• Title/Summary/Keyword: 칼슘의존성

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Divalent Cation-dependent Inactivation of N-type Calcium Channel in Rat Sympathetic Neurons (쥐 교감신경 뉴론 N형 칼슘통로의 2가 양이온의존성 비활성화)

  • Goo Yong-Sook
    • Progress in Medical Physics
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    • v.17 no.2
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    • pp.96-104
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    • 2006
  • Experiments from several groups Including ours have demonstrated that $Ca^{2+}$ can enhance the inactivation of N-type calcium channels. However, it is not clear if this effect can be ascribed to a 'classic' $Ca^{2+}$-dependent inactivation (CDI) mechanism. One method that has been used to demonstrate CDI of L-type calcium channels is to alter the intracellular and extracellular concentration of $Ca^{2+}$. In this paper we replaced the external divalent cation to monovalent ion ($MA^+$) to test CDI. In the previous paper, we could separate fast (${\tau}{\sim}150ms$) and slow (${\tau}{\sim}2,500ms$) components of inactivation in both $Ba^{2+}$ and $Ca^{2+}$ using 5-sec voltage step. Lowering the external divalent cation concentration to zero abolished fast inactivation with relatively little effect on slow inactivation. Slow inactivation ${\tau}$ correspond very well with provided the $MA^+$ data is shifted 10 mV hyperpolarized and slow inactivation ${\tau}$ decreases with depolarization voltage in both $MA^+\;and\;Ba^{2+}$, which consistent with a classical voltage dependent inactivation (VDI) mechanism. These results combined with those of our previous paper lead us to hypothesize that external divalent cations are required to produce fast N-channel inactivation and this divalent cation-dependent inactivation is a different mechanism from classic CDI or VDI.

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Phosphorylation as a Signal Transduction Pathway Related with N-channel Inactivation in Rat Sympathetic Neurons (N형 칼슘통로 비활성화와 연계된 세포 신호전달 체계로서의 인산화과정)

  • Lim Wonil;Goo Yong Sook
    • Progress in Medical Physics
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    • v.15 no.4
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    • pp.220-227
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    • 2004
  • In N-type $Ca^{2+}$ channels, the mechanism of inactivation - decline of inward current during a depolarizing voltage step- is still controversial between voltage-dependent inactivation and $Ca^{2+}$ -dependent inactivation. In the previous paper we demonstrated that fast component of inactivation of N-type calcium channels does not involve classic $Ca^{2+}$ -dependent mechanism and the slowly inactivating component could result from a $Ca^{2+}$ -dependent process. However, there should be signal transduction pathway which enhances inactivation no matter what the inactivation mechanism is. We have investigated the effect of phosphorylation on calcium channels of rat sympathetic neurons. Intracellular dialysis with the phosphatase inhibitors okadaic acid markedly enhanced the inactivation. The rapidly inactivating component is N-type calcium current, which is blocked by $\omega$-conotoxin GVIA. Staurosporine, a nonselective protein kinase inhibitor, prevented the action of okadaic acid, suggesting that protein phosphorylation is involved. More specifically lavendustin C, inhibitor of CaM kinase II, prevented the action of okadaic acid, suggesting that calmodulin dependent pathway is involved in inactivation process. It is not certain to this point whether phosphorylation process is inactivation itself. Molecular biological research regarding binding site should be followed to address the question of how the divalent cation binding site is related to phoshorylation process.

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Role of $Ca^{2+}$ for Inactivation of N-type Calcium Current in Rat Sympathetic Neurons (흰쥐 교감신경 뉴론 N형 칼슘전류의 비활성화에 미치는 칼슘효과)

