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황태준,이승배,권기록,Hwang, Tae-Jun,Lee, Seung-Bae,Gwon, Gi-Rok 대한약침학회 2001 Journal of pharmacopuncture Vol.4 No.2
This study was carried out for production of neutral antibody to bee venom $(anti-phospholipase\;A_2IgY)$. Hen layings were injected repeatedly with bee venom and phospholipase $A_2$ with Freund's adjuvant. Specific antibody in egg yolk from immunized hen laying was separated, and purified, also immunological characteristics of anti phospholipase $A_2\;IgY$ was invested. The results were summarized as follows: 1. Phospholipase $A_2$ was showed single band at molecular weight 17,000 in SDS-PAGE and bee venom was showed two band at molecular weight 17,000 and under molecular weight 6,500 in SDS-PAGE. 2. During 70 days after hen immunized with bee venom and phospholipase $A_2$, antibodies(anti-bee venom IgY) to bee venom were showed poor ELISA value in egg yolk, but antibodies$(anti-Phospholipase\;A_2IgY)$ to phospholipase $A_2$ in egg yolk were increased ELISA value from 8 days or 15 days and found maximum ELISA value at 42 days. Also after booster at 49 days, ELISA value of anti Phospholipase $A_2\;IgY$ in egg yolk was supported at optical density(O.D) 1.0 level, continuously. 3. Titer of phospholipase $A_2\;IgY$ was showed 1: 32,000. 4. In double immunodiffusion test to phospholipase $A_2$ after double dilution of anti-phospholipase $A_2\;IgY$, only precipitation line was made in 1:1 dilution well of anti-Phospholipase $A_2\;IgY$. But In immunodiffusion test to anti-phospholipase $A_2\;IgY$ after double dilution of phospholipase $A_2$, Precipitation line to 250ul/ml well of phospholipase $A_2$ was showed. In double immunodiffusion test to bee venom(1mg/ml) after double dilution anti-phospholipase $A_2\;IgY$, all well without 1:32 dilution well were showed strong precipitation line. 5. In dot bloting test to anti-phospholipase $A_2\;IgY$ after diluting bee venom(0.5mg/ml), dot bloting color was showed clearly to $1/100(5{\mu}g/ml)$ in bee venom.
99mTC 표지 향과립구단일클론항체를 이용한 골수신티그라피법의 개발
최창운(Chang Woon Choi),정준기(June Key Chung),이명철(Myung Chul Lee),김병국(Byung Kook Kim),고창순(Chang Soon Koh),정홍근(Hong Keun Chung) 대한내과학회 1994 대한내과학회지 Vol.46 No.1
Objectives: The purpose of the present study was to determine the immunologic characteristics of a home made anti-CEA monoclonal antibody (MAB) called CEA-79 which was considered to bind with the epitope of nonspecific cross-reacting antigen (NCA) in human granulocytes, and to evaluate the potential of 99mmTc- labeled CEA-79 as an immunoscintigraphic agent for bone marrow imaging. Methods: In order to evaluate the immunologic characteristics of this MAb, western blotting and immunohistochemical staining were performed. Periph eral blood smears of 6normals and bone marrow aspirates of 3normals, 12leukemic patients, and 1multiple myeloma patient were immunohistochemically stained by the alkaline phosphatase anti-alkaline phosphatase method. CEA-79 MAbs were labeled with 99mmTc by a transchelation method using β-mercaptoethanol as a reducing agent and glucarate as a chelator. With this 99mmTc-labeled CEA-79, scatchard analysis for affinity constant, immunoreactivity test and in vitro stability studies were performed. Formazan test was done for the evaluation of effect of CEA-79 to superoxide formation of granulocytes. Results: Western blotting of human granulocyte extracts with the MAb showed a single band at a site equivalent to a molecular weight of 95,000 daltons, suggesting that the binding was with an epitope of the NCA-95. Positive staining with CEA-79 antibody was shown in 93% of the peripheral granulocytes. Positively stained cells were derived from promyelocytes, myelocytes, metamyelocytes, band forms and segment forms. Erythroblasts of all maturation stages and normal lymphocytes were not stained. Leukemic blasts from patients with ALL, and Ml, M2, M5 subtypes of AML were also not stained. With a direct labeling method by transchelation of 99mmTc, the labeling efficiency of CEA-79 MAb with 99mmTc was 60 to 85%. Scatchard analysis of the MAb with granulocytes yielded an affinity constant of 1.10 to 4,75±10(10) 1/mol. Immunoreactivity was 60~65% which was similar to that of 131 I -labeled monoclonal antibodies prepared by the chloramine-T method(60%). The antibody was stable for 24 hours, with over 90% of the MAb remaining labeled at 24hours. And CEA-79 antibody did not change the granulocyte function of superoxide formation. Conclusion: It can be concluded that CEA-79 reacts specifically with an epitope of NCA-95 on human granulocytes and can be successfully labeled with 99mmTc by a direct labeling method. This indicates that 99mmTc-labeled CEA-79 MAb may be useful as an immunoscintigraphic agent for bone marrow imaging.
