• Title/Summary/Keyword: CA1

검색결과 12,075건 처리시간 0.038초

Cell Cycle-Dependent Activity Change Of $Ca^{2+}/$Calmodulin-Dependent Protein Kinase II In NIH 3T3 Cells

  • Kim, Dae-Sup;Suh, Kyong-Hoon
    • BMB Reports
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    • 제34권3호
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    • pp.212-218
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    • 2001
  • Although the blockage of a cell cycle by specific inhibitors of $Ca^{2+}/$calmodulin-dependent protein kinase II (CaMK-II) is well known, the activity profile of CaMK-II during the cell cycle in the absence of any direct effectors of the enzyme is unclear. The activity of native CaMK-II in NIH 3T3 cells was examined by the use of cell cycle-specific arresting and synchronizing methods. The total catalytic activity of CaMK-II in arrested cells was decreased about 30% in the M phase, whereas the $Ca^{2+}$-independent autonomous activity increased about 1.5-fold in the M phase and decreased about 50% at the G1/S transition. The in vivo phosphorylation level of CaMK-II was lowest at G1/S and highest in M. The CaMK-II protein level was unchanged during the cell cycle. When the cells were synchronized, the autonomous activity was increased only in M. These results indicate that the physiologically relevant portion of CaMK-II is activated only in M, and that the net activation of CaMK-II is required in mitosis.

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Calcium Chloride 첨가에 의한 깍두기의 가식기간 연장 효과 (Extention of Shelf-life of Kakdugi by Calcium Chloride Addition)

  • 박민경
    • 한국산학기술학회논문지
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    • 제3권1호
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    • pp.32-37
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    • 2002
  • Ca/sup 2+/ 이온은 식물조직의 경도 유지에 중요한 역할을 하는 것으로 알려져 있다. 따라서, Ca/sup 2+/의 첨가가 깍두기의 가식기간 연장에 미치는 영향, 적정 농도 및 효율적 첨가방법을 알아보고자 하였다. CaCl₂의 첨가에 의해 깍두기의 숙성기간 중 pH의 감소, 산도의 증가 및 기계적 경도의 감소 속도가 억제되어 가식기간이 연장되었다. 또한, Ca/sup 2+/ 첨가에 의해 관능적 특성 중 아삭함, 신맛 및 총체적인 기호도가 개선되었다. CaCl₂의 첨가방법과 농도는, 무를 절이는 염수에 0.1%의 CaCl₂를 첨가하고 절임과정이 끝나면 수세한 후 다시 양념과 함께 0.05%의 CaCl₂를 첨가하여 깍두기를 제조하는 것이 가장 효과적인 것으로 나타났다.

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Forskolin의 흰쥐적출관류부신으로 부터 Ach, Excess $K^+$, DMPP, McN-A-343에 의한 Catecholamine 분비효과의 증강작용 (Forskolin-Induced Potentiation of Catecholamine Secretion Evoked By Ach, DMPP, McN-A-343 and Excess $K^+$ From the Rat Adrenal Gland)

  • 임동윤;김원식;최철희
    • 대한약리학회지
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    • 제27권2호
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    • pp.167-181
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    • 1991
  • Adenylate cyclase 효소를 활성화시키는 약물인 Forskolin의 흰쥐 적출관류 부신으로부터 Ach, excess $K^+$, McN-A-343 및 caffein에 의한 catecholamines (CA) 분비작용에 대한 영향을 검색하고, 그 기전을 규명코자 연구를 시행하여 다음과 같은 연구결과를 얻었다. Forskolin (1.0 uM)은 흰쥐 부신적출정맥내로 1분동안 관류시킨 후 Ach(50 ug), excess $K^+$(56 mM), DMPP (100 uM) 및 caffeine (0.3 mM)에 의한 CA 분비작용을 현저히 증강시켰으나 McN-A-343에 의한 CA분비작용에는 영향을 미치지 않았다. Forskolin 자체는 CA분비작용을 일으키지 못하였다. 또한 세포의 calcium을 제거한 상태에서도 위 약물에 의한 CA분비작용에 대하여 유의한 증강작용을 나타내었다. 그러나 McN-A-343의 CA작용에는 영향이 없었으나 위의 약물의 CA분비작용을 유의하게 강화시켰다. Cyclic AMP를 증가시키는 약물로 알려져 있는 dibutyryl cyclic AMP (DBcAMP)는 300 uM농도를 1분간 관류시 Ach, excess $K^+$ 및 DMPP의 CA 분비작용을 뚜렷하게 증강시켰으나 McN-A-343 및 caffeine의 CA분비에는 별다른 영향이 없었다. DBcAMP 자체도 CA분비작용에는 영향을 미치지 못하였으나 또한 DBcAMP는 세포의 칼슘제거시에도 위의 약물에 의한 CA분비작용을 의의있게 증강시켰다. 그렇지만, McN-A-343의 CA분비작용은 증강시키지 못하였다. 이상의 연구결과로 보아 Forskolin는 adenylate cyclase를 활성화 시킴으로써 cyclic AMP 농도를 증가시켜 세포내로 칼슘유입을 증강시키며, 또한 세포내의 칼슘이동에도 관여함으로써 cholinergic nicotinic stimulation 및 depolarization에 의한 CA분비작용을 상승시키는 것으로 사료되어진다.

