• Title/Summary/Keyword: Cation channel

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Buffering Contribution of Mitochondria to the $[Ca^{2+}]_i$ Increase by $Ca^{2+}$ Influx through Background Nonselective Cation Channels in Rabbit Aortic Endothelial Cells

  • Kim, Young-Chul;Lee, Sang-Jin;Kim, Ki-Whan
    • The Korean Journal of Physiology and Pharmacology
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    • v.9 no.1
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    • pp.29-35
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    • 2005
  • To prove the buffering contribution of mitochondria to the increase of intracellular $Ca^{2+}$ level ($[Ca^{2+}]_i$) via background nonselective cation channel (background NSCC), we examined whether inhibition of mitochondria by protonophore carbonylcyanide m-chlorophenylhydrazone (CCCP) affects endothelial $Ca^{2+}$ entry and $Ca^{2+}$ buffering in freshly isolated rabbit aortic endothelial cells (RAECs). The ratio of fluorescence by fura-2 AM ($R_{340/380}$) was measured in RAECs. Biological state was checked by application of acetylcholine (ACh) and ACh ($10{\mu}M$) increased $R_{340/380}$ by $1.1{\pm}0.15$ ($mean{\pm}S.E.$, n=6). When the external $Na^+$ was totally replaced by $NMDG^+$, $R_{340/380}$ was increased by $1.19{\pm}0.17$ in a reversible manner (n=27). $NMDG^+$-induced $[Ca^{2+}]_i$ increase was followed by oscillatory decay after $[Ca^{2+}]_i$ reached the peak level. The increase of $[Ca^{2+}]_i$ by $NMDG^+$ was completely suppressed by replacement with $Cs^+$. When $1{\mu}M$ CCCP was applied to bath solution, the ratio of $[Ca^{2+}]_i$ was increased by $0.4{\pm}0.06$ (n=31). When $1{\mu}M$ CCCP was used for pretreatment before application of $NMDG^+$, oscillatory decay of $[Ca^{2+}]_i$ by $NMDG^+$ was significantly inhibited compared to the control (p<0.05). In addition, $NMDG^+-induced$ increase of $[Ca^{2+}]_i$ was highly enhanced by pretreatment with $2{\mu}M$ CCCP by $320{\pm}93.7$%, compared to the control ($mean{\pm}S.E.$, n=12). From these results, it is concluded that mitochondria might have buffering contribution to the $[Ca^{2+}]_i$ increase through regulation of the background NSCC in RAECs.

Characterization of the Stretch-Activated Channel in the Hamster Oocyte (햄스터난자에서 신전에 의해 활성화되는 통로의 성상)

  • Kim, Y.-M.;Hong, S.-G.
    • Journal of Embryo Transfer
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    • v.19 no.2
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    • pp.89-99
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    • 2004
  • Stretch-activated channels (SACs) responds to membrane stress with changes in open probability (Po). They play essential roles in regulation of cell volume and differentiation, vascular tone, and in hormonal secretion. SACs highly present in Xenopus oocytes and Ascidian oocytes are suggested to be involved in the regulation of pH and fluid transport to balance the osmotic pressure, but remain unclear in mammanlian oocytes. This study was investigated to find the presence of SACs in hamster oocytes and to examine their electrophysiological properties. To infer a role of SAC in relation to the development of early stage, we followed up to the stage of two-cell zygote with patch clamp techniques. Single channels were elicited by negative pressure (lower than ­15 cm$H_2O$). Interestingly, SACs were dependent on permeable cations such as $Na^+$ or $K^+$. As permeable cation removed from both sides across the membrane, SAC activity completely disappeared. When permeable cations present only in intracellular compartment, outward currents appeared at positive potentials. In contrast to this, inward currents occurred only at the negative voltage when permeable cation absent in cell interior. These result suggests that SAC carry cations through the nonselective cation channel (NSC channel). Taken together, we found that stretch activated channels present in hamster oocyte and the channel may carry cations through NSC channels. This stretch activated-NSC channels may play physiological role(s) in oocyte growth, maturation, fertilization and embryogenesis in fertilized oocytes to two-cell zygotes of hamster.

Selective Disproportionation of Toluene over Various Cation-exchanged ZSM-5 Catalysts (양이온 교환된 ZSM-5 촉매상에서 톨루엔의 선택적인 반응)

  • Jong Shin Yoo;Byoung Joon Ahn;Hakze Chon
    • Journal of the Korean Chemical Society
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    • v.27 no.2
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    • pp.127-132
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    • 1983
  • The catalytic activity of ZSM-5 catalyst for the disproportionation of toluene is dependent on the type of cation exchanged, the degree of ion-exchange and the reaction temperature. The activity increases in the order of alkaline-, alkali earth-, hydrogen, and rare-earth-exchanged ZSM-5 and decreases with increasing degree of cation exchange. Among the ion-exchanged ZSM-5 catalyst, only Cs-ZSM-5 shows predominant selectivity for p-xylene. The selectivity increases with increasing degree of $Cs^+$-exchange and decreasing reaction temperature. This phenomenon is interpreted in terms of shape selectivity arising from the partial blocking of channel intersections by large cesium ions.