Lee Dong-Hwa,Jeon Hyun Jeong,Oh Tae Keun 대한의학회 2026 Journal of Korean medical science Vol.41 No.7
Background: The classification of early onset (< 30 years old) patients with diabetes mellitus (DM) as either type 1 diabetes (T1D) or type 2 diabetes (T2D) can be a challenge due to their similar overlapping phenotypes. In this study, we attempted to utilize various clinical and laboratory characteristics in combination with immunological factors in the blood to determine whether it would be possible to distinguish and more accurately characterize our patients as T2D. Methods: Electronic medical records were evaluated to obtain information categorized as either early onset patients with DM (n = 102) and patients with T1D (n = 89). Using the stored serum from these patients, autoantibodies of anti-insulinoma associated 2 (IA2), anti-zinc transporter 8 (ZnT8) and anti-glutamic acid decarboxylase antibody (GAD) were measured. Results: In the clinical characteristics, early onset patients with DM (n = 102) were younger (31.7 ± 7.0 years old, P < 0.01), more overweight (28.1 ± 5.5 kg/m2 , P < 0.05), shorter duration of diabetes (10.4 ± 7.3 years, P < 0.01) and a more prevalent family history of diabetes (81%, P < 0.01) than patients with T1D. The laboratory values from early onset patients with DM exhibited lower glycated hemoglobin A1c (8.0 ± 2.1%, P < 0.01) and glucose levels (165 ± 73 mg/dL, P < 0.01) with conversely higher C-peptide levels (2.2 ± 1.2 ng/mL, P < 0.01). Measurements of immunological factors, demonstrated that the prevalence of anti-ZnT8 (2%) and anti-GAD antibody (2%) in early onset patients with DM was significantly lower (P < 0.01) compared to patients with T1D (13% for anti-ZnT8 and 38% for anti-GAD). The prevalence of anti-IA2 was not significantly different between early onset patients with DM (13%) versus patients with T1D (11%). In the multivariate logistic regression analysis, C-peptide level (B, 4.453; standard error [SE], 0.844; Wald, 27.808; P < 0.001) was the strongest independent factor to distinguish early onset patients with DM as T2D. After adjusting C-peptide level, family history of diabetes (B, 0.830; SE, 0.420; Wald, 3.909; P = 0.048), body mass index (BMI) (B, 0.111; SE, 0.039; Wald, 8.167; P = 0.004) and the relative negative status of anti-GAD (B, −2.041; SE, 0.597; Wald, 11.670; P < 0.001) were determining factors in our analyses. Conclusion: In this study, our findings suggested that early onset patients with DM may be more accurately diagnosed as T2D if they have a compilation of elevated C-peptide levels, higher BMI, more prevalent history of familial diabetes and the absence of detecting antiGAD antibodies.
