• Proceedings of the Zoological Society Korea Conference
• /
• 1998.10b
• /
• pp.285.1-285
• /
• 1998

No Abstract, See Full Text

• Proceedings of the Korean Biophysical Society Conference
• /
• 2002.06b
• /
• pp.19-19
• /
• 2002

The gating kinetics of an inward-rectifier K$\^$＋/ channel, ROMK2 (Kir1.lb), were described by a model having one open state and two closed states. The long closed state was abolished by EDTA, suggesting that it was due to block by divalent cations. These closures exhibit a biphasic voltage-dependence, implying that the divalent blockers can permeate the channel.(omitted)

• The Korean Journal of Physiology and Pharmacology
• /
• v.9 no.4
• /
• pp.203-207
• /
• 2005

Electrical rhythmicity in the gastrointestinal (GI) muscles is generated by pacemaker cells, known as interstitial cells of Cajal (ICC). In the present study, we investigated the effect of external divalent cations on pacemaking activity in cultured ICC from murine small intestine by using whole-cell patch clamp techniques. ICC generated pacemaker currents under a voltage clamp or electrical pacemaker potentials under a current clamp, and showed a mean amplitude of $-500{\pm}50$ pA or $30{\pm}1$ mV and the frequency of $18{\pm}2$ cycles/min. Treatments of the cells with external 0 mM $Ca^{2+}$ stopped pacemaking activity of ICC. In the presence of 2 mM $Ca^{2+}$, 0 mM external $Mg^{2+}$ depolarized the resting membrane potential, and there was no change in the frequency of pacemaking activity. However, 10 mM external $Mg^{2+}$ decreased the frequency of pacemaking activity ($6.75{\pm}1$ cycles/min, n=5). We replaced external 2 mM $Ca^{2+}$ with equimolar $Ba^{2+}$, $Mn^{2+}$ and $Sr^{2+}$, and they all developed inward current in the sequence of $Ba^{2+}$>$Mn^{2+}$>$Sr^{2+}$. Also the frequency of the pacemaking activity was stopped or irregulated. We investigated the effect of 10 mM $Ba^{2+}$, $Mn^{2+}$ and $Sr^{2+}$ on pacemaking activity of ICC in the presence of external 0 mM $Mg^{2+}$, and found that 10 mM $Ba^{2+}$ and $Mn^{2+}$ induced large inward current and stopped the pacemaking activity of ICC (n=5). Interestingly, 10 mM $Sr^{2+}$ induced small inward current and potentiated the amplitude of pacemaking activity of ICC (n=5). These results indicate that extracellular $Ca^{2+}$ and $Mg^{2+}$ are requisite for the pacemaking activity of ICC.

• Journal of Animal Reproduction and Biotechnology
• /
• v.34 no.3
• /
• pp.197-204
• /
• 2019

This study was investigated to test whether the zygote recognized the topoisomerase II beta (TOP2B) mediated DNA fragmentation in epididymal spermatozoa or the nuclease degradation in vas deferens spermatozoa by testing for the presence of gammaH2AX (γH2AX). The γH2AX is phosphorylation of histone protein H2AX on serine 139 occurs at sites flanking DNA double-stranded breaks (DSBs). The presence of γH2AX in the pronuclei of mouse zygotes which were injected with DNA broke epididymal spermatozoa was tested by immunohistochemistry at 5 and 9 h post fertilization, respectively. Paternal pronuclei that arose from epididymal spermatozoa treated with divalent cations did not stain for γH2AX at 5 h. On the other hand, in embryos injected with vas deferences spermatozoa that had been treated with divalent cations, γH2AX was only present in paternal pronuclei, and not the maternal pronuclei at 5 h. Interestingly, both pronuclei stained positively for γH2AX for all treatments and controls at 9 h after sperm injection. In conclusion, the embryos recognize DNA that is damaged by nuclease, but not by TOP2B because H2AX in phosphorylated in paternal pronuclei resulting from spermatozoa treated with fragmented DNA from vas deferens spermatozoa treated with divalent cations, but not from epididymal spermatozoa treated the same way.

