• Journal of Plant Biology
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• v.32 no.4
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• pp.215-226
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• 1989

The effects of Ca2+ on polyamines on callose contents of carrot suspension cultured cells were studied. The regeneration process of the cell wall of carrot protoplast observed through the electron microscope. Treatment of the carrot suspension cultured cells with Ca2+ and polyamines resulted in considerable increase on callose contents at 0.1 mM of Ca2+ and polyamines, particulary spermidine. Poly-L-lysine and poly-L-ornithine increased about 30% and 100% of callose contents than that of the control respectively, whereas verapamil and flunarizine markedly decreased the callose contents. These effects of Ca2+ of free ion rather than as Ca2+-calmodulin complex. During the cultivation of the protoplast, the regeneration of the cell wall was somewhat observed on the 4th day, however, it was inhibited by verapamil. These results suggested that the promotive action of Ca2+ and polyamines were manifested in the callose contents and the regeneraton of the cell wall.

• Journal of Plant Biology
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• v.33 no.4
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• pp.315-320
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• 1990

We investigated the interaction of auxin and Ca2+ on coleoptile segment elongation in seedlings of Zea mays L. Seedlings imbibed and raised either in the presence of 10 mM CaCl2 (HC), or in the absence of Ca2+ (LC) were used. Exposure to 10-5M auxin of coleoptiles from either HC or LC seedlings resulted in strong promotion of elongation. However, longer latent period (90 min) of the auxin effect was observed in HC than in LC seedlings (20 min). The length of latent period observed in HC coleoptiles was proportional to the concentration of CaCl2. The latent period of auxin effect observed in HC seedlings was abolished by pretreatment of the coleoptiles with TMB-8 which inhibits IP3-induced Ca2+ release from the tonoplasts. In segments of LC seedlings, the promotive effect of IAA (10-5M) was abolished by treatment with 5 mM calcium but was reversible upon treatment of the segments with 5 mM EGTA. These results suggest that the effect of auxin on coleoptile elongation is closely related to intracellular Ca2+ level.

• BMB Reports
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• v.43 no.3
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• pp.151-157
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• 2010

$Ca^{2+}$ is a universal signalling molecule that affects a variety of cellular processes including cardiac development. The majority of intracellular $Ca^{2+}$ is stored in the endoplasmic and sarcoplasmic reticulum of muscle and non-muscle cells. Calreticulin is a well studied $Ca^{2+}$-buffering protein in the endoplasmic reticulum, and calreticulin deficiency is embryonic lethal due to impaired cardiac development. Despite calsequestrin being the most abundant $Ca^{2+}$-buffering protein in the sarcoplasmic reticulum, viability is maintained in embryos without calsequestrin and normal $Ca^{2+}$ release and contractile function is observed. The $Ca^{2+}$ homeostasis regulated by the endoplasmic and sarcoplasmic reticulum is critical for the development and proper function of the heart.

• Journal of the Korean Ceramic Society
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• v.30 no.11
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• pp.905-910
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• 1993

$\alpha$-tricalcium phosphate($\alpha$-TCP) powders were synthesized and their hydration properties were investigated in Tris. solution. Two kinds of $\alpha$-TCP powder samples were prepared; the one is reaction product of CaHPO4.2H2O and CaCO3, and another is that of hydroxyapatite(HAp) and $\beta$-Ca2P2O7. They were satisfied with Ca/P mole ratio 1.5 and were heated at 150$0^{\circ}C$ for 5 hours. In the hydration of $\alpha$-TCP samples the powder which was synthesized from HAp and $\beta$-Ca2P2O7 was hydrated faster than that from CaHPO4.2H2O and CaCO3. The hydration reaction of $\alpha$-TCP powder transformed rapidly into HAp accompanying setting and hardening. It was realized that the hydration reaction of $\alpha$-TCP was due to the solution-precipitation mechanism and the hydrates from the reaction were Ca-deficient HAp having funtional group HPO42-.

• The Korean Journal of Physiology
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• v.21 no.1
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• pp.47-58
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• 1987