<i>In Situ</i> Nanoadjuvant-Assembled Tumor Vaccine for Preventing Long-Term Recurrence
Le, Quoc-Viet,Suh, Juhan,Choi, Jin Joo,Park, Gyu Thae,Lee, Jung Weon,Shim, Gayong,Oh, Yu-Kyoung American Chemical Society 2019 ACS NANO Vol.13 No.7
<P>Although immune checkpoint inhibitors have emerged as a breakthrough in cancer therapy, a monotherapy approach is not sufficient. Here, we report an immune checkpoint inhibitor-modified nanoparticle for an <I>in situ</I>-assembled tumor vaccine that can activate immune systems in the tumor microenvironment and prevent the long-term recurrence of tumors. Adjuvant-loaded nanoparticles were prepared by entrapping imiquimod (IQ) in photoresponsive polydopamine nanoparticles (IQ/PNs). The surfaces of IQ/PNs were then modified with anti-PDL1 antibody (PDL1Ab-IQ/PNs) for <I>in situ</I> assembly with inactivated tumor cells and immune checkpoint blocking of PDL1 (programmed cell death 1 ligand 1). The presence of anti-PDL1 antibodies on IQ/PNs increased the binding of nanoparticles to CT26 cancer cells overexpressing PDL1. Subsequent near-infrared (NIR) irradiation induced a greater photothermal anticancer effect against cells treated with PDL1Ab-IQ/PNs than cells treated with plain PNs or unmodified IQ/PNs. To mimic the tumor microenvironment, we cocultured bone marrow-derived dendritic cells with CT26 cells treated with various nanoparticle formulations and NIR irradiated. This coculture study revealed that NIR-inactivated, PDL1Ab-IQ/PN-bound CT26 cells induced maturation of dendritic cells to the greatest extent. Following a single intravenous administration of different nanoparticle formulations in CT26 tumor-bearing mice, PDL1Ab-IQ/PNs showed greater tumor tissue accumulation than unmodified nanoparticles. Subsequent NIR irradiation of mice treated with PDL1Ab-IQ/PNs resulted in tumor ablation. In addition to primary tumor ablation, PDL1Ab-IQ/PNs completely prevented the growth of a secondarily challenged CT26 tumor at a distant site, producing 100% survival for up to 150 days. A long-term protection study revealed that treatment with PDL1Ab-IQ/PNs followed by NIR irradiation inhibited the growth of distant, secondarily challenged CT26 tumors 150 days after the first tumor inoculation. Moreover, increased infiltration of T cells was observed in tumor tissues treated with PDL1Ab-IQ/PNs and NIR-irradiated, and T cells isolated from splenocytes of mice in which tumor recurrence was prevented showed active killing of CT26 cells. These results suggest that PDL1Ab-IQ/PNs in conjunction with NIR irradiation induce a potent, <I>in situ</I>-assembled, all-in-one tumor vaccine with adjuvant-containing nanoparticle-bound, inactivated tumor cells. Such <I>in situ</I> nanoadjuvant-assembled tumor vaccines can be further developed for long-term prevention of tumor recurrence without the need for chemotherapy.</P> [FIG OMISSION]</BR>
신생아에서 담석을 동반한 Anti-E 항체에 의한 동종 면역성 용혈성 질환 1례
이효진,홍승수,심윤희,김은령 대한신생아학회 2008 Neonatal medicine Vol.15 No.2
Cholelithiasis is rarely recognized in children, especially in infants. Hemolytic disorders, long-term total parenteral nutrition (TPN), congenital anomalies of the biliary tree leading to stasis of bile flow, congenital IgA-deficiency, furosemide treatment, and prolonged fasting have been reported as predisposing factors for cholelithiasis in childhood. Hemolytic disease of the newborn due to anti-E has rarely been reported as a risk factor for cholelithiasis. We report a case of gallbladder stones in a neonate associated with anti-E antibody hemolytic disease.
