• Journal of Interdisciplinary Genomics
• /
• v.5 no.2
• /
• pp.35-41
• /
• 2023

Background: Ca²⁺ signaling plays a vital role in neuronal signaling and altered Ca²⁺ homeostasis in Parkinson's disease (PD). Overexpression of αSYN significantly promote the Ca²⁺-Calmodulin (CaM) activity and subsequent nuclear translocation of nuclear factor of activated T cells (NFAT) transcription factor in dopaminergic neurons of midbrain. However, the exact role of Ca²⁺-CaM and NFAT in PD pathology is yet to be elucidated. Methods: We designed the CaM-NFAT-oligodeoxynucleotide (ODN), a synthetic short DNA containing complementary sequence for NFAT transcription factor and CaM mRNA. Then, the effect of CaM-NFAT-ODN on 1-methyl-4-phenylpyridinium (MPP⁺)-mediated neurotoxicity was investigated in mimic PD model in vitro. Results: First, the expression of αSYN and CaM was strongly increased in substantia nigra (SN) of PD and the expression of tyrosine hydroxylase (TH) was strongly increased in control SN. Additionally, the expression of apoptosis marker proteins was strongly increased in SN of PD. Transfection of CaM-NFAT-ODN repressed CaM and pNFAT, the target genes of this ODN in rat embryo primary mesencephalic neurons. It also reduced ERK phosphorylation, a downstream target of these genes. These results demonstrated that CaM-NFAT-ODN operated successfully in rat embryo primary mesencephalic neurons. Transfection of CaM-NFAT-ODN repressed TH reduction, αSYN accumulation, and apoptosis by MPP⁺-induced neurotoxicity response through Ca²⁺ signaling and mitogen-activated protein kinases (MAPK) signaling. Conclusion: Synthetic CaM-NFAT-ODN has substantial therapeutic feasibility for the treatment of neurodegenerative diseases.

• Molecules and Cells
• /
• v.37 no.11
• /
• pp.804-811
• /
• 2014

The protease-activated receptor (PAR)-2 is highly expressed in endothelial cells and vascular smooth muscle cells. It plays a crucial role in regulating blood pressure via the modulation of peripheral vascular tone. Although several mechanisms have been suggested to explain PAR-2-induced hypotension, the precise mechanism remains to be elucidated. To investigate this possibility, we investigated the effects of PAR-2 activation on N-type $Ca^{2+}$ currents ($I_{Ca-N}$) in isolated neurons of the celiac ganglion (CG), which is involved in the sympathetic regulation of mesenteric artery vascular tone. PAR-2 agonists irreversibly diminished voltage-gated $Ca^{2+}$ currents ($I_{Ca}$), measured using the patch-clamp method, in rat CG neurons, whereas thrombin had little effect on $I_{Ca}$. This PAR-2-induced inhibition was almost completely prevented by ${\omega}$-CgTx, a potent N-type $Ca^{2+}$ channel blocker, suggesting the involvement of N-type $Ca^{2+}$ channels in PAR-2-induced inhibition. In addition, PAR-2 agonists inhibited $I_{Ca-N}$ in a voltage-independent manner in rat CG neurons. Moreover, PAR-2 agonists reduced action potential (AP) firing frequency as measured using the current-clamp method in rat CG neurons. This inhibition of AP firing induced by PAR-2 agonists was almost completely prevented by ${\omega}$-CgTx, indicating that PAR-2 activation may regulate the membrane excitability of peripheral sympathetic neurons through modulation of N-type $Ca^{2+}$ channels. In conclusion, the present findings demonstrate that the activation of PAR-2 suppresses peripheral sympathetic outflow by modulating N-type $Ca^{2+}$ channel activity, which appears to be involved in PAR-2-induced hypotension, in peripheral sympathetic nerve terminals.

• Proceedings of the Korean Institute of Electrical and Electronic Material Engineers Conference
• /
• 2006.06a
• /
• pp.32-35
• /
• 2006

For the white UV-LED applications, $Eu^{2+}$-activated calcium aluminium silicate phosphors were synthesized for the first time and the structures and luminescence characteristics of these phosphors were investigated. The phosphors in this study emitted blue. green or blue-green light depending on the starting materials for synthesis. In addition, the structure was also changed when the different starting materials were used. When CaO and $CaCO_3$ was used as a starting material. tetragonal $Ca_2Al_2SiO_7$ was formed and blue-green and pure green light was emitted. respectively. However. in the case of $CaSiO_3$, triclinic $CaAl_2Si2O_8$ was formed and only pure blue emission was detected. The maximum emission intensity was obtained from $CaAl_2Si_2O_8:Eu^{2+}$ phosphors, which intensity was about 1.4 times higher than that of YAG:$Ce^{3+}$ phosphor used for blue LED.