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뼈조직과 세포에서의 칼슘이동기전에 대한 1,25 dihydroxycholecaliciferol과 Ca Ionophore A23187의 영향 (Effects of 1,25 Dihydroxycholecalciferol and Ca Ionophore A23187 on Ca Transports in Bone and Bone Cells)

  • 이선영
    • Journal of Nutrition and Health
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    • 제21권3호
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    • pp.173-181
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    • 1988
  • Various types of evidence suggest that some changes in cellular in cellular calcium may well signal the initiation of a chain of events leading to the physiological effects of the bone resorbing agents. The effects of 1,25-dihydorxycholecalciferol, $1.25\textrm{(OH)}_2\textrm{D}_3$, Ca ionophore A23187 and calcium antagonist, diltiazem on bone resprption and the cellular transport of Ca were investigated. Bone $^{45}\textrm{Ca}$ desaturation experiment was realized in isolated heterogenous rat bone cells after equilibrating the cells with $^{45}\textrm{Ca}$. Results of $^{45}\textrm{Ca}$ desaturation experiments were analysed by fitting the $^{45}\textrm{Ca}$ desaturation curve to a model of 2 exponential terms which indicated the presence of 2 exchangeable cellular calcium pools. $1.25\textrm{(OH)}_2\textrm{D}_3$ (0.5ng/$m\ell$) induced significantly bone resorption which was decreased by the physiological dose of diltiazeme(above 5nmol/$m\ell$) although it was ineffective alone. Ionophore A23187 (0.2$\mu\textrm{g}$/$m\ell$) decreased Ca release from bone but no additivity of effect with diltiazem(20nmol/$m\ell$) was observed. $1.25\textrm{(OH)}_2\textrm{D}_3$ (0.5ng/$10^{6}$ cells) had a moderate effect on the two kinetic phases of $^{45}\textrm{Ca}$ desaturation curve and these values were normalized when diltiazeme (20nmol/$10^{6}$ cells) was added along with $1.25\textrm{(OH)}_2\textrm{D}_3$. Ionophore($0.05\mu\textrm{g}$/$10^{6}$ cells) alone increased specifically the value of the slow turnover rate which was not affected by addition of diltiazem. The hypothesis concerning the involvement of calcium in bone resorption seems in fact to be verified in case of $1.25\textrm{(OH)}_2\textrm{D}_3$ but more unsettled for Ca inophore A23187.

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Regulatory mechanisms of the store-operated Ca2+ entry through Orai1 and STIM1 by an adaptor protein in non-excitable cells

