• Title/Summary/Keyword: Releasing concentration

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GABAA Receptor- and Non-NMDA Glutamate Receptor-Mediated Actions of Korean Red Ginseng Extract on the Gonadotropin Releasing Hormone Neurons

  • Cho, Dong-Hyu;Bhattarai, Janardhan Prasad;Han, Seong-Kyu
    • Journal of Ginseng Research
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    • v.36 no.1
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    • pp.47-54
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    • 2012
  • Korean red ginseng (KRG) has been used worldwide as a traditional medicine for the treatment of various reproductive diseases. Gonadotropin releasing hormone (GnRH) neurons are the fundamental regulators of pulsatile release of gonadotropin required for fertility. In this study, an extract of KRG (KRGE) was applied to GnRH neurons to identify the receptors activated by KRGE. The brain slice patch clamp technique in whole cell and perforated patch was used to clarify the effect of KRGE on the membrane currents and membrane potentials of GnRH neurons. Application of KRGE (3 ${\mu}g$/${\mu}L$) under whole cell patch induced remarkable inward currents (56.17${\pm}$7.45 pA, n=25) and depolarization (12.91${\pm}$3.80 mV, n=4) in GnRH neurons under high $Cl^-$ pipette solution condition. These inward currents were not only reproducible, but also concentration dependent. In addition, inward currents and depolarization induced by KRGE persisted in the presence of the voltage gated $Na^+$ channel blocker tetrodotoxin (TTX), suggesting that the responses by KRGE were postsynaptic events. Application of KRGE under the gramicidin perforated patch induced depolarization in the presence of TTX suggesting its physiological significance on GnRH response. Further, the KRGE-induced inward currents were partially blocked by 6-cyano-7-nitroquinoxaline-2,3-dione (CNQX; non-NMDA glutamate receptor antagonist, 10 ${\mu}M$) or picrotoxin (PIC; $GABA_A$ receptor antagonist, 50 ${\mu}M$), and almost blocked by PIC and CNQX mixture. Taken together, these results suggest that KRGE contains ingredients with possible GABA and non-NMDA glutamate receptor mimetic activity, and may play an important role in the endocrine function of reproductive physiology, via activation of $GABA_A$ and non-NMDA glutamate receptors in GnRH neurons.

Novel Bombesin Analogues Conjugated with DOTA-Ala(SO3H)-4 aminobenzoic acid and DOTA-Lys(glucose)-4 aminobenzoic acid: Synthesis, Radiolabeling, and Gastrin Releasing Peptide Receptor Binding Affinity

  • Lim, Jae Cheong;Choi, Sang Mu;Cho, Eun Ha;Kim, Jin Joo
    • Journal of Radiation Industry
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    • v.7 no.2_3
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    • pp.191-200
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    • 2013
  • In this study, a novel bombesin (BBN) analogues, DOTA-Ala($SO_3H$)-4 aminobenzoyl-Gln-Trp-Ala-Val-Gly-His-Leu-Met-$NH_2$ (DOTA-sBBN) and DOTA-Lys(glucose)-4 aminobenzoyl-Gln-Trp-Ala-Val-Gly-His-Leu-Met-$NH_2$ (DOTA-gluBBN), were synthesized and radiolabeled, and their binding affinities were evaluated. Peptides were prepared by a solid phase synthesis method and their purities were over 98%. DOTA is the chelating agent for $^{177}Lu$-labeling, and the DOTA-conjugated peptides were radiolabeled with $^{177}Lu$ by a high radiolabeling yield (>98%). The Log P values of DOTA-sBBN and DOTA-gluBBN were -2.20 and -2.79, respectively. 50.41% of $^{177}Lu$-DOTA-sBBN and 72.97% of $^{177}Lu$-DOTA-gluBBN were left undegraded by the serum incubation at $37^{\circ}C$ for 48 hr. A competitive displacement of $^{125}I-[Tyr^4]$-BBN on the PC-3 human prostate carcinoma cells revealed that 50% inhibitory concentration ($IC_{50}$) were 1.46 nM of DOTA-sBBN and 4.67 nM of DOTA-gluBBN indicating a highly nanomolar binding affinity for GRPR. Therefore, it is concluded that $^{177}Lu$-DOTA-sBBN and $^{177}Lu$-DOTA-gluBBN can be potential candidates as a targeting modality for the Gastrin-releasing peptide receptor (GRPR)-over-expressing tumors, and further studies to evaluate their biological and pharmacological characteristics are needed.