• The Korean Journal of Physiology
• /
• v.27 no.1
• /
• pp.107-114
• /
• 1993

Most of voltage operated $Ca^{2+}$ channels can be divided into three types (T-, N-, and L-type), according to the electrical and pharmacological properties. Their distribution is closely related to cell specific functions. Properties of the voltage activated $Ca^{2+}$ current in mouse eggs were examined to classify channel types and to deduce the function by using whole cell voltage clamp technique. $Ca^{2+}$ currents appeared below -40 mV and reached a maximum at -15 mV (half maximum was -31 mV), then decayed rapidly (inactivation time constant ${\tau}=28.2{\pm}9.59$ ms at -10 mV within 50 ms after the onset of step depolarization. Activation and inactivation of the $Ca^{2+}$ channel was steeply dependent on voltage, in a relatively low range of $-70\;mV{\sim}-10 mV,$ half maximum of activation was -31 mV and that of inactivation was -39 mV, respectively. This current was not decreased significantly by nifedipine, a specific dihydropyridine $Ca^{2+}$ channel blocker in the range of $1\;{\mu}M\;to\;100{\mu}M.$ The inhibitory effect of $Ni^{2+}\;on\;Ca^{2+}$ current was greater than that of $Cd^{2+}.$ The conductance of $Ba^{2+}$ through the channel was equal to or lower than that of $Ca^{2+}$ These results implied that $Ca^{2+}$ current activated at a lower voltage in the mouse egg is carried via a $Ca^{2+}$ channel with similar properties that of the T-type channel.

• YAKHAK HOEJI
• /
• v.56 no.2
• /
• pp.108-115
• /
• 2012

The hyperpolarization-activated current ($I_h$) is an inward cation current activated by hyperpolarization of the membrane potential and plays a role as an important modulator of action potential firing frequency in many excitable cells. In the present study we investigated the effects of extracellular divalent cations on $I_h$ in dorsal root ganglion (DRG) neurons using whole-cell voltage clamp technique. $I_h$ was slightly increased in $Ca^{2+}$-free bath solution. BAPTA-AM did not change the amplitudes of $I_h$. Amplitudes of $I_h$ were decreased by $Ca^{2+}$, $Mg^{2+}$ and $Ba^{2+}$ dose-dependently and voltage-independently. Inhibition magnitudes of $I_h$ by external divalent cations were partly reversed by the concomitant increase of extracellular $K^+$ concentration. Reversal potential of $I_h$ was significantly shifted by $Ba^{2+}$ and $V_{1/2}$ was significantly affected by the changes of extracellular $Ca^{2+}$ concentrations. These results suggest that $I_h$ is inhibited by extracellular divalent cations ($Ca^{2+}$, $Mg^{2+}$ and $Ba^{2+}$) by interfering ion influxes in cultured rat DRG neurons.

• The Korean Journal of Physiology and Pharmacology
• /
• v.12 no.2
• /
• pp.51-58
• /
• 2008

Cardiac fibroblasts constitute one of the largest cell populations in the heart, and contribute to structural, biochemical, mechanical and electrical properties of the myocardium. Nonetheless, their cardiac functions, especially electrophysiological properties, have often been disregarded in studies. $Ca^{2+}$-activated $K^+\;(K_{Ca})$ channels can control $Ca^{2+}$ influx as well as a number of $Ca^{2+}$-dependent physiological processes. We, therefore, attempted to identify and characterize $K_{Ca}$ channels in rat Cardiac fibroblasts. First, we showed that the cells cultured from the rat ventricle were cardiac fibroblasts by immunostaining for discoidin domain receptor 2 (DDR-2), a specific fibroblast marker. Secondly, we detected the expression of various $K_{Ca}$ channels by reverse transcription polymerase chain reaction (RT-PCR), and found all three family members of $K_{Ca}$ channels, including large conductance $K_{Ca}$ (BK-${\alpha}1-\;and\;-{\beta}1{\sim}4$subunits), intermediate conductance $K_{Ca}$ (IK), and small conductance $K_{Ca}$ (SK$1{\sim}4$ subunits) channels. Thirdly, we recorded BK, IK, and SK channels by whole cell mode patch clamp technique using their specific blockers. Finally, we performed cell proliferation assay to evaluate the effects of the channels on cell proliferation, and found that the inhibition of IK channel increased the cell proliferation. These results showed the existence of BK, IK, and SK channels in rat ventricular fibroblasts and involvement of IK channel in cell proliferation.