• Journal of Environmental Health Sciences
• /
• v.16 no.2
• /
• pp.113-119
• /
• 1990

Many studies on the analysis of cations in blood have been reported. However, no suitable method for the pretreatment of blood for the determination of cations by Ion Chromotography. As a result, pretreatment method that the membrane filtration of plasma a diluted 1 to 100 fold acidified pH 3.5 was found to be the most suitable. The recoveris of monovalent cations in blood were yield 101%(Na$^{+}$). 102%(NH$^{+}_{4}$) and 101%(K$^{+}$) Determinations of divalent cations(Mg and Ca ions) in blood by Ion chromatography were summarized as followed conditions Separator Column : CS$_{3}$. Suppressor Column : CMMS. Eluent conen : 25m M-HCl/2mM-Histidine. Regenerant conen: 40mM-Ba(OH)$_{2}$.

• The Korean Journal of Zoology
• /
• v.23 no.3
• /
• pp.137-148
• /
• 1980

The effects of divalent cations, $Hg^{2+}, Cu^{2+}, Pb^{2+}, Cd^{2+}$, and $Mn^{2+}$ on the total ATPase activity of the fragmented sarcoplasmic reticulum isolated from rabbit skeletal muscle were investigated. The inhibitory effects of the cations on the enzyme activity increased as the concentrations of the ions increased with the order of efficiency of $Hg^{2+}$ > $Cu^{2+}$ > $Pb^{2+}$ > $Cd^{2+}$ > $Mn^{2+}$ in the concentration range between 10 and 500$\mu$M. The 50% inhibition for each ion was almost identical with the inhibition constant (Ki) value for each ion. The Ki's were 10, 30 130, and 350$\mu$M for $Hg^{2+}, Cu^{2+}, Pb^{2+}, and Cd^{2+}$, respectively. $Mn^{2+}$ seemed to be an activator at lower concentrations and an inhibitor at higher concentrations. The presence of the cations did not change the Km values, suggesting that the ions act as a reversible noncompetitive inhibitor on the FSR ATPase. The energy of activation of the enzyme was aproximately 19 Kcal/mole. The presence of the ions decreased the value slightly. A possible mechanism for the reversible noncompetitive inhibitory effect of the cations was discussed.

• Environmental Mutagens and Carcinogens
• /
• v.25 no.2
• /
• pp.60-65
• /
• 2005

The human solute carrier, SLC41Al, is a $Mg^{2}+$ transporter that is regulated by extracellular magnesium. Although intracellular magnesium plays a fundamental role in cellular metabolism, little is known about how $Mg^{2}+$ is taken up and controlled by cells. Magnesium plays a fundamental role in cellular metabolism so that its control within the body is critical. Magnesium homeostasis is principally a balance between intestinal absorption of dietary magnesium and renal excretion of urinary magnesium. The kidney, mainly the distal convoluted tubule, controls magnesium reabsorption. Although renal reabsorption is under the influence of many hormones, selective regulation of magnesium transport is due to intrinsic control involving transcriptional processes and synthesis of transport proteins. Using microarray analysis, identification of the genetic elements involved with this transcriptional control has been begun. SLC41A1(GenBank Accession No. AJ514402), comprises 10 putative transmembrane domains, two of which are highly homologous to the integral membrane part of the prokaryote transports $Mg^{2}+$ and other divalent cations $Sr^2+,\;Zn^2+,\;Cu^2+,\;Fe^2+,\;Co^2+,\;Ba^2+,\;and\;Cd^2+,\;but\;not\;Ca^2+,\;Mn^2+,\;and\;Ni^2+.$ Transport of $Mg^{2}+$ by SLC41Al is rheogenic, voltage dependent, and not coupled to Na or Cl. Expressed SLC41Al transports a range of other divalent cations: $Mg^{2+},\;Sr^{2+},\;Zn^{2+},\;Cu^{2+},\;Fe^{2+},\;Co^{2+},\;Ba^{2+},\;and\;Cd^{2+}$. The divalent cations $Ca^{2+},\;Mn^{2+},\;and\;Ni^{2+}$and the trivalent ion $Gd^{3+}$ did not induce currents nor did they inhibit $Mg^{2+}$ transport. The nonselective cation $La^{3+}$ abolishes $Mg^{2+}$ uptake. Computer analysis of the SLC41Al protein structure reveals that it belongs to MgtE protein family & suggested that the human solute carrier, SLC41Al, might be a eukaryotic $Mg^{2+}$ transporter closely related $(60-70\%)$ protein encoded by SLC41A2 is a $Mg^{2}+$ transporter that might be involved in magnesium homeostasis in epithelial cells also transports a range of other divalent cations: $Ba^2,\;Ni^2,\;CO^2,\;Fe^2,\;or\;Mn^2,\;but\;not\;Ca^2,\;Zn^2,\;or\;Cu^{2+}$ that may have related functional properties.