  • Goo, Yong-Sook;Keith S. Elmslie
    • Progress in Medical Physics
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    • v.14 no.1
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    • pp.54-67
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    • 2003
  • The voltage-dependence of N-type calcium current inactivation is U-shaped with the degree of inactivation roughly mirroring inward current. This voltage-dependence has been reported to result from a purely voltage-dependent mechanism. However, $Ca^{2+}$-dependent inactivation of N-channels has also been reported. We have investigated the role of $Ca^{2+}$ in N-channel inactivation by comparing the effects of $Ba^{2+}$and $Ca^{2+}$ on whole-cell N-current in rat superior cervical ganglion neurons. For individual cells in-activation was always larger in $Ca^{2+}$ than in $Ba^{2+}$ even when internal EGTA (11 mM) was replaced with BAPTA (20 mM). The inactivation vs. voltage relationship was U-shaped in both divalent cations. The enhancement of inactivation by $Ca^{2+}$ was inversely related with the magnitude of inactivation in $Ba^{2+}$ as if the mechanisms of inactivation were the same in both $Ba^{2+}$ and $Ca^{2+}$. In support of this idea we could separate fast ( ${\gamma}$ ~150 ms) and slow ( ${\gamma}$ ~ 2500 ms) components of inactivation in both $Ba^{2+}$and $Ca^{2+}$ using 5 sec voltage steps. Differential effects were observed on each component with $Ca^{2+}$ enhancing the magnitude of the fast component and the speed of the slow component. The larger amplitude of fast component indicates that the more channels inactivate via this pathway with $Ca^{2+}$ than with $Ba^{2+}$, but the stable time constants support the idea the fast inactivation mechanism is identical in $Ba^{2+}$and $Ca^{2+}$. The results do not support a $Ca^{2+}$-dependent mechanism for fast inactivation. However, the $Ca^{2+}$-induced acceleration of the slowly inactivating component could result from a $Ca^{2+}$-dependent process.

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Virulence characters of Yersinia enterocolitica isolated in Korea (한국에서 분리한 Yersinia enterocolitica의 병원성에 관한 연구)

  • 이영희;정태화;이종삼
    • Korean Journal of Microbiology
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    • v.26 no.3
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    • pp.262-269
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    • 1988
  • In order to investigate the virulence of Y. enterocolitica isolated in Korea, all necessary experiments were done including several virulence determinating tests-autoagglutination test, calcium-dependency test, HeLa cell invasion test, Sereny test, crystal violet binding test, and electrophoresis for plasmid pattern. The obtained results are as follows: The virulent strains of Y. enterocolitica revealed positive reactions on autoagglutination test, cacium-dependency test, and drystal violet binding test, while the avirulent strains did not. A positive reaction was observed only at $37^{\circ}C$ implying that the expression of virulence is temperature-dependent. In Sereny test, the standard reference virulent strain (serotype 0:8) showed positive reactions while the virylent experimental strains (serotype 1:3, 0:9) revealed negative results, which indicates that the virulence of Y. enterocolitica in experimental animals varied according to their serotypes. Most of the virulent strains contained 36-38Mdal plasmids, but the avirulent strains did not. In addition, it was noted that autoagglutination, calcium-dependency, and crystal violet binding were related to the presence of plasmids.

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한국인의 영양실태

  • 성낙응
    • Food Industry
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    • s.4
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    • pp.10-13
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    • 1971
  • 한국인의 일반적인 영양실태는 어떻한가? 영양소섭취상태, 단백질섭취상태, 지방섭취상태, 칼슘섭취상태등 우리의 영양소섭취상태는 식물성식품에 의존하고 있으며 곡류에서 전체 80$\%$이상의 영양소를 섭취하고 있어 국민체위는 크게 발전을 못하고 있다

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Calcium Channel Subtype in Rat Adrenal Chromaffin Cells (흰쥐 부신수질 크로마핀세포의 칼슘통로 유형)

  • Goo, Yong-Sook
    • Progress in Medical Physics
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    • v.12 no.1
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    • pp.59-70
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    • 2001
  • Adrenal chromaffin cells secrete catecholamine in response to acetylcholine. The secretory response has absolute requirement for extracellular calcium, indicating that $Ca^{2+}$ influx through voltage operated $Ca^{2+}$ channels is the primary trigger of the secretion cascade. Although the existence of various types of $Ca^{2+}$ channels has been explored using patch clamp technique in adrenal chromaffin cells, there is still disagreement with the types of $Ca^{2+}$ channels existed in different species. Therefore, we have tried to identify several distinct types of $Ca^{2+}$ channels in rat chromaffin cells. By using nicardipine(L type channel blocker), $\omega$-CgTx GVIA(N type channel blocker), and $\omega$-AgaTx VIA(P type channel blocker), it was identified that L, N, and P type $Ca^{2+}$ channel exist in rat adrenal chromaffin cells and the order of contribution of each channel type to whole cell $Ca^{2+}$ current was L type> N type> P type. type> P type.