• YAKHAK HOEJI
• /
• v.41 no.6
• /
• pp.773-781
• /
• 1997

The activity of $Ca^{2+}$calmodulin (CaM)-dependent protein kinase Ia (CaM kinase Ia) is shown to be regulated through direct phosphorylation by CaM kinase I kinase (CaMK IK). In the present study, three distinct CaMKIK peaks were separated from Q-Sepharose colunm chromatography of pig brain homogenate using a Waters 650 Protein Purification System. The purified CaMKIK from the major peak potently and rapidly enhanced CaM kinase Ia activity, reaching a maximal stimulation within 2min at the concentrations of 12-15nM. The activated state of CaM kinase Ia is characterized by a markedly enhanced $V_{max}4 as well as significantly decreased $K_m\;and\;K_a$ values toward peptide substrate and CaM, respectively. These observations suggest the activation process of CaM kinase Ia. The phosphorylation of CaM kinase Ia by CaMKIK may induce its conformational change responsible for the alterations in the kinetic properties, which ultimately leads to the rapid enzyme activation.

• 한국정보디스플레이학회:학술대회논문집
• /
• 2003.07a
• /
• pp.836-839
• /
• 2003

We have synthesized some phosphors in the system $CaO-Y_{2}O_3-Al_{2}O_{3}$ by combinatorial polymerized-complex method. Composition and synthetic temperature of phosphors in the liblary was screened from the emission intensities of individual samples under VUV excitation. In $Tb^{3+}$-activated $CaO-Y_{2}O_3-Al_{2}O_{3}$, green phosphors showing good intensity were found to be $CaYAl_{3}O_{7}$, $CaYalO_{4}$, $YAlO_{3}$, $Y_{3}Al_{5}O_{12}$, $Y_{4}Al_{2}O_{9}$, $Ca_{3}Al_{2}O6$.

• Proceedings of the Korean Vacuum Society Conference
• /
• 2015.08a
• /
• pp.170.2-170.2
• /
• 2015

Enormous interest in trivalent rare-earth (RE) ions activated luminescent materials has been gaining owing to their promising applications in bio-imaging, solar cells, white light-emitting diodes and field-emission displays. Among these trivalent RE ions, dysprosium (Dy3+) was widely investigated due to its unique photoluminescence (PL) emissions. A series of Dy3+-activated CaWO4 phosphors were prepared by a facile high-temperature solid-state reaction method. The X-ray diffraction, PL spectra, cathodoluminescence (CL) spectra as well as PL decay curves were used to characterize the prepared samples. Under ultraviolet light excitation, the characteristic emissions of Dy3+ ions were observed in all the obtained phosphors. Furthermore, the PL emission intensity increased gradually with the increment of Dy3+ ion concentration, reaching its maximum value at an optimized Dy3+ ion concentration. Additionally, color-tunable emissions were obtained in Dy3+-activated CaWO4 system by adjusting the Dy3+ ion concentration and excitation wavelength. Ultimately, strong CL properties were observed in Dy3+-activted CaWO4 phosphors. These results suggested that the Dy3+-activted CaWO4 phosphors may have potential applications in the field of miniature color displays.

• The Korean Journal of Physiology and Pharmacology
• /
• v.12 no.4
• /
• pp.177-183
• /
• 2008

The layers of keratinocytes form an acid mantle on the surface of the skin. Herein, we investigated the effects of acidic pH on the membrane current and $[Ca^{2+}]_c$ of human primary keratinocytes from foreskins and human keratinocyte cell line (HaCaT). Acidic extracellular pH ($pH_e{\leq}5.5$) activated outwardly rectifying $Cl^-$ current ($I_{Cl,pH}$) with slow kinetics of voltage-dependent activation. $I_{Cl,pH}$ was potently inhibited by an anion channel blocker 4,4'-diisothiocyanostilbene-2,2'-disulphonic acid (DIDS, 73.5% inhibition at 1${\mu}$M). $I_{Cl,pH}$ became more sensitive to $pH_e$ by raising temperature from $24^{circ}C$ to $37^{circ}C$. HaCaT cells also expressed $Ca^{2+}$-activated $Cl^-$ current ($I_{Cl,Ca}$), and the amplitude of $I_{Cl,Ca}$ was increased by relatively weak acidic $pH_e$ (7.0 and 6.8). Interestingly, the acidic $pH_e$ (5.0) also induced a sharp increase in the intracellular [$Ca^{2+}$] (${\triangle}[Ca^{2+}]_{acid}$) of HaCaT cells. The ${\triangle}[Ca^{2+}]_{acid}$ was independent of extracellular $Ca^{2+}$, and was abolished by the pretreatment with PLC inhibitor, U73122. In primary human keratinocytes, 5 out of 28 tested cells showed ${\triangle}[Ca^{2+}]_{acid}$. In summary, we found $I_{Cl,pH}$ and ${\triangle}[Ca^{2+}]_{acid}$ in human keratinocytes, and these ionic signals might have implication in pathophysiological responses and differentiation of epidermal keratinocytes.