• Journal of Life Science
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• v.16 no.1
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• pp.37-43
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• 2006

Gap junction is an ion channel forming between adjacent cells. It also acts as a membrane channel like sodium or potassium channels in a single cell. The amino acid residues up to the $10^{th}$ position in the amino (N)-terminus of gap junction hemichannel affect gating polarity as well as current-voltage (I-V) relation. While wild-type Cx32 channel shows negative gating polarity and inwardly rectifying I-V relation, T8D channel in which threonine residue at $8^{th}$ position is replaced with negatively charged aspartate residue shows reverse gating polarity and linear I-V relation. It is still unclear whether these changes are resulted from the charge effect or the conformational change of the N-terminus. To clarify this issue, we made a mutant channel harboring cysteine residue at the $8^{th}$ position (T8C) and characterized its biophysical properties using substituted-cysteine accessibility method (SCAM). T8C channel shows negative gating polarity and inwardly rectifying I-V relation as wild-type channel does. This result indicates that the substitution of cysteine residue dose not perturb the original conformation of wild-type channel. To elucidate the charge effect two types of methaenthiosulfonate (MTS) reagents (negatively charged $MTSES^-$ and positively charged $MTSET^+$) were used. When $MTSES^-$ was applied, T8C channel behaved as T8D channel, showing positive gating polarity and linear I-V relation. This result indicates that the addition of a negative charge changes the biophysical properties of T8C channel. However, positively charged $MTSET^+$ maintained the main features of T8C channel as expected. It is likely that the addition of a charge by small MTS reagents does not distort the conformation of the N-terminus. Therefore, the opposite effects of $MTSES^-$ and $MTSETT^+$ on T8C channel suggest that the addition of a charge itself rather than the conformational change of the N-terminus changes gating polarity and I-V relation. Furthermore, the accessibility of MTS reagents to amino acid residues at the $8^{th}$ position supports the idea that the N-terminus of gap junction channel forms or lies in the aqueous pore.

• Journal of Life Science
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• v.14 no.5
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• pp.882-890
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• 2004

Gap junction is a membrane structure facilitating the direct transmission of several ions and small molecules between two cells. It is also called an 'intercellular channel' to distinguish it from other well-known cellular channels (e.g. sodium and potassium channels). Gap junction channels are not passive conduits, rather the ion channels modulated by several stimuli including pH, calcium ion, voltage, and a chemical modification (mainly known as phosphorylation). Among them, the effects of voltage on the gating of gap junction channels have been well studied. Gap junction channels are more sensitive to the transjunctional potential ($V_j$) between two cells rather than the membrane potential($V_m$) between inside and outside the cell. In this review, I will summarize the general properties of gap junction channel and discuss the gating mechanism for the gap channels.

• Journal of Life Science
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• v.18 no.6
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• pp.764-769
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• 2008

Mutations in the human connexin 32 (Cx32) gene are responsible for X-linked Charcot-Marie-Tooth (CMTX) disease. Although over 300 different mutations have been identified the detailed molecular etiology of CMTX disease is poorly understood. Several studies reported that connexin membrane channels share most biophysical properties with their parental gap junction channels. In this study, two connexin mutant membrane channels (one mutant channel called the M34T channel in which the methionine residue at the $34^{th}$ position of the Cx32 protein is replaced with threonine residue and the other mutant channel called the T86C channel in which the threonine residue at the $86^{th}$ position is replaced with cysteine residue) associated with CMTX mutations were characterized at the single-channel level instead of using mutant gap junction channels. The biophysical properties of the M34T channel were very similar to those of the gap junction channel formed by M34T mutation. In addition, the mutant membrane channel study revealed the reversal of the gating polarity, the loss of fast gating and the gain of slow gating. The T86C channel also behaves like its parental wild type Cx32 membrane channel. Taken together, these results suggest that a study using connexin membrane channels is useful to characterize CMTX mutants.

• Journal of Power Electronics
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• v.16 no.5
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• pp.1706-1715
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• 2016

In this paper, a single phase modified switched-diode topology for both symmetrical and asymmetrical cascaded multilevel inverters is presented. It consists of a Modified Switched-Diode Unit (MSDU) and a Twin Source Two Switch Unit (TSTSU) to produce distinct positive voltage levels according to the operating modes. An additional H-bridge synthesizes a voltage waveform, where the voltage levels of either polarity have less Total Harmonic Distortion (THD). Higher-level inverters can be built by cascading MSDUs. A comparative analysis is done with other topologies. The proposed topology results in reductions in the number of power switches, losses, installation area, voltage stress and converter cost. The Nearest Level Control (NLC) technique is employed to generate the gating signals for the power switches. To verify the performance of the proposed structure, simulation results are carried out by a PSIM under both steady state and dynamic conditions. Experimental results are presented to validate the simulation results.