• 생명과학회지
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• 제8권2호
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• pp.189-196
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• 1998

다양한 동물세포로부터 그 cDNA가 dlining된 glycosylphosphatidylinositol-linked ADP-ribosyltransferase는 공통적으로 carboxy말단에 풍부한 glutamic acid motif (EEEVLP)를 소유하고 있다. 유사한 motif가 mouse 임파구의 ADP-ribosyltransferase(Yac-2)에서 발견되어진다. Yac-2는 ADP-ribosyltransferase 활성 뿐 아니라 NDA glycohyrolase의 활성도 소유하고 있다. yac-2에 있어, Glutamic acid가 풍부한 motif의 역할을 알아보기 위해 site-directed mutagensis가 수행 되었다. 돌연변이체인 E22OQ, E22OA, E222Q, E222A는 ADP-ribosyltransferase에 대해 불활성을 보였다. 이러한 결과는 Yac-2의 220번과 222번의 glutamic acid가 ADP-ribosyltransferase와 NDA glycohydrolase 활성에 필수적임을 나타내는 것으로, 이는 carboxy말단의 glutamic acid들이 Yac-2 효소의 활성에 중요한 역할을 함을 시사하는 것이라 하겠다.

• Journal of Life Science
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• 제10권1호
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• pp.20-23
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• 2000

Mono-ADP-ribosylation, catalyzed by ADP-ribosyltransferases, is a post-translational modification of proteins in which the ADP-ribose moiety of NAD is transferred to an acceptor protein. Previously, we have identified and cloned a glycosylphosphatidylinositol-linked ADP-ribosyltransferase (Yac-1) from mouse lymphoma cells. Yac-1 enzyme contains three regions (region I,II,III) similar to those found in several bacterial toxins and vertebrate ADP-ribosyltransferases. Site-directed mutagenesis was performed to verify the role of Glu 233 in region III. Mutants E233Q, E233D and E233A were inactive for ADP-ribosyltransferase activity. Thus Glu 233 in Yac-1 is essential for enzyme activity, suggesting that Glu 233 in Glu-rich motif near the carboxy terminus plays a catalytic role in ADP-ribosyltransferase activity.

• 한국해안해양공학회지
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• 제14권3호
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• pp.222-231
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• 2002

ADP는 음향의 Doppler효과를 이용하여 층별 유속과 유향을 측정하는 장비이며, 최근에는 반사음향의 강도로부터 부유 퇴적물의 농도측정이 가능하다고 제기되고 있다. 본 연구에서는 염산 인근의 한 정점에 ADP 기기를 설치하고 자료를 수집하였다. 부유사 농도를 분석하기 위하여 해수 분석을 통한 음향계수를 정한 후 보정된 음향강도를 이용하여 부유사 농도를 구하였다. 관측된 부유사 농도분포 식은 해석해와 비교하였으며, 농도변화의 경향에 대해서는 비교적 양호한 결과를 나타냈다. 또한, 관측기간 동안의 부유물질의 이동량에 대한 정량적 결과를 얻었으며 ADP를 활용한 연직방향의 부유입자 농도변화를 관측할 수 있음을 보였다.

• 한국응용과학기술학회지
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• 제24권1호
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• pp.61-66
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• 2007

X-ray diffraction studies have been made to investigate the effects of binding of ADP, ADP+Vi, ADP+AIF4, $ADP+BeF_3$ on the structure of glycerinated rabbit skeletal muscle in the rigor state. Although these phosphate analogs are known to bind actively cycling myosin heads, it is not clear whether they can bind to the attached heads in the rigor muscle. We have found that these analogs can bind to the myosin heads attached to actin filaments in the rigor state. The present results indicate that (1) bound myosin heads altered their conformation in the proximal end toward the plane perpendicular to the fiber axis when MgADP bound to them, and (2) myosin heads were dissociated substantially (up to 50%) from actin filaments but still remained in the vicinity of actin filaments when MgADP and metallofluorides (AIF4 and BeF3) or vanadate bound to them. We detected new conformations of myosin heads attached to actin filaments when they had MgADP or ADP.Pi analogs. We report here these findings on the effects of MgADP and MgADP+phosphate analogs to the rigor crossbridges.

• Molecules and Cells
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• 제37권1호
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• pp.9-16
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• 2014

ADP-ribosylation is a type of posttranslational modification catalyzed by members of the poly(ADP-ribose) (PAR) polymerase superfamily. ADP-ribosylation is initiated by PARPs, recognized by PAR binding proteins, and removed by PARG and other ADP-ribose hydrolases. These three groups of proteins work together to regulate the cellular and molecular response of PAR signaling, which is critical for a wide range of cellular and physiological functions.

