• Tuberculosis and Respiratory Diseases
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• 제41권5호
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• pp.489-493
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• 1994

연구배경: NAD glycohydrolase(NADase)는 세포 표면에 위치하며 glycosylphatidylinositol(GPI)로 세포표면에 부착되어 있으며 bacterial PI-specific phospholipase C(PI-PLC)에 의해 분리된다. 최근 결핵환자에서 NADase가 증가한다는 보고가 있었으나 결핵균자체가 NADase가 높기 때문에 절대적인 NADase치가 증가했는 지는 확실치 않다. 따라서 저자들은 정상 대조군과 결핵환자의 적혈구에서 순수한 NADase activity를 측정하였다. 방법: 19명의 정상 건강 대조군과 16명의 과거 결핵의 진단 및 치료를 받지 않은 결핵환자를 대상으로하여 NADase activity를 측정하였고 결핵환자는 결핵치료 3개월후 재 검사하였다. NADase activity는 [carbonyl-$^3H$] nicotinamide 동위원소를 사용하여 측정하였다. 결과: 건강 대조군에서 $2031{\pm}824.0pmol/min/10^6$ erythrocytes, 결핵 감염군에서 $3339{\pm}1568.0$, 그리고 isoniazide와 rifampin으로 치료한 3개월 후 $2238.6{\pm}1013.1$을 얻어 결핵 감염시 NADase activity가 유의한 차이를 가지고 증가하며(p<0.05), 치료전에 비하여 치료후 유의있게 감소하였다. 결론: 결핵감염시 NADase activity가 올라가고 결핵 치료시 NADase activity가 정상화 되어 NADase activity가 결핵감염의 진단 및 치료에 대한 새로운 지표가 될수 있을 것으로 사료된다.

• 한국임상약학회지
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• 제8권1호
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• pp.29-34
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• 1998

Murine CD38 is a 42 kDa type II glycoprotein expressed on cell surface of both B and T lymphocytes. CD38 is a multifunctional enzyme that catalyzes the formation and hydrolysis of cyclic adenosine diphosphoribose (cADPR): ADP-ribosyl cyclase activity of CD38 catalyzes the formation of cADPR from NAD and cADPR hydrolase activity of CD38 catalyzes the hydrolysis of cADPR to ADP-ribose (ADPR). And also, CD38 has the catalytic activity of NAD glycohydrolase (NADase) which catalyzes the hydrolysis of catalyzes the formation and hydrolysis of cyclic adenosine diphosphoribose (cADPR): ADP-ribosyl cyclase activity of CD38 catalyzes the formation of cADPR from NAD to ADPR. In this study, we attempted to purify CD38 from mouse lymphocytes by using the immobilized anti-CD38 monoclonal antibody. The single step immuno-affinity column chromatography resulted in homogeneous purification, showing a single protein of 42 kDa on a SDS polyacrylamide gel. We have investigated the effects of various inhibitors on the enzyme activities of the purified CD38. Cibacron blue (0.5 mM) inhibited all three enzyme activities of CD38, NADase, ADP-ribosyl cyclase and cADPR hydrolase activities. ADPR (2 mM) showed inhibitory effect on both cADPR hydrolase activity and NADase, but not on ADP-ribosyl cyclase activity. However, ATP (2 mM) inhibited only cADPR hydrolase activity. $Zn^{2+}$ (1 mM) showed similar inhibitory effect as that of ADPR, but activated cyclase activity These results suggest that CD38 has three different catalytic activity domains which might be differentially regulated by their specific inhibitors.

• Toxicological Research
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• 제17권
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• pp.329-333
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• 2001

Apoptosis is the normal physiological process of cell death essential for the maintenance of homeostasis. The function of nicotinamide adenine dinucleotide (NAD) and adenine diphosphate (ADP) ribosylation (transfer of ADP-ribose to proteins) reactions in modifying apoptosis have recently been of great interest. Recently. CD38. a type 2 transmembrane glycoprotein expressed in hematopoietic and non hematopoietic cell lines. has been reported to possess NAD glycohydrolase activity (Han. 1999) and PC-1 and CD38 NADase regulates T cells by inhibition of phosphodiesterase/pyrophosphatase activity of PC-1 by its association with glycosaminoglycan (Hozada et al., 1999). Sindhuphak et al. (2000) has reported that cervical cancer cells can be differentiated from normal cells by using FTIR (Fourier-Transformed Infrared) technique. which has characterized shifts to be due to the phosphodiester bond in nucleic acid. protein amide I&II. carbohydrate and glycogen bands. Mechanisms how phosphodiester bond shift in cervical cancer cells as compared to control cells remain to be elucidated. Suramana et al. (2000) as well as Lohitnavy and Sinhaseni (1998) have studied methomyl and colchicine effects in rat splenocytes. Lactate Dehydroge-nase Isozymes 3 (LDH3) and LDH4 were observed to increase transiently and subsided in plasma of rats exposed to 6~8 mg/kg methomyl after 48 hours. Phosphodiester bond shift of nucleic acid. detected by FTIR. was also reported (Suramana et al., 2000). We report here, after analysis of bond shift patterns. a similar bond shifts detected by FTIR spectrum observed in human cervical cells and splenocytes of rats exposed orally to 2~8 mg/kg methomyl as well as rats exposed to colchicine 2~6 mg/kg orally.