Review of Sarcoplasmic Reticulum Ca$^{2+}$ Releasing Mechanisms in Skeletal Muscle Contraction (골격근 수축에 있어서 근장그물로부터의 Ca$^{2+}$ 유리 기전에 대한 고찰)

  • Koo, Hyun-Mo;Kim, Jin-Sang
    • The Journal of Korean Physical Therapy
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    • v.13 no.1
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    • pp.237-243
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    • 2001
  • Skeletal muscle cells are activated by ${\alpha}$-motorneurons which release acetylcholine at the neuromuscular junction. This results in a local depolarization of surface membrane which triggers an action potential. The action potential propagates along the surface membrane and also into the T-tubule system. In the triads T-tubules are in close connection with the terminal cisternae of the sarcoplasmic reticulum(SR). The action potential activaies T-tubule voltage sensors(DHP receptors). which activates SR Ca$^{2+}$ release channels(ryanodinc receptors). Ca$^{2+}$ have a key role in skeletal muscle in that an increase of free myoplasmic Ca$^{2+}$ concentration. The process of coupling chemical and electrical signals at the cell surface to the intracellular release of Ca$^{2+}$and ultimate contraction of muscle fibers is termed excitation-contraction coupling(ECC). Coupling of cel1 surface signals to intracellular Ca$^{2+}$ release proceeds by several mechanisms in skeletal muscle cells. This review focus on sarcopiasmic reticulum(SR) Ca$^{2+}$ releasing mechanisms from sarcoplasmic reticulum in the skeletal muscle. The mechanisms include DCCR, CICR, and HCR.

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Regulation of Prolactin Secretion: Dopamine is the Prolactin-release Inhibiting Factor (PIF), but also Plays a Role as a Releasing Factor (PRF)

  • Shin, Seon H.;Song, Jin-Hyang;Ross, Gregory M.
    • Animal cells and systems
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    • v.3 no.2
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    • pp.103-113
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    • 1999
  • Many in-depth reviews related to regulations of prolactin secretion are available. We will, therefore, focus on controversial aspects using personal opinion in this review. The neuroendocrine control of prolactin secretion from the anterior pituitary gland involves multiple factors including prolactin-release inhibiting factor (PIF) and prolactin releasing factor (PRF). The PIF exerts a tonic inhibitory control in the physiological conditions. The PIF should be able to effectively inhibit prolactin release or a lifetime, but the inhibitory action of dopamine cannot be sustained for a long period of time. Perifusion of a high concentration of dopamine (l ,000 nM) could not sustain inhibitory action on prolactin release but when a small amount of ascorbic acid (0.1 mM) is added in a low concentration of dopamine (3 nM) solution, prolactin release was inhibited for a long period. Ascorbate is essential for dopamine action to inhibit prolactin release. We have, therefore, concluded that the PIF is dopamine plus ascorbate. The major transduction system for dopamine to inhibit prolactin release is the adenylyl cyclase system. Dopamine decreases cyclic AMP concentration by inhibiting adenylyl cyclase, and cyclic AMP stimulates prolactin release. However, the inhibitory mechanism of dopamine on prolactin release is much more complex than simple inhibition of CAMP production. The dopamine not only inhibits cyclic AMP synthesis but also inhibits prolactin release by acting on a link(s) after the CAMP event in a chain reaction for inhibiting prolactin release. Low concentrations of dopamine stimulate prolactin release. Lactotropes are made of several different subtypes of cells and several different dopamine receptors are found in pituitary. The inhibitory and stimulatory actions induced by dopamine can be generated by different subtype of receptors. The GH$_4$ZR$_7$ cells express only the short isoform (D$_{2s}$) of the dopamine receptor, as a result of transfecting the D$_{2s}$ receptors into GH$_4$C$_1$ cells which do not express any dopamine receptors. When dopamine stimulates or inhibits prolactin release in GH$_4$ZR$_7$ cells, it is clear that the dopamine should act on dopamine D$_{2s}$ receptors since there is no other dopamine receptor in the GH$_4$ZR$_7$. Dopamine is able to stimulate prolactin release in a relatively low concentration while it inhibits in a high concentration in GH$_4$ZR$_7$. These observations indicate that the dopamine D$_2$ receptor can activate stimulatory and/or inhibitory transduction system depending upon dopamine concentrations.