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Dependence of Na+ leakage on intrinsic properties of cation exchange resin in simulated secondary environment for nuclear power plants

  • Hyun Kyoung Ahn;Chi Hyun An;Byung Gi Park;In Hyoung Rhee
    • Nuclear Engineering and Technology
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    • v.55 no.2
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    • pp.640-647
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    • 2023
  • Material corrosion in nuclear power plant (NPP) is not controlled only by amine injection but also by ion exchange (IX) which is the best option to remove trace Na+. This study was conducted to understand the Na+ leakage characteristics of IX beds packed with ethanolamine-form (ETAH-form) and hydrogen-form (H-form) resins in the simulated water-steam cycle in terms of intrinsic behaviors of four kinds of cation-exchange resins through ASTM test and Vanselow mass action modeling. Na+ was inappreciably escaped throughout the channel created in resin layer. Na+ leakage from IX bed was non-linearly raised because of its decreasing selectivity with increasing Na+ capture and with increasing the fraction of ETAH-form resin. Na+ did not reach the breakthrough earlier than ETAH+ and NH4+ due to the increased selectivity of Na+ to the cation-exchange resin (H+ < ETAH+ < NH4+ ≪ Na+) at the feed composition. Na+ leakage from the resin bed filled with small particles was decreased due to the enhanced dynamic IX processes, regardless of its low selectivity. Thus, the particle size is a predominant factor among intrinsic properties of IX resin to reduce Na+ leakage from the condensate polishing plant (CPP) in NPPs.

Mutation of a putative S-nitrosylation site of TRPV4 protein facilitates the channel activates

  • Lee, Eun-Jeoung;Shin, Sung-Hwa;Hyun, Sung-Hee;Chun, Jae-Sun;Kang, Sang-Sun
    • Animal cells and systems
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    • v.15 no.2
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    • pp.95-106
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    • 2011
  • The transient receptor potential vanilloid 4 (TRPV4) cation channel, a member of the TRP vanilloid subfamily, is expressed in a broad range of tissues. Nitric oxide (NO) as a gaseous signal mediator shows a variety of important biological effects. In many instances, NO has been shown to exhibit its activities via a protein S-nitrosylation mechanism in order to regulate its protein functions. With functional assays via site-directed mutagenesis, we demonstrate herein that NO induces the S-nitrosylation of TRPV4 $Ca^{2+}$ channel on the $Cys^{853}$ residue, and the S-nitrosylation of $Cys^{853}$ reduced its channel sensitivity to 4-${\alpha}$ phorbol 12,13-didecanoate and the interaction between TRPV4 and calmodulin. A patch clamp experiment and $Ca^{2+}$ image analysis show that the S-nitrosylation of $Cys^{853}$ modulates the TRPV4 channel as an inhibitor. Thus, our data suggest a novel regulatory mechanism of TRPV4 via NO-mediated S-nitrosylation on its $Cys^{853}$ residue.

Binding Symmetry of External Divalent Cations to Cyclic Nucleotide-gated IonChannel Reveled by Channel Tandem Dimers

  • Kwon, Ryuk-Jun;Park, Chul-Seung
    • Proceedings of the Korean Biophysical Society Conference
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    • 2001.06a
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    • pp.37-37
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    • 2001
  • Cyclic nucleotide-gated (CNG) channels are composed of homo or hetero tetramer of ${\alpha}$ and ${\beta}$ subunits. The a subunits of these channels have a conserved glutamate residue within the pore-forming region. This residue determines the selectivity as well as the affinity for the extracellular divalent cations. Using the high affinity mutant (E363D) of bovine retinal CNG channel in which the Glu was replaced to Asp at position 363, we constructed tandem dimers and investigated the binding symmetry of divalent cation to the site.(omitted)

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Characteristics of CCh-activated Nonselective Cation Channel in Gastric Smooth Muscle Cells.

