• The Korean Journal of Pharmacology
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• v.29 no.2
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• pp.183-188
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• 1993

Effects of glucose on the catecholamine release from the hypothalamic fragments in vitro were studied. Basal release of catecholamines was inversely related to the concentrations $(5{\sim}30\;mM)$ of glucose in the incubation medium. Glucose did not affect the 30 mM $K{^+}-stimulated$ release of catecholamine. In the presence of tetrodotoxin $(10\;{\mu}M)$, the inhibitory effect of glucose on the basal release of catecholamines was largely persisted, but the inhibitory effect of 30 mM glucose on dopamine release was largerly blocked. In the presence of both tetrodotoxin $(10\;{\mu}M)$ and desipramine $(3\;{\mu}M)$, glucose failed to affect the basal catecholamine release. The results suggest that glucose modulates the catecholamine release through a direct action on the catecholaminergic nerve terminals, as well as through a trans-synaptical action. The glucose-modulation of the catecholamine release may explain, at least in part, the diabetes-induced changes in the hypothalamic catecholamine metabolism.

• Journal of Adhesion and Interface
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• v.19 no.3
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• pp.123-128
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• 2018

As a mussel-inspired surface independent modification chemistry using catecholamine family molecule was suggested on 2007, there are tremendous efforts being done by researchers from around the world to adjust and develop diverse applications using catecholamine family. Accordingly, we will discuss about the novel method to extend catecholamine applications, which is through the functional group substitution of catecholamine molecules.

• Journal of Adhesion and Interface
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• v.24 no.4
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• pp.113-119
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• 2023

Since it was reported that the unusual amino acid DOPA in synergy with lysine and histidine residues found in mussel adhesive proteins plays a pivotal role in mussel adhesion in underwater environments, there has been a burgeoning development of various catecholamines-based adhesives for biomedical applications. Among these, catechol-conjugated chitosan, containing catecholamine, featuring multiple catechol groups within its aminerich chitosan backbone, has found versatile utility in fields, such as tissue adhesion, wound dressing, tissue healing, hemostats, drug delivery systems, and tissue engineering scaffolds. Significantly, chitosan-catechol is a mussel-inspired material approved by both US Food and Drug Administration (FDA) and KR Ministry of Food and Drug Safety (MFDS) for its effectiveness in hemostasis. This review focuses on 1) general aspects of catechol-conjugated chitosan, highlighting catechol group integration into chitosan backbones, 2) examination of proposed mechanisms of hemostasis, and 3) exploration of diverse physical forms, including solution, hydrogels, patches, and thin films with practical applications inapplicable to hemostasis.

• Proceedings of the Korean Society of Applied Pharmacology
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• 1992.05a
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• pp.26-26
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• 1992

신경계의 수용체 중에서 카테콜아민 신경계의 작용을 매개하는 수용체에는 $\alpha$-, $\beta$-, D-수용채 등이 있으며 카테콜아민 신경계의 활성변화를 유발시켜 인위적으로 생리현상 변화를 초래할 목적으로 사용되는 각종 의약품 등의 효능도 결국 체내에서 이들 수용체를 경유하여 발현된다는 사실들이 밝혀지고 있다. 신약대상물질의 신속한 효능검색 이외에 수용체를 활용해야 하는 중요한 신약개발 연구는 수용체의 구조 파악과 수용체와의 결합력을 근간으로 하여 신약의 기본구조에 접근하는 방식이다. 이러한 연구에서 소기의 성과를 얻기 위해서는 수용체의 추출, 정제, 특성파악, 수용체-신호전달 체계의 상관성, 수용체 관련 질병의 분류, 수용채의 클로닝 및 대량생산 등이 동반 수행되어야 한다.

• Proceedings of the Korean Society of Applied Pharmacology
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• 1992.05a
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• pp.38-38
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• 1992

횐쥐 적출 완류부신을 이용하여 neuronal nicotinic(NN) agonist인 DMPP와 M1-muscarinic agonist인 McN-A-343의 카테콜아민(CA) 분비 작용의 차이와 특성에 대해서 연구한 결과는 다음과 같다. DMPP (100 $\mu$M)와 McN-A-343(100 $\mu$M)은 부신정맥내로 투여시 유의한 카테콜아민 분비작용을 나타내었다. Mol농도로 비교시 McN-A-343의 CA분비작용은 DMPP의 약 1/5정도였다. DMPP의 CA분비작용은 chlorisondamine이나 desipramine 또는 $Ca_2$$^{2}$-free Krebs ＋ EGTA 관류등의 전처치로 의의있게 억제되었으나, pirenzepine, ouabain 및 physostigmine등 전처치에 의해서는 영향을 받지않았다. 그러나 atropine 전처치시 DMPP의 분비작용은 오히려 증강되었다.