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A Fire Simulation of Light Railway Transit (경량전철시스템의 화재 시뮬레이션)

  • Won Chan-Shik;Lee Ki-Choon;Hur Nahmkeon;Mok Jae-Kyun
    • 한국전산유체공학회:학술대회논문집
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    • 2001.05a
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    • pp.170-175
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    • 2001
  • Fire inside light railway transit(LRT) was simulated for various fire scenarios using CFD analysis in order to assess the safety of passengers. Considered in the present paper are the effects of locations of fire, a fire size, an operation of ventilation system and an opening time of door on evolution of temperature and smoke concentration inside the LRT. For fire simulation, fire cells releasing heat and smoke corresponding to fire size were positioned at the location of fire. From the results, it is seen that the ventilation system and the opening time of door were the most important factors on temperature and smoke concentration inside the LRT

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Peroxynitrite Inactivates Carbonic Anhydrase II by Releasing Active Site Zinc Ion

  • Kim, Young-Mi;Han, Sang-Hwa
    • Bulletin of the Korean Chemical Society
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    • v.25 no.5
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    • pp.711-714
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    • 2004
  • Peroxynitrite enters erythrocytes through band 3 anion exchanger and oxidizes cytosolic proteins therein. As a protein associated with band 3, carbonic anhydrase II may suffer from peroxynitrite-induced oxidative damages. Esterase activity of carbonic anhydrase II decreased as the concentration of peroxynitrite increased. Neither hydrogen peroxide nor hypochlorite affected the enzyme activity. Inactivation of the enzyme was in parallel with the release of zinc ion, which is a component of the enzyme's active site. SDS-PAGE of peroxynitrite-treated samples showed no indication of fragmentation but non-denaturing PAGE exhibited new bands with lower positive charges. Western analysis demonstrated that nitration of tyrosine residues increased with the peroxynitrite concentration but the sites of nitration could not be determined. Instead MALDI-TOF analysis identified tryptophan-245 as a site of nitration. Such modification of tryptophan residues is responsible for the decrease in tryptophan fluorescence. These results demonstrate that peroxynitrite nitrates tyrosine and tryptophan residues of carbonic anhydrase II without causing fragmentation or dimerization. The peroxynitrite-induced inactivation of the enzyme is primarily due to the release of zinc ion in the enzyme's active site.

Microencapsulation of Dibutylphthalate by Interfacial Polymerization (계면중합에 의한 Dibutylphthalate의 마이크로 캡슐화)

  • 박차철;김호정;김한도
    • Textile Coloration and Finishing
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    • v.7 no.3
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    • pp.15-21
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    • 1995
  • Polyurethane microcapsules containing dibutylphthalate(DBP) were perpared by the interfacial polymerization using diisocyanates and polyois. Effects of chemical structure of PU, dispersing agent and polymerization time on the mean diameter of microcapsules were investigated. The releasing of DBP from microcapsules depended on the chemical structure of PU and solvents. The diameter decreased with increasing dispersing agent concentration, and it is decreased in the order of the dispersing agents using gelatine > PVA > arabic gum at the same concentration. A slight increase in the diameter was observed when the ratio C$H_2$/OOCNH of PU was increased. As the ratio C$H_2$/OOCNH of PU was increased, the amount of extracted DBP for hexane using as a extracting solvent was decreased, however, it was not changed for THF.

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Oxime Generation of Silk Fibers by Hydroxlammonium choride treatment

  • Bae, Do-Gyu
    • Journal of Sericultural and Entomological Science
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    • v.41 no.2
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    • pp.116-121
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    • 1999
  • This study was aimed to explain the essence of Hydroxylammonium hydrochloride(H.A.) effect on degummed silk fiber increasing the colour sites due to oxime generating reaction. H.A. in aqueous solution caues to increase the amount of [H+] and reduce pH values as the concentration of H.A. increases. The rate of [H+] absorption of silk fiker in acidic solution differs on the basic of solution pH and shows a specific uptake in each pH, the lower the pH of solution, the higher the amount [H+] absorption. The pH of solution after treating of silk fiber in H.A. and HCl, showed more remaining [H+] in H.A. solution due to [H+] releasing under the procedure of oxime production. Also it was revealed that in higher concentration of H.A. the reaction for oxime fixation in silk fiber carried out stonger and as a result the bigger gap with acid uptake curve appeared. FT-IR analysis of silk fiber treated with H.A. revealed the creating of intermolecular H-bond at the 2,981-2.930 cm-1, which was not appeared for nontraeted silk fibers and shows H-bond between N-OH group in oue chain and C=) group in another chain of silk protein. Colourimetry of dyed silk fiber after H.A. tratment showed that the silk fiber treated with the high concentration of H.A. compare to low concentration, absorbed more dyeing molecules and so Showed less percontage of Whiteness.