• IMMUNE NETWORK
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• 제5권4호
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• pp.199-204
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• 2005

Background: ADP-ribosyl pyrophosphatases (ADPRase) has been known to catalyze the hydrolysis of ADP-ribose to ribose-5-phosphate and AMP. The role of ADPRase has been suggested to sanitize the cell by removing potentially toxic ADP-ribose. In this study, we examined the effect of nitric oxide on ADPRase activity in macrophages. Methods: ADPRase activity was measured in NO-inducing J774 cells. For in vitro experiments, recombinant human ADPRase was prepared in bacteria. Results: ADPRase activity was increased by the treatment of exogenous NO generating reagent, sodium nitroprusside (SNP), in J774 cells. The increased ADPRase activity was mediated by the post-translational modification, likely to cause cADP-ribosylation via nitrosylation of cysteine residue on the enzyme. The stimulation with endogeneous NO inducers, $TNF-{\alpha}/IFN-{\gamma}$, also increased ADPRase activity through NO synthesis. Futhermore, ADPRase activity may be mediated by the post-translational modification of ADPRase, ADP-ribosylation. Conclusion: These results indicate that NO synthesized by macrophage activation plays a critical role in the increase in ADPRase activity following ADP-ribose metabolism.

• Biomolecules & Therapeutics
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• 제11권1호
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• pp.51-57
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• 2003

General pharmacological properties of ADP, a new pharmaceutical composition, which contains a mixed water extract obtained from the mixture of Phellodendron cortex (Phellodendron amurense) and Anemarrhena rhizoma (Anemarrhena asphodeloides), as the active ingredients, were investigated in experimental animals administering orally and in vitro test system. ADP had no influences on general behavior, pentobarbital sleeping time, spontaneous motor activity, motor coordination of mice, normal body temperature, chemoshock produced by pentylenetetrazole and writhing syndromes induced by 0.8% acetic acid at the dose of 150 and 1500 mg/kg. Gastric secretion of rats and intestinal motility of mice were not also influenced by the administration of ADP at doses of 150 and 1500 mg/kg, with the exception of the significant decrease of free HCI concentration at a dose of 1500 mg/kg in rats. ADP (150 and 1500 mg/kg) did not alter mean arterial blood pressure and heart rate in conscious rats. ADP given to anesthetized rats showed no effect on respiratory rate at the same doses. In in vitro experiments, ADP at the concentration of 150 mg/L did not show direct effect and inhibitory or augmentative action on histamine- or acetylcholine-induced contractions in the isolated ileum of guinea-pig. Taken together, these results indicate that ADP does not induce any adverse effects in experimental animals.

• 한국전기전자재료학회:학술대회논문집
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• 한국전기전자재료학회 2006년도 추계학술대회 논문집 Vol.19
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• pp.328-329
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• 2006

반도체 소자의 소형화, 고질적화는 junction 깊이 감소와 도핑농도의 증가를 요구한다. 현재 상용화되는 도핑법은 이온빔 주입(Ion Beam Ion Implantation, IBII)인데, 이 방법은 낮은 가속에너지를 가하는 경우 이온빔의 정류가 금속이 감소해 주입 속도가 낮아져 대랑 생산이 어렵고 장비가 고가라는 단점이 있다. 하지만 플라즈마를 이용한 이온주입법 (Plasma Source Ion Implantation, PSII)은 공정 속도가 빠르고 제조비용이 매우 저렴해 새로운 이온주입법으로 주목받고 있다. PSII법에서 플라즈마 특성은 그 결과에 큰 영향을 미치므로 플라즈마 특성의 적절한 제어가 필수적으로 요구된다. 본 연구에서는 공정압력과 RF power를 변화시키며 플라즈마 밀도 측정했다. 그 결과 공정압력이 증가함에 따라서 플라즈마 밀도는 감소되었고 RF power 증가함에 따라서 플라즈마 밀도는 증가되었다.

• 생명과학회지
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• 제8권5호
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• pp.486-491
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• 1998

mouse의 임파구로부터 두 종류의 ADP-ribosyltransferase (Yac-1과 Yac-2)가 클로닝되어 특성을 규명한 바 있다. Yac-2는 ADP-ribosyltransferase 활성 뿐 아니라 높은 NAD glycohydrolase 활성도 가지고 있다. Yac-2는 두 보존된 glutamic acids 사이인 221번 위치에 arginine를 소유하고 있다. 두 효소 활성에 대한 Arg-221의 중요성을 조사하기 위해 Arg-221이 Glutamic acid (R221E)와 Alanine (R221A)으로 돌연변이 되었다. 돌연변이체인 R221E와 R221A는 두 효소에 대해 야생형과 유사한 활성을 나타내었으며 이러한 결과는 Yac-2의 Arg-221이 ADP-ribosyltransferase와 NAD glycohydrolase의 활성에 필수적인 역할을 하지 않음을 시사해준다.

• 한국응용과학기술학회지
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• 제24권4호
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• pp.362-368
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• 2007

To study the relationship between elementary biochemical states and structural states of the actomyosin crossbridges in muscle, the effects of binding of MgADP to myosin heads in the rigor muscle were examined by X-ray diffraction using synchrotron radiation. X-ray diffraction studies have been made to investigate the effects of binding of ADP on the structure of glycerinated rabbit skeletal muscle in the rigor state. The intensity increase was accompanied by a slight but distinct decrease in the 5.9 am layer-line intensity close to the meridian. These results strongly suggest that myosin heads altered their attached conformation in the proximal end toward the plane perpendicular to the fiber axis when MgADP was bound to them. We found that the intensity of the 14.5 nm-based meridional reflections increase by 20-50% when MgADP was added to the rigor muscle in the presence of hexokinase and myokinase inhibitor.