• Proceedings of the Korean Institute of Surface Engineering Conference
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• 2012.11a
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• pp.65-65
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• 2012

카테콜아민의 일종인 노레피네프린을 이용하면 다양한 물질의 표면을 효과적으로 개질시킬 수 있음이 최근 보고되었다. 단순한 표면 개질뿐만 아니라 OH- 작용기의 도입이 가능하다는 장점을 갖는 노레피네프린 코팅법은 산화그래핀 혹은 흑연과 같은 비활성 표면에까지 성공적으로 적용되었으며, 그 결과 생체 적합성을 갖는 기능성 표면이 개발되었다.

• Development and Reproduction
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• v.6 no.2
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• pp.105-110
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• 2002

Numerous hormones are involved in the regulation of reproduction. Among them, estrogen and progesterone are the most important ovarian steroid hormones regulating female fertility. On the other hand, diverse stressors impede female receptivity and fertility. Since norepinephrine(NE) and epinephrine(E) are released from the adrenal during stress, it might play a role in stress-induced disruptions of fEmale reproductive parameters. The present study was performed to analyze the changes in adrenal catecholaminergic activities in cycling rats. The tissue content and secretion level of catecholamines were determined by high performance liquid chromatography coupled with electrochemical detector(HPLC-ECD). Adrenomedullary content of norepinephrine(NE) was increased on proestrus stage (59.47 $\pm$ 6.86 ug/gland), peaked on diestrus I stage(65.22 $\pm$ 5.99 ug/gland), and was nadir on diestrus II stage(41.63 $\pm$ 1.33 ug/gland). The highest E content was observed on proestrus stage(361.86 $\pm$ 15.58 ug/gland) while the lowest level was on diestrus II stage(285.58 $\pm$ 12.25 ug/gland). In addition to these observations, a significant reduction of the NE : E ratio was observed (1 : 4.81 on diestrus I vs 1 : 6.13～7.02 on other stages). In vitro secretion of adrenal NE and E was increased on proestrus stage, peaked on estrus stage, and decreased on diestrus II stage. Interestingly, the NE : E ratio in conditioned media was significantly increased on estrus stage (1 : 3.32 vs 1 : 2.34～2.65 on other stages. The biosynthesis of NE and E is mediated by tyrosine hydroxylase(TH) and phenylethanolamine-N-methyltransferase(PNMT) which acts conversion of tyrosine into DOPA and NE into E, respectively. These finding demonstrated that sex steroids, during setrous cycle, seem to be able to modify the adrenal catecholamines biosynthesis and secretion with stage-specific manner by modulation of the enzyme activities.

• The Korean Journal of Pharmacology
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• v.24 no.1
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• pp.31-42
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• 1988

The effect of Panaxadiol(PD), which is an active component of Korean Ginseng Saponins, on the secretion of catecholamines (CA) from the rabbit adrenal gland and its mode of action were investigated in the present study. $PD(400{\mu}g)$ increased significantly the secretion of CA from the isolated perfused rabbit adrenal gland. PD-induced secretion of CA was reduced markedly by treatment of atropine, CA secretion induced by Ach or PD was potentiated significantly by physostigmine-treatment. Chlorisondamine did inhibit CA secretion of PD or Ach. Perfusion of $PD(400{\mu}g)$ for 30 min enhanced the secretory activity of CA by Ach. Ouabain weakened the secretory response induced by PD but rather enhanced the response by Ach. Adenosine-treatment resulted in marked enhancement of CA secretion by PD or Ach, Pefusion with $Ca^{2+}-free$ Krebs containing EGTA (5 mM) for about 30 min totally blocked secretory effect induced by Ach and also weakened that by PD. From the above experimental results, it is suggested that PD causes secretion of catecholamines from the rabbit adrenal gland by a calcium-dependent exocytotic mechanism. The secretory effect of PD is due to the stimulation of cholinergic muscarinic and nicotinic receptors present in the adrenal gland and partly to a direct action on the chromaffin cell itself.

• Analytical Science and Technology
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• v.24 no.5
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• pp.319-335
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• 2011

• Proceedings of the Korean Society of Applied Pharmacology
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• 1993.04a
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• pp.150-150
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• 1993

목적 :크롬친화세포는 카테콜아민 (CA)을 분비하는 새포로서 무신 수질내에 주로 존재한다. 따라서 부신피질의 영향을 배제하여 여러가지 자율신경계 작용 약물의 약리작용을 연구하는데 중요한 조직이다. 그러므로, 부신으로부터 크롬친화세포를 분리하여 배양하는 방법을 습득하여 자율신경계 작용약물연구에 이용코자 히스타민을 이용하여 CA 분비작용을 연구하였다. 방법: 도살장에서 소를 즉사시킨 후 좌우양측 부신을 분리하여 collagenase digestion으로 부신수질로부터 분리하고 Percoll gradient에 의해서 chromaffine cell을 정제하였다. 이렇게 정제한 크롬친화세포는 Dulbecco's modified Eagle medium에 10% fetal calf serum과 함께 culture dish에다 넣어 5% $CO_2$, incubator에서 유지시켜 주면서 실험을 시행하였다. 배양세포는 분리후 일주일 이내에 사용하였다. Catecholamine측정은 electrochemical detector를 연결하여 HPLC로 측정하였다.