  • Kang, Tong-Mook;Kim, Young-Chul;Rhee, Poong-Lyul;So, In-Suk;Rhee, Jong-Chul;Uhm, Dae-Yong;Kim, Ki-Whan
    • Proceedings of the Korean Biophysical Society Conference
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    • 1997.07a
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    • pp.26-26
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    • 1997
  • In the present study, we recorded CCh-activated nonselective cation (NSC) current in guinea-pig gastric smooth muscle cells and investigated the characteristics of the current. In whole-cell voltage-clamp mode, CCh activated NSC current. The same NSC current could be activated by internal dialysis of GTP${\gamma}$S.(omitted)

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Functional Characteristics of TRPC4 Channels Expressed in HEK 293 Cells

  • Sung, Tae Sik;Kim, Min Ji;Hong, Soojin;Jeon, Jae-Pyo;Kim, Byung Joo;Jeon, Ju-Hong;Kim, Seon Jeong;So, Insuk
    • Molecules and Cells
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    • v.27 no.2
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    • pp.167-173
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    • 2009
  • The classical type of transient receptor potential (TRPC) channel is a molecular candidate for $Ca^{2+}$-permeable cation channels in mammalian cells. Because TRPC4 and TRPC5 belong to the same subfamily of TRPC, they have been assumed to have the same physiological properties. However, we found that TRPC4 had its own functional characteristics different from those of TRPC5. TRPC4 channels had no constitutive activity and were activated by muscarinic stimulation only when a muscarinic receptor was co-expressed with TRPC4 in human embryonic kidney (HEK) cells. Endogenous muscarinic receptor appeared not to interact with TRPC4. TPRC4 activation by $GTP{\gamma}S$ was not desensitized. TPRC4 activation by $GTP{\gamma}S$ was not inhibited by either Rho kinase inhibitor or MLCK inhibitor. TRPC4 was sensitive to external pH with $pK_a$ of 7.3. Finally, TPRC4 activation by $GTP{\gamma}S$ was inhibited by the calmodulin inhibitor W-7. We conclude that TRPC4 and TRPC5 have different properties and their own physiological roles.

Channel Function of TRPML1 Prompts Lipolysis in Mature Adipocytes

  • Kim, Mi Seong;Kim, Min Seuk
    • International Journal of Oral Biology
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    • v.43 no.1
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    • pp.23-27
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    • 2018
  • Increased intracellular levels of $Ca^{2+}$ are generally thought to negatively regulate lipolysis in mature adipocytes, whereas store-operated $Ca^{2+}$ entry was recently reported to facilitate lipolysis and attenuate lipotoxicity by inducing lipophagy. Transient receptor potential mucolipin1 (TRPML1), a $Ca^{2+}$-permeable non-selective cation channel, is mainly expressed on the lysosomal membrane and plays key roles in lysosomal homeostasis and membrane trafficking. However, the roles of TRPML1 in lipolysis remains unclear. In this study, we examined whether the channel function of TRPML1 induces lipolysis in mature adipocytes. We found that treatment of mature adipocytes with ML-SA1, a specific agonist of TRPML1, solely upregulated extracellular glycerol release, but not to the same extent as isoproterenol. In addition, knockdown of TRPML1 in mature adipocytes significantly reduced autophagic flux, regardless of ML-SA1 treatment. Our findings demonstrate that the channel function of TRPML1 partially contributes to lipid metabolism and autophagic membrane trafficking, suggesting that TRPML1, particularly the channel function of TRPML1, is as therapeutic target molecule for treating obesity.

Bile Acid Inhibition of N-type Calcium Channel Currents from Sympathetic Ganglion Neurons

  • Lee, Hye-Kyung;Lee, Kyoung-Hwa;Cho, Eui-Sic
    • The Korean Journal of Physiology and Pharmacology
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    • v.16 no.1
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    • pp.25-30
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    • 2012
  • Under some pathological conditions as bile flow obstruction or liver diseases with the enterohepatic circulation being disrupted, regurgitation of bile acids into the systemic circulation occurs and the plasma level of bile acids increases. Bile acids in circulation may affect the nervous system. We examined this possibility by studying the effects of bile acids on gating of neuronal (N)-type $Ca^{2+}$ channel that is essential for neurotransmitter release at synapses of the peripheral and central nervous system. N-type $Ca^{2+}$ channel currents were recorded from bullfrog sympathetic neuron under a cell-attached mode using 100 mM $Ba^{2+}$ as a charge carrier. Cholic acid (CA, $10^{-6}M$) that is relatively hydrophilic thus less cytotoxic was included in the pipette solution. CA suppressed the open probability of N-type $Ca^{2+}$ channel, which appeared to be due to an increase in (no activity) sweeps. For example, the proportion of sweep in the presence of CA was ~40% at +40 mV as compared with ~8% in the control recorded without CA. Other single channel properties including slope conductance, single channel current amplitude, open and shut times were not significantly affected by CA being present. The results suggest that CA could modulate N-type $Ca^{2+}$ channel gating at a concentration as low as $10^{-6}M$. Bile acids have been shown to activate nonselective cation conductance and depolarize the cell membrane. Under pathological conditions with increased circulating bile acids, CA suppression of N-type $Ca^{2+}$ channel function may be beneficial against overexcitation of the synapses.