  • Kang, Jung Yun;Yang, Yu-Mi
    • International Journal of Oral Biology
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    • 제47권3호
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    • pp.33-40
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    • 2022
  • Store-operated Ca2+ entry (SOCE) represents one of the major Ca2+ entry routes in non-excitable cells. It is involved in a variety of fundamental biological processes and the maintenance of Ca2+ homeostasis. The Ca2+ release-activated Ca2+ (CRAC) channel consists of stromal interaction molecule and Orai; however, the role and action of Homer proteins as an adaptor protein to SOCE-mediated Ca2+ signaling through the activation of CRAC channels in non-excitable cells still remain unknown. In the present study, we investigated the role of Homer2 in the process of Ca2+ signaling induced by the interaction between CRACs and Homer2 proteins in non-excitable cells. The response to Ca2+ entry by thapsigargin-mediated Ca2+ store depletion remarkably decreased in pancreatic acinar cells of Homer2-/- mice, as compared to wild-type cells. It also showed critical differences in regulated patterns by the specific blockers of SOCE in pancreatic acinar cells of Homer2-/- mice. The response to Ca2+ entry by the depletion in Ca2+ store markedly increased in the cellular overexpression of Orai1 and STIM1 as compared to the overexpression of Homer2 in cells; however, this response was remarkably inhibited by the overexpression of Orai1, STIM1, and Homer2. These results suggest that Homer2 has a critical role in the regulatory action of SOCE activity and the interactions between CRAC channels.

Structure and expression analysis of the OsCam1-1 calmodulin gene from Oryza sativa L.

  • Phean-o-pas, Srivilai;Limpaseni, Tipaporn;Buaboocha, Teerapong
    • BMB Reports
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    • 제41권11호
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    • pp.771-777
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    • 2008
  • Calmodulin (CaM) proteins, members of the EF-hand family of $Ca^{2+}$-binding proteins, represent important relays in plant calcium signals. Here, OsCam1-1 was isolated by PCR amplification from the rice genome. The gene contains an ORF of 450 base pairs with a single intron at the same position found in other plant Cam genes. A promoter region with a TATA box at position-26 was predicted and fused to a gus reporter gene, and this construct was used to produce transgenic rice by Agrobacterium-mediated transformation. GUS activity was observed in all organs examined and throughout tissues in cross-sections, but activity was strongest in the vascular bundles of leaves and the vascular cylinders of roots. To examine the properties of OsCaM1-1, the encoding cDNA was expressed in Escherichia coli. The electrophoretic mobility shift when incubated with $Ca^{2+}$ indicates that recombinant OsCaM1-1 is a functional $Ca^{2+}$-binding protein. In addition, OsCaM1-1 bound the CaMKII target peptide confirming its likely functionality as a calmodulin.

Ca1-xSrxS:Mn 형광체의 합성과 광 특성 (Synthesis and Optical Properties of Ca1-xSrxS:Mn Phosphors)

  • 성혜진;허영덕
    • 한국재료학회지
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    • 제17권3호
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    • pp.137-141
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    • 2007
  • A series of $Ca_{1-x}Sr_{x}S:Mn$ phosphors were synthesized by solid-state reactions. The emission peaks of $Ca_{1-x}Sr_{x}S:Mn$ is blue shifted front 605 to 570 nm with increasing Sr content. Since $Ca_{1-x}Sr_{x}S:Mn$. Mn phosphors exhibit strong absorption in region of 254 nm, the emission wavelength of a fluorescent lamp, these phosphors can be used as wavelength tunable emitting phosphors from reddish orange to yellow. We investigated the optical and structural properties of $Ca_{1-x}Sr_{x}S:Mn$ phosphors.

배양액내 Ca : K 비율이 상추의 광합성, 증산, 생육 및 tipburn 발생에 미치는 영향 (Effects of Ca : K Ratios in Nutrient Solution on Photosynthesis, Transpiration, Growth and Incidence of Tipburn in Butterhead and Leaf Lettuce.)

  • 배종향;이용범;최기영
    • 생물환경조절학회지
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    • 제8권1호
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    • pp.42-48
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    • 1999
  • 반결구 상추 ‘Omega’와 잎상추 ‘Grand Rapids’의 m 재배에서 배양액내 Ca : K 비율이 광합성, 증산, 생육 및 tipburn 발생에 미치는 영향을 밝히고자 실험을 수행하였다. 반결구 상추와 잎상추 두 종 모두 광합성은 Ca : K 비율 3:6과 4.5:4.5에서 높았으며, 기공 저항은 잎상추가 반결구 상추보다 낮았다. 증산율은 3:6의 Ca : K 비율에서 두 종 모두 가장 높았으며, 잎상추의 증산율이 반결구 상추보다 높아 종간 차이를 보였다. 엽위에 따른 증산율은 완전 전개잎에 비해 미숙잎에서 낮았는데, 이것은 미숙잎에서 tipburn 발생이 많은 것과 깊은 관계가 있는 것으로 보였다. Ca 결핍구인 Ca : K 비율 0:9처리는 두 종 모두 극단적인 생육 저하와 함께 tipburn이 100% 발생하였으며, 반결구 상추는 Ca : K 1.5:7.5 처리에서도 tipburn이 25% 발생하였으나, 잎상추에서는 나타나지 않았다 작물 생육은 Ca 결핍구를 제외한 두 종 모두 Ca : K 3:6 처리에서 가장 높았다. 배양액의 Ca과 K의 불균형은 기공저항과 확산저항을 높여 광합성과 증산의 감소를 유도함으로써 Ca 이동에 영향을 미친 것으로 보였다.