It has been reported that the luteal function may be regulated by the intracellular $Ca^{++}$ level which may be adjusted partially by the high affinity $Ca^{++}-ATPase$ in luteal cell membranes. Then, one may expect that luteotropic and/or luteolytic agents, such as gonadotropins, prostaglandin $F_{2{\alpha}}\;(PGF_{2{\alpha}})$ and ouabain, affect the intracellular $Ca^{++}$ level. In this present study, therefore, we examined the effects of luteinizing hormone (LH, or human chorionic gonadotropin, hCG), $PGF_{2{\alpha}}$ and ouabain on the kinetic properties of the high affinity $Ca^{++}-ATPase$ in light membrane, heavy membrane, and microsomal fractions from the highly luteinized ovary. LH (or hCG) increased the affinity and the Vmax for $Ca^{++}$ both in light membrane and heavy membrane. $PGF_{2{\alpha}}$ increased the Vmax in light membrane and decreased the Km in heavy membrane for $Ca^{++}$ at low concentration $(5\;{\mu}g/ml)$. At higher concentration, however, $PGF_{2{\alpha}}$ oppositly affected on kinetic properties, that shown at low concentration. Ouabain, a potent inhibitor of $Na^+-K^+-ATPase$, increased the Km at high concentration $(10^{-4}\;M)$, however, decreased the Vmax for $Ca^{++}$ in light membrane at low concentration $(10^{-6}\;M)$. Also, ouabain increased the Km for $Ca^{++}$ in heavy membrane without changes in the Vmax at both concentrations. It seems that LH and low dose of $PGF_{2{\alpha}}$ increase the intracellular $Ca^{++}$ level and cause in activation of $Ca^{++}-ATPase$, however, higher dose of $PGF_{2{\alpha}}$ and ouabain inhibit directly $Ca^{++}-ATPase$ activity and result in increase in intracellular $Ca^{++}$ level. According to the above results, we suggest that luteotropic and/or luteolytic agents regulate the luteal progesterone $(P_4)$ production through two different pathways; one is cyclic adenosine monophosphate (cAMP)-dependent and another is $Ca^{++}-dependent$. Intracellula. $Ca^{++}$ level regulated by the high affinity $Ca^{++}-ATPase$ may affect both pathways in a time-dependent fashion. LH (or hCG) acts on the luteal $P_4$ production via both pathways. The initial step is $Ca^{++}$ dependent, and the late step is cAMP dependent. $PGF_{2{\alpha}}$ and ouabain increase the intracellular $Ca^{++}$ concentration so that basal luteal $P_4$ production is increased and LH-stimulated $P_4$ production is inhibited by the inhibiting LH-dependent adenylate cyclase activity.

• Applied Biological Chemistry
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• v.28 no.2
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• pp.56-61
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• 1985

The mass balances of calcium salts during the manufacturing processes of Tofu were established by conductometric method and chemical analysis method. During the manufacturing processes of soy milk and Tofu, 66% of solid and 63% of calcium was transfered from soy-bean to the soy milk, and 47.8% of total solid from soybean was transfered to the Tofu, respectively. When the $CaCl_2$ was used as coagulant, calcium contents in Tofu $(Y_{Tofu},\;mg{\cdot}Ca/g{\cdot}Tofu,\;wet\;basis)$ and drained solution $(Y_{drained\;soln},\;mg{\cdot}Ca/ml{\cdot}drained\;soln.)$ were linearly increased with the amounts of $CaCl_2(C,g{\cdot}CaCl_2/ml{\cdot}soy\;milk)$ added in soy milk, and correlative equations between them were obtained as $Y_{Tofu}=0.3369\;C+1.2689$ for Tofu$(moisture\;content:\;81.5{\pm}0.5%)$ with r=0.9898, and $Y_{drained\;soln}= 0.2899C+0.0399$ for drained solution with r= 0.9991. It was proved that conductometric method was reasonably applicable to the measurement of calcium contents of the products from every processes of Tofu manufacture except soy-bean. However the conductometric method was not recomendable in the case of $CaSO_4$ as coagulant due to its low solubility ana uneven distribution in soy milk and Tofu tissue.

• Journal of the Korean Ceramic Society
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• v.37 no.12
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• pp.1178-1186
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• 2000

타일의 내마모성과 내산성을 향상시키기 위해 결정화유리가 최근에 새로운 유약 재료로서 소개되고 있다. 신 유약의 연구에 사용된 조성은 $Ca_2$ZrSi$_4$O$_{12}$ 상에 근접하는 CaO-ZrO$_2$-SiO$_2$계의 유리조성의 분말로, 마이크로파 가열 (2.45 GHz)에 의해서 900-120$0^{\circ}C$의 0-20분간 소성되어 평가되었다. 그 결과, 100$0^{\circ}C$ 이상에서 소성한 시편은 내부 결정화를 나타내었으며, 결정상은 미세(5$mu extrm{m}$)한 크기를 갖는 $Ca_2$ZrSi$_4$O$_{12}$가 주 결정상이며, $Ca_2$ZrSi$_4$O$_{12}$, CaSiO$_3$, SiO$_2$의 세 상이 나타났다. 소결체의 미세구조는 사용한 유리분말의 입도의 영향을 받았다. 미세분말 (<38$\mu\textrm{m}$)을 이용한 소결체의 조직이 조세분말 (45-150$\mu\textrm{m}$)의 경우보다 수축율면에서 높았으며 낮은 기공도를 갖는 미세구조를 가졌다. 마이크로파에 의한 유리분말의 소성은 1000-120$0^{\circ}C$ 구간에서 10분 이내 결정화가 완료되는 급속 가열 공정이었으며 CaO-ZrO$_2$-SiO$_2$계 결정화 유리 제조에 균일한 체적가열을 할 수 있었다.