• The Korean Journal of Physiology
• /
• v.26 no.2
• /
• pp.113-122
• /
• 1992

It is well known that chromaffin cells of adrenal medulla secrete catecholamine in response to sympathetic nerve activation and the influx of $Ca^{2+}$ through the voltage dependent $Ca^{2+}$ channels (VDCC) in the cell membrane do a major role in this secretory process. In this study, we explored the effect of divalent cations on VDCC of rat chromaffin cells. Rat (Sprague-Dawley rat, 150-250 gm) chromaffin cells were isolated and cultured. Standard giga seal, whole cell recording techniques were employed to study $Ca^{2+}$ current with external and internal solutions that could effectively isolate VDCC currents $(NMG\;in\;external\;and\;TEA\;and\;Cs^{2+}\;in\;internal\;solution)$. The voltage dependence and the inactivation time course of VDCC in our cells were identical to those of bovine chromaffin cells. A persistent inward current was first activated by depolarizing step pulse from the holding potential (H.P.) of -80 mV to -40 mV, increased to maximum amplitude at around +10 mV, and became smaller with progressively higher depolarizing pulses to reverse at around +60 mV. The inactivation time constant $(\tau)$, fitted from the long duration test potential (2 sec) was $1295.2{\pm}126.8$ msec $(n=20,\;1\;day\;of\;culture,\;mean\;{\pm}S.E.M.)$ and the kinetic parameters were not altered along the culture duration. Nicardipine $(10\;{\mu}M)$ blocked the current almost completely. Among treated divalent cations such as $Cd^{2+},\;Co^{2+},\;Ni^{2+},\;Zn^{2+}\;and\;,Mn^{2+},\;Cd^{2+}$ was the most potent blocker on VDCC. When the depolarizing step pulse from -80 mV to 10 mV was applied, the equilibrium dissociation constant $(K_d)$ of $Cd^{2+}\;was\;39\;{\mu}M,\;K_d\;of\;Co^{2+}\;was\;100\;{\mu}M\;and\;K_d\;of\;Ni^{2+}];was];780{\mu}M.$ The principal findings of this study are as follows. First, the majority of $Ca^{2+}$ channels in rat chromaffin cells are well classified to L-type $Ca^{2+}$ channel in the view of kinetics and pharmacology. Second, all divalent cations tested could block the $Ca^{2+}$ current and the most potent blocker among the tested was $Cd^{2+}$.

• Journal of the Korean Chemical Society
• /
• v.33 no.4
• /
• pp.357-365
• /
• 1989

The positional parameters of framework atoms, cations, and water molecules in hydrated and dehydrated $Mg_4Na_4-A$, $Ca_6-A$, $Zn_5Na_2-A$ and $Co_4Na_4-A$ were determined by the optimization technique using some potential energy functions and VAIOA optimization program. Upon dehydration, cations in hydrated states move toward the framework oxygens of 6 rings. Frameworks of fully dehydrated zeolite A are more stable than those of fully dehydrated divalent cation exchanged Zeolite A. There are three different kinds of water molecules in divalent cation exchanged Zeolite A; W(III) (water molecules having hydrogen bonds), W(II) (water molecules associated with $Na^+$ ions), and W(I) (water molecules associated with divalent cations). Three different DTA endothermic peaks were observed corresponding to the dehydration of three different kinds of water molecules in divalent cation exchanged Zeolite A.

• Food Science and Biotechnology
• /
• v.14 no.1
• /
• pp.108-111
• /
• 2005

To improve water-resistance and physical properties of sodium alginate film, effects of sodium alginate and plasticizer concentrations, divalent cation types and concentrations, and immersion time of films into divalent cation solutions on sodium alginate films were evaluated, based on elongation strength (ES), elongation rate (E), water vapor permeability (WVP), and water solubility (WS). Film made from 1.5% sodium alginate solution (w/w) had low WVP and WS, which are optimal characteristics for application of film preparation. Addition of plasticizer increased E and WS. Less than 2% $CaCl_2$ addition and 15min immersion time reduced WVP, WS, and E significantly (p<0.05). Sodium alginate films treated with $CuCl_2$, and $ZnCl_2$ solutions had lower WVP and WS, whereas $MgCl_2$ had no influence on improving water resistance of films.