• Korean Journal of Veterinary Research
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• v.56 no.1
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• pp.47-49
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• 2016

An 11-year-old, spayed female poodle presented with fever and shifting lameness. Physical examination revealed hyperthermia ($40.6^{\circ}C$), and proteinuria was detected upon urinalysis. Increased neutrophils (83%) and decreased viscosity were revealed upon synovial fluid analysis. Serum antinuclear antibody was positive at 1 : 80. Based on these findings, the dog was diagnosed with systemic lupus erythematosus. Immunosuppressive therapy was initiated with prednisolone and cyclosporine, and the condition was markedly improved after the treatments. This case report describes the clinical and laboratory findings, imaging characteristics and successful outcomes after prednisolone plus cyclosporine therapy in a canine systemic lupus erythematosus case.

• Journal of Digestive Cancer Research
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• v.6 no.2
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• pp.45-49
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• 2018

Colorectal cancer (CRC) is the third most common cause of cancer-related death in the world. Although the long-term outcome of patients with metastatic CRC is still poor, target therapy including anti EGFR agents and anti VEGF agents and immunotherapy including anti PD-1 antibody and anti CTLA-4 antibody have shown clinical benefits in the treatment of patient with metastatic CRC. In the future, the personalized treatment strategy based on the clinical characteristics and biologic features of patients with metastatic CRC will be necessary. In this review, we summarized the mechanisms and clinical evidences of target therapy and immunotherapy, and the guideline of clinical practice in patients with metastatic CRC.

• IMMUNE NETWORK
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• v.4 no.1
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• pp.16-22
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• 2004

Background: To develop a novel treatment strategy for hepatitis B virus infection, a major cause of liver chirosis and cancer, we aimed to make human monoclonal antibodies inhibiting RNase H activity of P protein playing in important role in HBV replication. In this regard, phage display technology was employed and demonstrated as an efficient cloning method for human monoclonal antibody. So this study analysed the usability of human monoclonal antibody as protein based gene therapy. Methods: RNase H of HBV was expressed as fusion protein with maltose binding protein and purified with amylose resin column. Single chain Fv (scFv) phage antibody library was constructed by PCR cloning using total RNAs of PBMC from 50 healthy volunteers. Binders to RNase H were selected with BIAcore 2000 from the constructed library, and purified as soluble antibody fragment. The affinity and sequences of selected antibody fragments were analyzed with BIAcore and ABI automatic sequencer, respectively. And finally RNase H activity inhibiting assay was carried out. Results: Recombinant RNase H expressed in E. coli exhibited an proper enzyme activity. Naive library of $4.46{\times}10^9cfu$ was screened by BIAcore 2000. Two clones, RN41 and RN56, showed affinity of $4.5{\times}10^{-7}M$ and $1.9{\times}10^{-7}M$, respectively. But RNase H inhibiting activity of RN41 was higher than that of RN56. Conclusion: We cloned human monoclonal antibodies inhibiting RNase H activity of P protein of HBV. These antibodies can be expected to be a good candidate for protein-based antiviral therapy by preventing a replication of HBV if they can be expressed intracellularly in HBV-infected hepatocytes.

• Molecules and Cells
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• v.27 no.3
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• pp.313-319
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• 2009

The dual-vector system-II (DVS-II), which allows efficient display of Fab antibodies on phage, has been reported previously, but its practical applicability in a phage-displayed antibody library has not been verified. To resolve this issue, we created two small combinatorial human Fab antibody libraries using the DVS-II, and isolation of target-specific antibodies was attempted. Biopanning of one antibody library, termed DVFAB-1L library, which has a $1.3{\times}10^7$ combinatorial antibody complexity, against fluorescein-BSA resulted in successful isolation of human Fab clones specific for the antigen despite the presence of only a single light chain in the library. By using the unique feature of the DVS-II, an antibody library of a larger size, named DVFAB-131L, which has a $1.5{\times}10^9$ combinatorial antibody complexity, was also generated in a rapid manner by combining $1.3{\times}10^7$ heavy chains and 131 light chains and more diverse anti-fluorescein-BSA Fab antibody clones were successfully obtained. Our results demonstrate that the DVS-II can be applied readily in creating phage-displayed antibody libraries with much less effort, and target-specific antibody clones can be isolated reliably via light chain promiscuity of antibody molecules.

• Journal of Radiopharmaceuticals and Molecular Probes
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• v.5 no.1
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• pp.11-17
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• 2019

Recently, antibody-like scaffold proteins have received a great deal of interest in diagnosis and therapy applications because of their intrinsic features that are often required for tumor imaging and therapy. Intrinsic issues that are associated with therapeutic application of antibody-like scaffold proteins, particularly in cancer treatment, include an efficient and straightforward radiolabeling for understanding in vivo biodistribution and excretion route, and monitoring therapeutic responses. Herein, we report an efficient and straightforward method for radiolabeling of antibody-like scaffold proteins with the $[^{99m}Tc(OH_2)_3(CO)_3]^+$ ($^{99m}Tc$-tricarbonyl) by using a site-specific direct labeling method via hexahistidine-tag, which is a widely used for general purification of recombinant proteins with His-affinity chromatography. Repebody is a new class of antibody-like scaffold protein that consists of highly diverse leucine-rich repeat (LRR) modules. Although all possible biomedical applications with repebody are ongoing, it's in vivo biodistribution and excretion pathway has not yet been explored. In this study, hexahistidine ($His_6$)-tag bearing repebody (rEgH9) was labeled with [$^{99m}Tc$]-tricarbonyl. Repebody protein was radiolabeled with high radiolabeling efficiency (>90%) and radiolabeled compound was more than 99% pure after purification. These results clearly demonstrate that the present radiolabeling method will be useful molecular imaging study.

