EnvironmetaI Education through Outdoor Education

1996Environmental problems are mounting at an unprecedented rate in our society. The news media reported recently that fish died by hundreds of thousands in a river due to waterborne toxic wastes which were illegally discharged into a river. The large Shi-hwa lake, a reclaimed lake in tidal area on the west coast near the city of Ansan, where one of the largest industrial estates in the capital region is located, had to release its water back into the ocean because the water was so polluted by waterborne industrial wastes and municipal wastes that it could not be irrigated onto farm land. These are only some of examples to indicate how our environmental problems are increasingly serious, not only by a few industrial plant managers' illegal actions and by our negligent administrative practices in applying strict environmental laws against illegal and harmful environmental damages, but also by the irresponsible behavior of the public in general

Orphan G protein-coupled receptors MrgA1 and MrgC11 are distinctively activated by RF-amide-related peptides through the G{alpha}q/11 pathway

MrgA1 and MrgC11 belong to a recently identified family of orphan G-protein coupled receptors, called mrgs (mas-related genes). They are only expressed in a specific subset of sensory neurons that are known to detect painful stimuli. However, the precise physiological function of Mrg receptors and their underlying mechanisms of signal transduction are not known. We therefore have screened a series of neuropeptides against human embryonic kidney (HEK) 293 cells that stably express either MrgA1 or MrgC11 to identify ligands and/or agonists. MrgA1- or MrgC11-specific agonists stimulated dose-dependent increases in intracellular free Ca2+ in a pertussis toxin-insensitive manner, but failed to alter basal or forskolin-stimulated levels of intracellular cAMP. Furthermore, studies using embryonic fibroblasts derived from various G{alpha} protein knockout mice demonstrated that both the MrgA1 and MrgC11 receptors are coupled to the G{alpha}q/11 signaling pathway. Screening of neuropeptides identified surrogate agonists, most of these peptides included a common C-terminal -RF(Y)G or -RF(Y) amide motif. Structure-function studies suggest that endogenous ligands of Mrg receptors are likely to be RF(Y)G and/or RF(Y) amide-related peptides and that postprocessing of these peptides may serve to determine Mrg receptor-ligand specificity. The differences in ligand specificity also suggest functional diversity amongst the Mrg receptors

The Interaction of Phospholipase C-{beta}3 with Shank2 Regulates mGluR-mediated Calcium Signal

Phospholipase C-{beta} isozymes that are activated by G protein-coupled receptors (GPCR) and heterotrimeric G proteins carry a PSD-95/Dlg/ZO-1 (PDZ) domain binding motif at their C terminus. Through interactions with PDZ domains, this motif may endow the PLC-{beta} isozyme with specific roles in GPCR signaling events that occur in compartmentalized regions of the plasma membrane. In this study, we identified the interaction of PLC-{beta}3 with Shank2, a PDZ domain-containing multimodular scaffold in the postsynaptic density (PSD). The C terminus of PLC-{beta}3, but not other PLC-{beta} isotypes, specifically interacts with the PDZ domain of Shank2. Homer 1b, a Shank-interacting protein that is linked to group I metabotropic glutamate receptors and IP3 receptors, forms a multiple complex with Shank2 and PLC-{beta}3. Importantly, microinjection of a synthetic peptide specifically mimicking the C terminus of PLC-{beta}3 markedly reduces the mGluR-mediated intracellular calcium response. These results demonstrate that Shank2 brings PLC-{beta}3 closer to Homer 1b and constitutes an efficient mGluR-coupled signaling pathway in the PSD region of neuronal synapses

Role of G{alpha}12 and G{alpha}13 as Novel Switches for the Activity of Nrf2, a Key Antioxidative Transcription Factor

G{alpha}12 and G{alpha}13 function as molecular regulators responding to extracellular stimuli. NF-E2-related factor 2 (Nrf2) is involved in a protective adaptive response to oxidative stress. This study investigated the regulation of Nrf2 by G{alpha}12 and G{alpha}13. A deficiency of G{alpha}12, but not of G{alpha}13, enhanced Nrf2 activity and target gene transactivation in embryo fibroblasts. In mice, G{alpha}12 knockout activated Nrf2 and thereby facilitated heme catabolism to bilirubin and its glucuronosyl conjugations. An oligonucleotide microarray demonstrated the transactivation of Nrf2 target genes by G{alpha}12 gene knockout. G{alpha}12 deficiency reduced Jun N-terminal protein kinase (JNK)-dependent Nrf2 ubiquitination required for proteasomal degradation, and so did G{alpha}13 deficiency. The absence of G{alpha}12, but not of G{alpha}13, increased protein kinase C {delta} (PKC {delta}) activation and the PKC {delta}-mediated serine phosphorylation of Nrf2. G{alpha}13 gene knockout or knockdown abrogated the Nrf2 phosphorylation induced by G{alpha}12 deficiency, suggesting that relief from G{alpha}12 repression leads to the G{alpha}13-mediated activation of Nrf2. Constitutive activation of G{alpha}13 promoted Nrf2 activity and target gene induction via Rho-mediated PKC {delta} activation, corroborating positive regulation by G{alpha}13. In summary, G{alpha}12 and G{alpha}13 transmit a JNK-dependent signal for Nrf2 ubiquitination, whereas G{alpha}13 regulates Rho-PKC {delta}-mediated Nrf2 phosphorylation, which is negatively balanced by G{alpha}12

Optimal Voltage Control Using an Equivalent Model of a Low-Voltage Network Accommodating Inverter-Interfaced Distributed Generators

The penetration of inverter-based distributed generators (DGs), which can control their reactive power outputs, has increased for low-voltage (LV) systems. The power outputs of DGs affect the voltage and power flow of both LV and medium-voltage (MV) systems that are connected to the LV system. Therefore, the effects of DGs should be considered in the volt/var optimization (VVO) problem of LV and MV systems. However, it is inefficient to utilize a detailed LV system model in the VVO problem because the size of the VVO problem is increased owing to the detailed LV system models. Therefore, in order to formulate and solve the VVO problem in an efficient way, in this paper, a new equivalent model for an LV system including inverter-based DGs is proposed. The proposed model is developed based on an analytical approach rather than a heuristic-fitting one, and it therefore enables the VVO problem to be solved using a deterministic algorithm (e.g., interior point method). In addition, a method to utilize the proposed model for the VVO problem is presented. In the case study, the results verify that the computational burden to solve the VVO problem is significantly reduced without loss of accuracy by the proposed model.11Ysciescopu

Phase Current Measurement Method of Dual Inverter-Motor Drive System Using a Single DC Link Current Sensor

In recent years, electric propulsion systems have become widely, used and these systems have strict limits in volume and weight. Therefore, it is necessary to reduce the weight of the inverter-motor drive system. In a typical n inverter-motor drive system, at least 2n phase current sensors are required. In order to reduce the number of phase current sensors, this paper proposes a method for measuring phase current using n DC link current sensors in a 2n inverter-motor drive system. Two phase currents per inverter-motor system are measured during one period of the switching frequency using the pulse width modulation (PWM) shift method. However, since the measured phase current contains an error component in the average current, the error component was compensated for in order to obtain a current similar to the actual phase current by using the slope and dwell time of the phase current. The effectiveness of the proposed method is verified through experiments

1000 nm tunable acousto-optic filter based on photonic crystal fiber

Author name used in this publication: W. JinAuthor name used in this publication: J. Ju2007-2008 > Academic research: refereed > Publication in refereed journalVersion of RecordPublishe