• The Korean Journal of Physiology and Pharmacology
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• v.7 no.6
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• pp.375-379
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• 2003

$Ca^{2+}$ influx appears to be important for triggering myoblast fusion. It remains, however, unclear how $Ca^{2+}$ influx rises prior to myoblast fusion. Recently, several studies suggested that NMDA receptors may be involved in $Ca^{2+}$ mobilization of muscle, and that $Ca^{2+}$ influx is mediated by NMDA receptors in C2C12 myoblasts. Here, we report that other types of ionotropic glutamate receptors, non-NMDA receptors (AMPA and KA receptors), are also involved in $Ca^{2+}$ influx in myoblasts. To explore which subtypes of non-NMDA receptors are expressed in C2C12 myogenic cells, RT-PCR was performed, and the results revealed that KA receptor subunits were expressed in both myoblasts and myotubes. However, AMPA receptor was not detected in myoblasts but expressed in myotubes. Using a $Ca^{2+}$ imaging system, $Ca^{2+}$ influx mediated by these receptors was directly measured in a single myoblast cell. Intracellular $Ca^{2+}$ level was increased by KA, but not by AMPA. These results were consistent with RT-PCR data. In addition, KA-induced intracellular $Ca^{2+}$ increase was completely suppressed by treatment of nifedifine, a L-type $Ca^{2+}$ channel blocker. Furthermore, KA stimulated myoblast fusion in a dose-dependent manner. CNQX inhibited not only KA-induced myoblast fusion but also spontaneous myoblast fusion. Therefore, these results suggest that KA receptors are involved in intracellular $Ca^{2+}$ increase in myoblasts and then may play an important role in myoblast fusion.

• Bulletin of the Korean Chemical Society
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• v.30 no.8
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• pp.1703-1710
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• 2009

The single-crystal structure of |$Ca_{35.5}$|[$Si_{121}Al_{71}O_{384}$]-FAU, $Ca_{35.5}Si_{121}Al_{71}O_{384}$ per unit cell, a = 24.9020(10) $\AA$, dehydrated at 673 K and 2 ${\times}\;10^{-6}$Torr, has been determined by single-crystal X-ray diffraction techniques in the cubic space group Fd$\overline{3}$m at 294 K. The large single crystals of zeolite Y (Si/Al = 1.70) were synthesized up to diameters of ${\mu}m\;and\;Ca^{2+}$-exchanged zeolite Y were prepared by ion exchange in a batch method of 0.05 M aqueous Ca($NO_3)_2$ for 4 hrs at 294 K. The structure was refined using all intensities to the final error indices (using only the 971 reflections for which $F_o\;>\;4{\sigma}(F_o))\;R_1$ = 0.038 (based on F) and $R_2$ = 0.172 (based on $F^2$). About 35.5 $Ca^{2+}$ ions per unit cell are found at an unusually large number of crystallographically distinct positions, four. Nearly filling site I (at the centers of the double 6-rings), 14.5 octahedrally coordinated $Ca^{2+}$ ions (Ca-O = 2.4194(24) $\AA$ and O-Ca-O = 87.00(8) and 93.00($8^o$) are found per unit cell. One $Ca^{2+}$ ion per unit cell is located at site II’ in the sodalite cavity and extends 0.50 $\AA$ into the sodalite cavity from its 3-oxygen plane (Ca-O = 2.324(13) $\AA$ and O-Ca-O = 115.5(10)o). The remaining twenty $Ca^{2+}$ ions are found at two nonequivalent sites II (in the supercages) with occupancies of 10 and 10 ions, respectively. Each of these $Ca^{2+}$ ions coordinates to three framework oxygens, either at 2.283(3) or 2.333(5) $\AA$, respectively, and extends either 0.24 or 0.54 $\AA$, respectively, into the supercage from the three oxygens to which it is bound. In this crystal, site I is the most populated; sites II’ and II are only sparsely occupied.$Ca^{2+}$+ appears to fit the octahedral site I best. No cations are found at sites III or III’, which are clearly less favorable for $Ca^{2+}$ ions in dehydrated zeolite Y.

• Resources Recycling
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• v.15 no.4 s.72
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• pp.27-35
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• 2006

In order to use alunite as an activator of blast furnace slag, we studied the hydration characteristics of the calcined alunite and the ground blast furnace slag. The alunite calcined at $650{\cire}C$ consists of KAl($KAl(SO_{4})_{2}$ and $Al_{2}O_{3}$. The calcined alunite reacts with $Ca(OH)_{2}$ and gypsum to form etrringite ($3CaO{\cdot}Al_{2}O_{3}{\cdot}3CaSO_{4}{\cdot}32H_{2}O$) as fellows:$2KAl(SO_{4})_{2}+2Al_{2}O_{3}+13Ca(OH)_{2}+5CaSO_{4}{\cdot}2H_{2}O+73H_{2}O{\rightarrow}3(3CaO{\cdot}Al_{2}O_{3}{\cdot}3CaSO_{4}{\cdot}32H_{2}O)+2KOH$. The $SO_{4}^{2-}$ ions from calcined alunite reacts with CaO in blast furnace slag to from gypsum, which reacts with CaO and $Al_{2}O_{3}$ to from ettringite in calcined alunite-blast furnace slag system. Therefore blast furnace slag can be activated by calcined alunite.