• Oncology Letters
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• v.42 no.6
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• pp.2686-2693
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• 2019

In recent years, efforts to treat cancer by improving the immune function of patients have received a great deal of attention. As part of the immune system, complement is also under such evaluation. Among the many components of the complement system, complement decay accelerating factor (CD55 or DAF) is known to inhibit complement-mediated cell lysis. However, little is known about the role of CD55 in terms of cancer therapy. The present study aimed to demonstrate that increased levels of CD55 are strongly correlated with the progression of colorectal cancer. A novel CD55 chimeric monoclonal antibody was developed that may boost the immune response, thereby suppressing cancer. The CD55 antibody treatment activated complement and therefore suppressed the proliferation, invasion and migration of colorectal cancer cells. This tumoricidal activity is partly explained by the inflammatory response via the activation of proinflammatory cytokines. In addition, the CD55 antibody treatment synergistically enhanced the tumoricidal activity of 5-FU in colorectal cancer cells, suggesting that combined treatment may be a better strategy in colorectal cancer therapy.

• Parasites, Hosts and Diseases
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• v.38 no.1
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• pp.29-31
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• 2000

A toxoplasmic uveitis case was reported on the focus of impairment of pathological findings and serological antibody titers after chemotherapy. A chief complaint of a 60-year-old male was a decreased and blurred vision in his right eye for 2 weeks after experiencing tremendous stress and fatigue. A steroid therapy for 3 weeks was not effective and the retinal lesion became necrotic. Anti-Toxoplasma gondii antibody titer was checked to be a strong positive by both ELISA and indirect latex agglutination assay (lLA). He was treated with Fansidar F for 8 weeks. His vision improved as the necrotic lesion healed by scarring, but the antibody titers still remained very high without any signs of negative conversion. It is suggested to be a recurrent case of the past asymptomatic infection by presumed immune suppression caused by excessive stress.

• BMB Reports
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• v.57 no.3
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• pp.155-160
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• 2024

Lung cancer carries one of the highest mortality rates among all cancers. It is often diagnosed at more advanced stages with limited treatment options compared to other malignancies. This study focuses on calnexin as a potential biomarker for diagnosis and treatment of lung cancer. Calnexin, a molecular chaperone integral to N-linked glycoprotein synthesis, has shown some associations with cancer. However, targeted therapeutic or diagnostic methods using calnexin have been proposed. Through 1D-LCMSMS, we identified calnexin as a biomarker for lung cancer and substantiated its expression in human lung cancer cell membranes using Western blotting, flow cytometry, and immunocytochemistry. Anti-calnexin antibodies exhibited complement-dependent cytotoxicity to lung cancer cell lines, resulting in a notable reduction in tumor growth in a subcutaneous xenograft model. Additionally, we verified the feasibility of labeling tumors through in vivo imaging using antibodies against calnexin. Furthermore, exosomal detection of calnexin suggested the potential utility of liquid biopsy for diagnostic purposes. In conclusion, this study establishes calnexin as a promising target for antibody-based lung cancer diagnosis and therapy, unlocking novel avenues for early detection and treatment.

• Proceedings of the Korean Society of Toxicology Conference
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• 2003.10b
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• pp.89-90
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• 2003

Biological products are composed of vaccines, antitoxin, blood products, DNA recombinant protein drugs, monoclonal antibody, cell therapy and gene therapy. Biological products are divided into traditional (i.e. recombinant proteins and monoclonal antibodies) and novel biological products (gene and cell therapy) and will require a similar re-evaluation of the approaches taken during each development program.(omitted)

• BMB Reports
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• v.40 no.6
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• pp.875-880
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• 2007

Glucose oxidase (GOD) is an oxidoreductase catalyzing the reaction of glucose and oxygen to peroxide and gluconolacton (EC 1.1.3.4.). GOD is a widely used enzyme in biotechnology. Therefore the production of monoclonal antibodies and antibody fragments to GOD are of interest in bioanalytics and even tumor therapy. We describe here the generation of a panel of monoclonal antibodies to native and heat inactivated GOD. One of the hybridomas, E13BC8, was used for cloning of a single chain antibody(scFv). This scFv was expressed in Escherichia coli XL1-blue with the help of the vector system pOPE101. The scFv was isolated from the periplasmic fraction and detected by western blotting. It reacts specifically with soluble active GOD but does not recognize denatured GOD adsorbed to the solid phase. The same binding properties were also found for the monoclonal antibody E13BC8.