca2 influx in... -
Prevention of Diabetes Using Adenoviral Mediated Hepatocyte Growth Factor Gene Transfer in Mice
Hye-JeongLee, Hyun-JeongKim, Mee-SookRoh, Jae-IkLee, Sung-WonLee, Dong-SikJung, Duk-KyuKim, Mi-KyoungPark 대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 6 Pages
대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 2003, Vol.7 No.5 3 261-266 (6 pages)
Type 1 diabetes is an organ-specific autoimmune disease caused by the cytotoxic T cells-mediated destruction of the insulin-producing beta cells in the Langerhans pancreatic islets. Hepatocyte growth factor (HGF) is a potent mitogen and a promoter of proliferation of insulin producing beta cells of pancreatic islets. To study the role of HGF via viral vector in the development of streptozotocin (STZ)-induced diabetes in mice, we have developed an adenoviral vector genetically engineered to carry... -
Salicylate Regulates Cyclooxygenase-2 Expression through ERK and Subsequent NF-κB Activation in Osteoblasts
Han-JungChae, Jun-KiLee, Joung-OukByun, Soo-WanChae, Hyung-RyongKim 대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 8 Pages
대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 2003, Vol.7 No.4 8 239-246 (8 pages)
The expression of cyclooxygenase-2 (COX-2) is a characteristic response to inflammation and can be inhibited with sodium salicylate. TNF-α plus IFN-γ can induce extracellular signal-regulated kinase (ERK), IKK, IκB degradation and NF-κB activation. The inhibition of the ERK pathway with selective inhibitor, PD098059, blocked cytokine-induced COX-2 expression and PGE2 release. Salicylate treatment inhibited COX-2 expression induced by TNF-α/IFN-γ and regulated the activation of ERK, IKK and... -
PDTC Inhibits TNF-α-Induced Apoptosis in MC3T3E1 Cells
Han-JungChae, JeehyeonBae 대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 7 Pages
대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 2003, Vol.7 No.4 2 199-205 (7 pages)
Osteoblasts are affected by TNF-α overproduction by immune cells during inflammation. It has been suggested that functional NF-κB sites are involved in TNF-α-induced bone resorption. Thus, we explored the effect of pyrrolidine dithiocarbamate (PDTC), which potently blocks the activation of nuclear factor (NF-κB), on the induction of TNF-α-induced activation of JNK/SAPK, AP-1, cytochrome c, caspase and apoptosis in MC3T3E1 osteoblasts. Pretreatment of the cells with PDTC blocked... -
Alteration of Substrate Specificity by Common Variants, E158K/E308G and V257M, in Human Hepatic Drug-metabolizing Enzyme, Flavin-containing Monooxygenase 3
Jung-KyuLee, Ju-HeeKang, Young-NamCha, Woon-GyeChung, , Chang-ShinPark 대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 6 Pages
대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 2003, Vol.7 No.3 6 157-162 (6 pages)
Our earlier studies found a significant correlation between the activities of ranitidine N-oxidation catalyzed by hepatic flavin-containing monooxygenase (FMO) and the presence of mutations in exon 4 (E158K) and exon 7 (E308G) of the FMO3 gene in Korean volunteers. However, caffeine N-1 demethylation (which is also partially catalyzed by FMO) was not significantly correlated with these FMO3 mutations. In this study, we examined another common mutation (V257M) in exon 6 of FMO3 gene. The V257M... -
Blockade of p38 Mitogen-activated Protein Kinase Pathway Inhibits Interleukin-6 Release and Expression in Primary Neonatal Cardiomyocytes
Han-JungChae, Hyun-KiKim, Wan-KuLee, Soo-WanChae 대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 7 Pages
대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 2002, Vol.6 No.6 7 319-325 (7 pages)
The induction of interleukin-6 (IL-6) using combined proinflammatory agents (LPS/IFN-γ or TNF-α/ IFN-γ) was studied in relation to p38 mitogen-activated protein kinase (MAPK) and NF-κB transcriptional factor in primary neonatal cardiomyocytes. When added to cultures of cardiomyocytes, the combined agents (LPS/IFN-γ or TNF-α/IFN-γ) had stimulatory effect on the production of IL-6 and the elevation was significantly reduced by SB203580, a specific p38 MAPK inhibitor. SB203580 inhibited... -
Analysis of a Sphingosine 1-phosphate Receptor hS1P3 in Rat Hepatoma Cells
Dong-SoonIm 대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 4 Pages
대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 2002, Vol.6 No.3 2 139-142 (4 pages)
in plasma membrane, hS1P3 DNA was transfected into RH7777 rat hepatoma cell line, and the inhibition of forskolin-induced cAMP accumulation and activation of MAP kinases by S1P were tested. In hS1P3 transformants, S1P inhibited forskolin-induced activation of adenylyl cyclase activity by about 80% and activated MAP kinases in dose-dependent and pertussis-toxin (PTX) sensitive manners. In oocytes expressing hS1P3 receptor, S1P evoked Cl conductance. These data suggested that PTX-sensitive... -
GLUT Phosphorylation May be Required to GLUT Translocation Mechanism
Jong-SikHah 대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 10 Pages
대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 2000, Vol.4 No.6 8 487-496 (10 pages)
In this work, GLUTs phosphorylations by a downstream effector of PI3-kinase, PKC-ζ, were studied, and GLUT4 phosphorylation was compared with GLUT2 phosphorylation in relation to the translocation mechanism. Prior to phosphorylation experiment, PKC-ζ kinase activity was determined as 20.76⁑4.09 pmoles Pi/min/25 ng enzymes. GLUT4 was phosphorylated by PKC-ζ and the phosphorylation was increased on the vesicles immunoadsorpted from LDM and on GLUT4 immunoprecipitated from GLUT4-... -
Comparative Effects of PKB-α and PKC-ζ on the Phosphorylation of GLUT4-Containing Vesicles in Rat Adipocytes
Jong-SikHah 대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 8 Pages
대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 2000, Vol.4 No.6 7 479-486 (8 pages)
Insulin stimulates glucose transport in muscle and fat cells by promoting the translocation of glucose transporter (GLUT4) to the cell surface. Phosphatidylinositide 3-kinase (PI3-kinase) has been implicated in this process. However, the involvement of protein kinase B (PKB)/Akt and PKC-ζ, those are known as the downstream target of PI3-kinase in regulation of GLUT4 translocation, is not known yet. An interesting possibility is that these protein kinases phosphorylate GLUT4 directly in this... -
p38 MAPK and NF-κB are Required for LPS-Induced RANTES Production in Immortalized Murine Microglia (BV-2)
Sae-ByeolJangKweon-HaengLee 대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 8 Pages
대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 2000, Vol.4 No.5 1 339-346 (8 pages)
Using murine immortalized microglial cells (BV-2), we examined the regulation of RANTES production stimulated by lipopolysaccharide (LPS), focusing on the role of mitogen-activated protein kinase (MAPK) and nuclear factor (NF)-κB. The result showed that RANTES (regulated upon activation of normal T cell expressed and secreted) was induced at the mRNA and protein levels in a dose- and time-dependent manner in response to LPS. From investigations of second messenger pathways involved in...