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Effect of Twice Daily Administration of GH-releasing Peptide-2 for 10 Days on Growth Performance, Plasma GH Responses and Insulin-like Growth Factor-1 Concentrations in Swine

  • Nou, V.;Inoue, H.;Lee, H.G.;Matsunaga, N.;Kuwayama, H.;Hidari, H.
    • Asian-Australasian Journal of Animal Sciences
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    • v.16 no.8
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    • pp.1193-1198
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    • 2003
  • An increase in frequency of administration of exogenous growth hormone (GH) or GH-releasing hormone was reported to be a model to increase blood circulating insulin-like growth factor-1 (IGF-1) and to improve growth performance in animals. We have investigated the effect of twice daily administration of GH-releasing peptide-2 (GHRP-2) on growth performance, GH responsiveness and plasma insulin-like growth factor IGF-1 in swine. We administered to eight swine, 3 control and 5 treatment, a twice daily s.c. injections of GHRP-2 ($30{\mu}g/kg\;BW$) for a period of 10 days. Every day blood samples immediately taken before injections of GHRP-2 or saline, at 08:00 h and 16:00 h, were measured for IGF-1 concentrations. Blood samples for GH assay were collected every 20 min on days 1, 6 and 10, from 1 hour before and 3 h after GHRP-2 or saline injections at 08:00 h. GH peak concentrations and GH area under curve (GH AUC) on day 1, 6 and 10 in treatment group of swine were higher than those in control swine (p<0.05). Twice daily administration of GHRP-2 caused a significantly attenuation (p<0.05) of GH peak concentrations ($80.25{\pm}13.87$, $39.73{\pm}5.72$ and $27.57{\pm}6.06ng/ml$ for day 1, 6 and 10, respectively) and GH AUCs ($3,536.15{\pm}738.35$, $1,310.31{\pm}203.55$ and $934.37{\pm}208.99ng/ml$ for day 1, 6 and 10, respectively). However, there was no significant difference in GH peak concentration and GH AUC between day 6 and 10. Plasma IGF-1 concentration levels were higher in treatment than control group of swine (p<0.05) after 3 days of the treatment, and the levels reached a plateau from day 3 to 10 of experiment. Growth performance did not alter by GHRP-2 administration, even though a numerical increase of body weight gain and feed efficiency was observed. These results indicate that twice daily administration of GHRP-2 for 10 days in swine did not significantly influence on growth performance, caused an overall attenuation of GH response, and that elevation of plasma GH concentrations caused by GHRP-2 administration increased plasma IGF-1 concentrations, even though an attenuation of GH response was observed.

Glutamate attenuates lipopolysaccharide induced intestinal barrier injury by regulating corticotropin-releasing factor pathway in weaned pigs

  • Guo, Junjie;Liang, Tianzeng;Chen, Huifu;Li, Xiangen;Ren, Xiaorui;Wang, Xiuying;Xiao, Kan;Zhao, Jiangchao;Zhu, Huiling;Liu, Yulan
    • Animal Bioscience
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    • v.35 no.8
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    • pp.1235-1249
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    • 2022
  • Objective: The purpose of this study was to evaluate the protection of glutamate (GLU) against the impairment in intestinal barrier function induced by lipopolysaccharide (LPS) stress in weaned pigs. Methods: Twenty-four weaned pigs were divided into four treatments containing: i) non-challenged control, ii) LPS-challenged control, iii) LPS+1.0% GLU, and iv) LPS+2.0% GLU. On day 28, pigs were treated with LPS or saline. Blood samples were collected at 0, 2, and 4 h post-injection. After blood samples collection at 4 h, all pigs were slaughtered, and spleen, mesenteric lymph nodes, liver and intestinal samples were obtained. Results: Dietary GLU supplementation inhibited the LPS-induced oxidative stress in pigs, as demonstrated by reduced malondialdehyde level and increased glutathione level in jejunum. Diets supplemented with GLU enhanced villus height, villus height/crypt depth and claudin-1 expression, attenuated intestinal histology and ultrastructure impairment induced by LPS. Moreover, GLU supplementation reversed intestinal intraepithelial lymphocyte number decrease and mast cell number increase induced by LPS stress. GLU reduced serum cortisol concentration at 4 h after LPS stress and downregulated the mRNA expression of intestinal corticotropin-releasing factor signal (corticotrophin-releasing factor [CRF], CRF receptor 1 [CRFR1], glucocorticoid receptor, tryptase, nerve growth factor, tyrosine kinase receptor A), and prevented mast cell activation. GLU upregulated the mRNA expression of intestinal transforming growth factor β. Conclusion: These findings indicate that GLU attenuates LPS-induced intestinal mucosal barrier injury, which is associated with modulating CRF signaling pathway.