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Cell Cycle-Dependent Activity Change of Calcium/Calmodulin-Dependent Protein Kinase II (칼슘/calmodulin-의존적 단백질 인산화 효소 II의 동물세포 주기에 따른 활성도 변화에 관한 연구)

  • Koung, Hoon-Suh
    • The Journal of Natural Sciences
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    • v.9 no.1
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    • pp.1-7
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    • 1997
  • Calcium/calmodulin-dependent protein kinase II (CaMK-II) is responsible for the phosphorylation of proteins involved in various cellular functions. Since the level of intracellular calcium ($Ca_2+$) oscillate during the cell cycle, it is expected that the activity of CaMK-II is also dependent on the cell cycle. The kinase activity in NIH3T3 cells which were arrested at or released from certain phase of the cell cycle was measured and compared to that in the normally growing asynchronous control cells to investigate whether the activity of this kinase is cell cycle-dependent. Cells were arrested at G0, G1, G1/S, G2/M and M phase, respectively by use of various drugs which do not have any effect on the kinase activity of CaMK-II at G0, G1, G1/s and G2/M phase was similar to that of the control cells, whereas lower at M. Calcium-independent activity of CaMK_II by autophosphorylation was higher at M and, thus, higher autonomy at M, which represented the physiologically relevant activity of CaMK-II. A similar pattern of activity change of the kinase was demonstrated during the cell cycle of synchronized cells which were released from G1 arrest. These results indicate that the activity of CaMK-11 is cell cycle-dependent and is activity during the mitosis.

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Enzymatic Properties of Barley $\alpha$-Amylase Chimeric Enzymes Produced by Staggered Extension Process (Staggered Extension Process를 통해 제조한 보리 알파아밀라제 Chimera 효소의 특성)

  • Kim, Tae-Jip;Choi, Seung-Ho;Jang, Myoung-Uoon;Park, Jung-Mi;Svensson, Birte
    • Microbiology and Biotechnology Letters
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    • v.38 no.2
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    • pp.151-157
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    • 2010
  • Barley malt produces two different $\alpha$-amylase isozymes (AMY1 and AMY2), which share up to 80% of amino acid sequence identity with each other. However, their enzymatic properties differ remarkably. In this study, five chimeric enzymes between AMY1 and 2 were constructed by staggered extension process (StEP) technique, and their enzymatic properties were characterized. According to the results, chimeric AMY-D2, D8, and E12 showed the mixed or intermediate types of calcium-dependent activity between AMY1 and 2. Meanwhile, only AMY-E10 chimera could be significantly inhibited by barley $\alpha$-amylase/subtilisin inhibitor (BASI) protein. Chimera AMY-C6 showed the same calcium-dependency as AMY1, while AMY-E10 was closely similar to AMY2. As a result, it can be proposed that some amino acid residues in the region II, III, and IV of barley $\alpha$-amylases can play very important roles in the interaction with BASI, and those in III, V, VI, and VII may partly affect on the calcium-dependent activity.

Effect of γ-PGA (Poly-γ-Glutamic Acid) Supplement on Calcium Absorption and Bone Metabolism in Rats (γ-PGA(Poly-γ-glutamic acid) 보충이 흰쥐의 칼슘 흡수율 및 골대사에 미치는 영향)

  • Lee, Min-Sook;Kang, Jung-Il;Kim, Hyun-Su
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.35 no.3
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    • pp.255-261
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    • 2006
  • This study was Conducted to investigate the effect of ${\gamma}-PGA\;({\gamma}-poly\;glutamic\;acid)$ on Ca absorption and bone metabolism in rats. Weaned 4-week old male rats were fed Ca-deficient diets for 3 weeks after the adjustment period. Rats were divided into 6 groups and were fed experimental diets for four weeks. Experimental groups were basal (Ca deficient), control (Ca diet: Ca 0.45%), CP1(Ca 0.45%+casein phosphopeptide 1%), PG1(Ca 0.45%+gamma poly glutamic acid 1%), CPG (Ca 0.45%+casein phosphopeptide 1%+gamma poly glutamic acid 1%) and PG3(Ca 0.45%+gamma poly glutamic acid 3%). Though daily Ca intake and food intake of experimental groups showed no significant difference that of control group. The values of fecal Ca excretion and urinary Ca excretion in groups fed ${\gamma}-PGA$ were significantly lower than that in tile control group. The values of Ca absorption in groups fed ${\gamma}-PGA$ were significantly higher than that in the control group. The levels of femur Ca in ${\gamma}-PGA$ supplemented group were significantly increased compared to the control group. Also, breaking force of femur in ${\gamma}-PGA$ supplemented group showed about 40% increase compared to the control group. These results show that ${\gamma}-PGA$ supplement could be helpful to increase Ca absorption as well as to intensify the femur strength and to increase the Ca content of femur in rats.