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난소절제 골다공증 모델 흰쥐의 체내 칼슘 이용성 저하에 대한 칼슘 섭취 수준의 효과 (Effect of Dietary Calcium Levels on the Reduction of Calcium Availability in Ovariectomized Osteoporosis Model Rats)

  • 오주환
    • Journal of Nutrition and Health
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    • 제26권3호
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    • pp.277-285
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    • 1993
  • To investigate the effects of dietary calcium levels on the Ca metabolism in a rat model of ovariectomized osteoporosis, two studies were conducted. In Expt. I, five week-old femalc rats ovariectomized and fed a low Ca diet(0.06% Ca) for four weeks were compared with rats fed a normal (0.53% Ca) or low Ca diet under the sham-operated condition. Ovariectomized rats showed a significant increase in body weight and food intake. In rats fed the low Ca diet, a remarkable decrease was shown regardless of ovariectomy in serum Ca concentration, breaking force of bones, Ca and phopsphrus contents of bones, and apparent absorption and retention of Ca. Furthermore hte decrease of Ca contents of serum and bones in rats ovariectomized and fed the low Ca diet was similar to that in rats model of postmenopausal osteoporosis. In Expt. II, rats ovariectomized and fed on the low Ca diet for four weeks were divided into three groups, those given low Ca diet, normal Ca diet and high Ca diet(1.06%) respectively. The results indicated that supplementations of Ca at the intake level of 0.53% and 1.06% for 4 weeks tend to improve the relative Ca deficiency shown in experimental rat model of ovariectomized osteoporosis.

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Forskolin Changes the Relationship between Cytosolic $Ca^{2+}$ and Contraction in Guinea Pig Ileum

  • Han, Koon-Hee;Cheon, Gap-Jin;Yeon, Dong-Soo;Kwon, Seong-Chun
    • The Korean Journal of Physiology and Pharmacology
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    • 제13권3호
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    • pp.189-194
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    • 2009
  • This study was designed to clarify the mechanism of the inhibitory effect of forskolin on contraction, cytosolic $Ca^{2+}$ level $([Ca^{2+}]_i)$, and $Ca^{2+}$ sensitivity in guinea pig ileum. Forskolin (0.1 nM ${\sim}$ 10 ${\mu}M$) inhibited high $K^+$ (25 mM and 40 mM)- or histamine (3 ${\mu}M$)-evoked contractions in a concentration-dependent manner. Histamine-evoked contractions were more sensitive to forskolin than high $K^+$-evoked contractions. Spontaneous changes in $[Ca^{2+}]_i$ and contractions were inhibited by forskolin (1 ${\mu}M$) without changing the resting $[Ca^{2+}]_i$. Forskoln (10 ${\mu}M$ ) inhibited muscle tension more strongly than $[Ca^{2+}]_i$ stimulated by high $K^+$, and thus shifted the $[Ca^{2+}]_i$-tension relationship to the lower-right. In histamine-stimulated contractions, forskolin (1 ${\mu}M$) inhibited both $[Ca^{2+}]_i$ and muscle tension without changing the $[Ca^{2+}]_i$-tension relationship. In ${\alpha}$-toxin-permeabilized tissues, forskolin (10 ${\mu}M$) inhibited the 0.3 ${\mu}M$ $Ca^{2+}$-evoked contractions in the presence of 0.1 mM GTP, but showed no effect on the $Ca^{2+}$-tension relationship. We conclude that forskolin inhibits smooth muscle contractions by the following two mechanisms: a decrease in $Ca^{2+}$ sensitivity of contractile elements in high $K^+$-stimulated muscle and a decrease in $[Ca^{2+}]_i$ in histamine-stimulated muscle.