서정아,박용원,이종국,김상우,엄태현,신보문 인제대학교 1999 仁濟醫學 Vol.20 No.1
신생아 동종면역성 용혈성 질환은 임신중에 태반을 통해 산모로부터 태아로 불완전항체인 IgG가 전해져 신생아 적혈구와 결합하여 용혈시키는 질환으로 임상증상은 과빌리루빈혈증과 빈혈이 주된 소견이다. 저자들은 황달을 주소로 입원한 신생아에서 항-E 항체와 항-E 항체 및 항-c 항체에 의한 동종면역성 용혈성질환 5례 모두에서 교환수혈과 광선요법 등의 치료 후 증상의 호전을 경험하였기에 보고하는 바이다. Alloimmune hemolytic disease of newborn is a disease characterized by progressive neonatal hyperbilirubinemia and anemia which is caused by transplacental IgG alloantibody transmitted from the mother to the fetus. Authors have experienced four cases of alloimmune hemolytic disease due to anti-E and one case due to anti-E and anti-c, who were hospitalized due to jaundice. All five cases were treated with exchange transfusion and phototherapy, so jaundice was improved in all cases.
Cho, Hongsik,Kim, Byoung Ju,Park, Sang-Hyug,Hasty, Karen A,Min, Byoung-Hyun Dove Medical Press 2018 INTERNATIONAL JOURNAL OF NANOMEDICINE Vol.13 No.-
<P><B>Background</B></P><P>Early stage osteoarthritis (OA) is clinically asymptomatic due to the avascular and the aneural nature of the cartilage tissue. Nevertheless, early detection of cartilage tissue is critical in order to impede the progression of OA. Hence, in order to develop effective preventive therapy for OA, diagnosis in the early stages is necessary.</P><P><B>Methods</B></P><P>To achieve this goal, we have developed targeted, fluorescent nanosomes conjugated with monoclonal anti-type II collagen antibodies (MabCII) for diagnosis of early OA. The MabCII-coated nanosomes (targeted-nanosomes) bind to the damaged cartilage explants in vitro and in vivo in an OA mouse model that mimics early stage OA. The OA mouse model was induced by destabilization of the medial meniscus (DMM) in 9–10 weeks old C57Bl/6 mice.</P><P><B>Results</B></P><P>The targeted-nanosomes enhanced the binding specificity to the cartilage tissue according to the severity of damage.</P><P><B>Conclusion</B></P><P>We show that MabCII-nanosomes can precisely detect early stage OA in the DMM mouse model. Thus, MabCII-nanosomes have the potential to be used as a non-invasive method for diagnosing the early osteoarthritic lesions.</P>
Hai-Nan Lan,Hai-Long Jiang,Wei Li,Tian-Cheng Wu,Pan Hong,Yu Meng Li,Hui Zhang,Huan-Zhong Cui,Xin Zheng 아세아·태평양축산학회 2015 Animal Bioscience Vol.28 No.4
B-32 is one of a panel of monoclonal anti-idiotypic antibodies to growth hormone (GH) that we developed. To characterize and identify its potential role as a novel growth hormone receptor (GHR) agonist, we determined that B-32 behaved as a typical Ab2β based on a series of enzyme-linked immunosorbent assay assays. The results of fluorescence-activated cell sorting, indirect immunofluorescence and competitive receptor binding assays demonstrated that B-32 specifically binds to the GHR expressed on target cells. Next, we examined the resulting signal transduction pathways triggered by this antibody in primary porcine hepatocytes. We found that B-32 can activate the GHR and Janus kinase (2)/signal transducers and activators of transcription (JAK2/STAT5) signalling pathways. The phosphorylation kinetics of JAK2/STAT5 induced by either GH or B-32 were analysed in dose-response and time course experiments. In addition, B32 could also stimulate porcine hepatocytes to secrete insulin-like growth factors-1. Our work indicates that a monoclonal anti-idiotypic antibody to GH (B-32) can serve as a GHR agonist or GH mimic and has application potential in domestic animal (pig) production.